MXPA97006471A - Proof of multi-specific electroquimioluminiscence, of multip arrangements - Google Patents

Abstract

The present invention relates to materials and methods for producing multispecific, multi-arranged, electronically excited arrays for use in tests based on electrochemiluminescence. Materials and methods are provided for the chemical and / or physical control of conductive domains and reagent reservoir for use in deployments in flat panels and multispecific test procedures.

Description

PROOF OF MULTIPLEPECIFIC ELECTRONIC, MULTIPLE-PURPOSE ELECTROQUIMICOLUMINISCENCE This request is a continuation in part of copending application Serial No. 08 / 402,076 filed on March 10, 1995, and of copending application Serial No. 08 / 402,277, filed on March 10, 1995, which are hereby incorporated by reference in their entirety. 1. INTRODUCTION The present invention offers a multi-arrangement, multi-array (PMAMS) configured surface for tests based on the basic metabolic process, as well as methods for making and using PMAMS. 2. BACKGROUND OF THE INVENTION 2.1. DIAGNOSTIC TESTS There is a significant economic need for sensitive and rapid diagnostic technologies. Diagnostic technologies are important in a wide range of economic markets including the health sector, research, agriculture, the veterinary sector, and industry. An improvement in sensitivity, time required, ease of use, robustness or cost can open up entirely new diagnostic markets where previously no technology could meet the needs of the market. Certain diagnostic technologies may have a high sensitivity but are too expensive to meet the needs of the market. Other techniques may be economical but not robust enough for several markets. A novel diagnostic technique that can combine these qualities is a significant advance and an opportunity in the field of diagnostics. There are numerous different analytical techniques used in diagnostic applications. These techniques include radioactive labeling, enzyme-linked immunoassays, chemical calorimetric assays, fluorescent labeling, chemoluminescent labeling, and electrochemiluminescent labeling. Each of these techniques has a unique combination of levels of sensitivity, ease of use, robustness, speed and cost that define and limit its usefulness in different diagnostic markets. These differences are due in part to the physical limitations inherent in each technique. Radioactive marking, for example, presents a lack of robustness because the marking itself disintegrates and the removal of the resulting radioactive waste causes economic, safety and environmental costs for many applications. Many of the sensitive diagnostic techniques that are used today have market limitations essentially due to the need for specialized technicians to carry out the tests. The electrochemical procedures in use today, for example, require not only specialized technicians but repeated steps of washing and preparation. This increases both the costs and the need to get rid of waste. Innovative diagnostics that simplify test procedures as well as the reduction of cost per test will be very important and very useful for opening new markets as well as improving the performance of existing markets. 2.2 ELECTROCHI TESTING ICOLUMINISCENCE Electrochemlycoluminescence ("ECL") is the phenomenon by which an electrically excited species emits a photon (see, for example, Leland and Powell, 1990 J. Electroche. Soc. 137 (10) Í 3127-3131 ). Such species are called ECL markers and are also known here as MARKERS. ECL markers commonly employed include: organic compounds in which the metal is derived, for example, from the noble metals of rump VIII, including organometallic compounds containing Ru and Os such as the Ru (2, 2 '~ bipi ridine) portion ( + • ++) (also known as "Rubpy"), presented, for example, by Bard et al. (US Patent No. 5,238,808). The light generated by ECL markers can be used as a reporter in diagnostic procedures (Bard et al, US Patent No. 5, 221, 05). For example, an ECL tag can be covalently coupled to a binding agent such as a nucleic acid probe or antibody. The ECL labeling agent / binding agent can be used to test several substances (Bard et al., US Patent No. 5,238,808). The need for an electrical potential to excite the ECL marker for which I emit a photon is critical for ECL-based detection systems. An electrical potential waveform is applied to an ECL test solution. through an electrode surface, typically a metal surface, and a counter electrode (see, for example, U.S. Patent Nos. 5,068,088, 5,093,268, 5,061,445, 5,238,808, 5,147,806, 5,247,243, 5,296,191, 5,310,687, 5,221,605). Various apparatuses well known in the art are available for conducting and detecting ECL reactions. For example, Zhang et al. (U.S. Patent No. 5,324,457) presents exemplary electrodes for use in electrochemical cells for conducting ECL. Levantis et al. (U.S. Patent No. 5,093,268) presents electrochemical cells for use in ECL reactions. K.amin et al. (US Patent No. 5,147,806) presents apparatus for carrying out and detecting ECL reactions, including voltage control device. Zos i et al. (US Patent No. 5,061,445) presents an apparatus for carrying out and detecting ECL reactions, including electrical potential waveform diagrams to obtain ECL reactions, converters of digital elements into analog, control apparatus, detection apparatus, and methods for detecting the current generated by an ECL reaction at the working electrode to provide feedback information to the electronic control apparatus. The ECL technique is presented in detail, for example, in U.S. Patent No. 5,093,268. In summary, the ECL technique is a method to detect in a volume of a sample of an analyte of interest present in the sample in relatively small concentrations. The portion of ECL, called TAG (MARKER) in the aforementioned prior patents may or may not be linked to an analyte, but is in any way promoted in an excited state as a result of a series of chemical reactions triggered by the received electrical energy. from the working electrode. A molecule that promotes the ECL of the MARKER, is advantageously provided in the form of oxalate or, more preferably, tripropi sheet (see US Pat. No. 5,310,687). 2.3. ECL COMMERCIAL ESSAYS To date, all commercial ECL reactions are carried out on centimeter-sized electrode surfaces. The centimetric scale electrodes establish a balance between the increased magnitude of an ECL signal resulting from larger electrostatic and the desire to decrease the total sample volume needed for each test. However, even centimeter scale electrodes do not achieve the sensitivity required for many tests. In an attempt to overcome this problem, all commercial ECL systems additionally increase the sensitivity by using reverted magnetic beads to capture ECL or reactive apalitos. Then the beads san moved adjacent to a working electrode to increase the sensitivity. However, the use of magnetic beads presents numerous limitations. The accounts themselves are coated with proteins that break down and degrade over time, causing signal variations. Due to the complexity of the management and the form of the trials based on accounts, the commercial diagnosis of ECL requires a complex set preformed in series of procedures for each test carried out with a given sample which increases the time and cost to carry out the tests. The 5 micron face of the beads prevents most ECL MARKER attached to the beads from reaching the thin film adjacent to the working electrodes, which results in an ineffectiveness at the excitation level of the ECL MARKER. Leventis et al. (US Patent No. 5,093,268) has proposed a method to assay more than one analyte differently by using different ECL markers for each analyte, each emitting protons at different wavelengths for each different analyte in a single assay. However, this technique is limited, for example, by the lack of availability of a sufficient number of effective ECL markers that radiate at different wavelengths and the need to optimize the chemical conditions for each ECL marker. These practical limitations have prevented the commercialization of such multiple analyte ECL detection systems, at multiple wavelengths. Another approach to increase the sensitivity of ECL is to improve the technology of the electrodes. Zhang et al. (US Patent No. 5,324,457) have directly deposited ECL species films on various metallic or semiconducting surfaces. The Zhang and Bard technique employing bulk saturation of the electrode surface results (as described by the authors) in an uneven reservoir in the form of patches unsuitable for high sensitivity tests. The above methods for carrying out an ECL test also require that the test cell, including the electrodes, be purified by any of several methods, including the use of dilute acids, diluted bases, detergent solutions, etc., in accordance with the presented, for example in the North American Patent No. 5,147,806. Accordingly, it is an object of the present invention to provide a novel and economical assay for carrying out various ECL reactions, either sequentially or concurrently, and in a preferred embodiment, to provide integrated control standards to improve accuracy. . It is a further object of the present invention to provide a cassette comprising one or more carriers suitable for carrying out a plurality of ECL reactions either simultaneously or sequentially, said cassette being disposable. It is a further and related object of this invention to reduce the time and cost to carry out individual assays for analytes of interest in Islamic b samples. It is another additional and related object of the present invention to provide methods and apparatus for carrying out the plurality of simultaneous assays for a plurality of analytes of interest in a single biological sample. 3. COMPENDIUM OF THE INVENTION The present invention relates to a cassette for carrying out ECL reactions and ECL assays comprising a plurality of discrete binding domain immobilized on a support, the discrete linking domains are spatially aligned with one or several pairs of electrodes and one or more pairs of counter electrodes. The cassette preferably includes a first support having a plurality of discrete binding domains immobilized on the surface. It can have one or more electrode pairs and one or more pairs of counter electrodes. The electrode and counter-electrode pairs can be accessed separately by a source of electrical energy in the form of an effective waveform to trigger the electrochemi-luminescence effect. The cassette may also comprise a second support capable of being positioned adjacent to the first support to provide between them a device that contains the sample, and / or to serve as an electrode. The binding domains are configured on a support surface and are prepared in such a way that they bind the analytes or reagents of interest. The invention further relates to an apparatus for measuring the electrochemical inception of a sample, which provides a cassette handling device or support, a voltage control device adapted to apply an effective controlled voltage waveform to trigger the elec icalumirascencia, a photon detector device for detecting electrochemical luminescence from the sample and a device for manipulating the sample. The invention further relates to methods for using the cassettes for measuring the electrochemi-luminescence in a sample by contacting the plurality of binding domains of a cassette with a sample containing a plurality of analytes of interest, under test conditions of ECL, and then by applying an effective voltage waveform to trigger the electrochemlycoluminescence at each of the plurality of pairs of electrodes and counter electrodes and the detection or measurement of the electrochemical luminescence unchained. In a broad aspect, the invention provides ECL assay methods where the sample does not come into contact with an electrode. Additionally, as an alternative to the use of electrode and counter electrode pairs, the invention provides scanning of an electrode and counter electrode in the binding domains. The invention also provides a set of elements comprising components that include cassettes suitable for simultaneously measuring a plurality of electrochemiluminescence reactions, support surface and on which a plurality of domains, assay, means for carrying out the ECL assay are immobilized. which produces chemical reactions. The invention also offers electrodes prepared from graphite nanotubes. 4. DESCRIPTION OF THE FIGURES Figure 1 illustrates two supports forming a cassette according to the invention where a plurality of link domain 14 are present in a support 10 and a plurality of corresponding electrodes 16 is present in the support such that the approach of the supports will place a pair of electrodes adjacent to each link domain. Figure 1A illustrates two supports forming a cassette according to the present invention, where a plurality of link domain 14 are present in the support 10 and a plurality of corresponding electrodes 16 is present in the support 12 in such a way that the approach of the supports places a pair of electrodes adjacent to each link domain. Figure 2 illustrates two supports forming a cassette according to the present invention where a plurality of link domain 30 on the support 26 are adjacent to each of the individual electrodes 32 such that the approach of the supports 26 and 28 place each of the counter electrodes 38 adjacent to each of the link domains 30. 1 *? Figure 3 illustrates two cassette forming supports according to the present invention where a plurality of link domains 48 have adjacent pairs of electrodes-counter electrodes on a support 44. Support 46 can optionally be placed adjacent support 44 in such a way that the holder 46 provides a device containing sample adjacent to the link domains 48 and electrodes 50. Figure 4 illustrates two carriers forming a cassette according to the invention where a plurality of link domains 64 in the support 60 are in contact with a sample suspected of containing an ana lyte. The support 62 has regions 66 which contain reaction medium for detecting or t > either to measure an analyte of interest or to carry out a desired reaction in such a way that the support 60 and the approaching support 62 cause the linking domains 64 and the regions 66 to come in contact with each other. Figure 5A illustrates a top view of link domain configured for a multiple array, multi-stitch bond surface. Geometric shapes, triangles, squares and circles represent specific binding domains for different analytes. The binding domains can be hydrophobic or hydraumatic. The surrounding surface may have the opposite property (hydrachemical or hydrophobic) of the binding domains to minimize the expansion of the binding reagents or the analyte from the binding domains. Figure 5B illustrates a top view of a microfluidic guide for delivering binding reagents and / or analytes to discrete binding domains. Each point illustrates a cut of an icrofluid guide (for example, a capillary). FIG. 5C illustrates a side view of a microfluidic guide showing the approximation of aligned or corresponding microfluidic guides for delivering binding and / or analogous reagents to a plurality of configured binding domains. Each microfluidic guide can supply a different binding reagent to a discrete binding domain. Figure 6A illustrates the approximation of a multiple set of electrodes in correspondence with a surface that has symmetric or complex link domains of multiple sets configured. A removable electrode protection barrier is present between the electrode assembly and the link surface assembly. The complete assembly forms a cassette to carry out a plurality of ECL reactions. Figure 6B illustrates the approximation of a set of working electrodes and counter electrodes corresponding or aligned to which power can be supplied. The electrodes may have a form complementary to the binding domain or may have other forms (for example interd ig i such i zac ion). Figure 7 illustrates the side view of an approximate set of corresponding or aligned work electrodes and counter electrodes to which energy can be supplied and the complementary bond surface where conductive polymers are grown from the surface of the electrodes through the space between the set of electrodes and the binding domains in such a way that the potential field extends around the ECL marker of the sample to increase the efficiency of ECL reaction. Figure 8 illustrates the side view of an approximate array of corresponding or aligned work electrodes and counter electrodes and the interface surface complements the conductive particles scattered between the two components to extend the potential field. By extending the potential field around the ECL marker of the sample, the efficiency of the ECL reaction is increased. The conductive particles can be magnetic to allow easy handling. Figure 9 illustrates the side view of an approximate set of working electrode and corresponding or aligned cantra electrodes and the complementary bond surface where the electrodes have fine projections extending between the space between the electrode surface and the link domains to extend the potential field around an ECL marker in the sample, to increase the efficiency of the ECL reaction. Figure 10 illustrates the side view of an approximate set of corresponding or aligned work and counter electrodes and the complementary link surface where; the surfaces are not parallel, but they conform to each other in a complementary manner. The. Figure 11 illustrates the side view of a support having a metal layer on it to provide a unique assembly of its electrode and bonding surface in the form of a cassette. A set of self-adhesive monolayers "SAMs" is configured in the metallic layer. Figure 12 illustrates the side view of a support having a metal layer on it to provide a unique assembly of bond surface and electrode in the form of a cassette. A set of SAMs is configured in the metallic layer and conductive microparticles are scattered among the SAMs configured to extend the potential field around the ECL marker. of the sample, to increase the efficiency of the ECL reaction. Figure 13 illustrates the side view of a support having a metal layer on it to provide a unique assembly of bonding surfaces and electrodes in the form of a cassette. A set of self-assembled SAMs monolayers is configured in the metal layer and the growth of a conductive polymer and / or fiber from the ECL marker is illustrated to extend the potential field around the ECL marker of the sample to increase the efficiency of the ECL reaction. Figure 14 is a diagram of a support having a set of electrode pairs controlled by a computer. Figure 15 is a diagram of a support having a set of electrode pairs. Figure 16 is a diagram of a support having a set of electrode pairs and a computer system for controlling the power supply of each pair of electrodes. Figure 17 is a diagram of a support having an array of electrode pairs and a computing system with a plurality of voltage source and mul iplexers to control the power supply of each electrode pair. Figure 18 is a diagram of a support having a set of electrode pairs and a computer system with a plurality of switched voltage sources for controlling the power supply of each pair of elec- trodes. FIGS. 19 (a) - (e) are plan views of various alternative combinations of electrode pairs versus countermeasures. Figure 20 illustrates a support with a finished patterned test. Figure 21 illustrates two opposite surfaces of PMAMS on supports. Figure 22A illustrates a set of microfluidic guides (2201) and a fibril mat (2200). Figure 22B illustrates link domains (2202). Figure 23A illustrates an apparatus for forming a fibril mat by vacuum filtration. Figure 23B illustrates a fibril mat (2304) on a filter membrane (2303). Figure 24 illustrates the use of knees to produce fibril mats. Figure 25 shows a scheme of a multilayer fibril mat wherein the top layer has binding domains used for assays. Figure 26 shows a scheme of a fibril derived with portions that increase the non-specific binding, and several species, both biological and non-biological, are bonded on the surface. Figure 27 shows a scheme of a fibril derived with portions that increase the non-specific binding and several species linked to a fibril derived with some species additionally linked to ligands. Figure 28 illustrates several species covalently fixed on a fibril and some species are additionally linked to additional entities. Figure 29 illustrates the use of a multi-layer fibril mat as an optical filter which, depending on the position of a light source on the mat or on said mat, can allow the passage of light and / or absorb and / or absorb it. scatter light. Figure 30A illustrates cyclic voltammograms from electrochemical electrode measurements of carbon fibril mats. Figure 30B illustrates cyclic cytograms from electrochemical measurements on gold foil electrodes. Figure 31 compares an electrochemical property of fibril mats as a function of the thickness of the mat and the scanning speed. Figure 32 shows a graph illustrating that the non-specific binding in fibrils is generally raised as the concentration of fibrils in a protein solution rises.

Figure 33 demonstrates that the use of surfactants can reduce the non-specific binding between MARCAD0R1 tagged protein from ECL and carbon fibrils. Figure 34 shows a schematic of a top view of an experimental cell used to measure the electrochemical and ECL properties in a fibril mat electrode. Figure 35 shows an ECL signal obtained using a fibril mat and an electrode and 1000 pM MARCAD0R1 r (solid line) in solution a signal from a test regulator (without MARKER1) (broken line). Figure 36 shows a schematic of two surface devices of PMAMS, where two sets of supported electrodes are separated by a configured dielectric layer. Figure 37 illustrates an apparatus with a plurality of link domain (3702) in one support and one electrode and counter electrode in another support. Figure 38 shows a cassette where link domains are present on the surfaces of different objects supported on the counter electrode. Figure 39 shows a gel in contact with a working electrode and a counter-electrode. Figure 40 shows a graph of intensity of ECL and a cyclic voltammogram from a gel marked for ECL in contact with a working electrode and a contact with the ctrode. Figure 41 shows a graph of ECL intensity and a cyclic voltamagram from an unlabeled gel for ECL in contact with a working electrode and a counter electrode. Figure 42 shows a schematic for a bisuperfusion cassette used for ECL. Figure 43 demonstrates that fibril mats can be used co ct electrodes for MARCAD0R1 ECL of antibody adsorbed on the mats. Figure 44A shows the ECL intensity of a protein marked with MARCAD0R1 immobilized on an electrode. Figure 44B shows the vol cyclic vol of a coated electrode. Figure 45A shows a nearly reversible repetitive generation of ECL signal from a protein marked with MARCAD0R1 for ECL. Figure 45B shows the cyclic voltammogram of a coated electrode indicating partial preservation of the coating. Figure 46A shows the irreversible signal generation of ECL from a protein marked with MARCAD0R1 for inlaid ECL. Figure 46B shows the cyclic voltammogram of a coated electrode indicating substantial loss of the revetment. Fig. 47 shows an apparatus for multi-array ECL and a microprocessor containing a controller device for generating and analyzing ECL signals. 5. DETAILED DESCRIPTION OF THE INVENTION Accordingly, the present invention includes in general terms cassettes for carrying out a plurality of electrochemistry and miniscence assays. The cassettes are formed of supports having a plurality of binding domain capable of specifically binding to one or more analytes of interest. Link domains are prepared as multi-fix, multi-array, (PMAMS) configured surfaces on the support. The PMAMS offer a significant improvement compared to a previously known ECL assay method by, for example, a significant increase in the density of the assays that can be carried out and allowing a plurality of different assays that can be carried out rapidly or simul directly. The cassette may include a plurality of electrodes capable of selectively triggering light emission for ECL from labeled ECL labeled reagents over the binding domains. Figure 47 shows a multi-array ECL apparatus having electrodes 4700, 4704, a 4702 matrix with link domains 4706, and a microprocessor containing a controlling device 4720 for generating and analyzing an ECL signal connected by means of conductors 4710 -4716. In the embodiment of the invention presented in Figure 1, a cassette comprises supports 10, 12 where a plurality of link domain 14 are present on a surface of a first support 10 and a plurality of pairs 16 of electrodes / counter electrodes are present. find presentí? on a second support surface 12. The link domains and the electrode / counter electrode pairs are aligned such that each pair of the various electrode / counter electrode pairs 16 is adjacent to a link domain different from the domain plurality. of link 14 when the first support 10 and the second support 12 come together. The first support 10 that lies below the binding domains 14 is preferably a PMAMS with a ring film surface and transparent binding domains. The second support 12 is preferably a transparent flat plastic sheet having pairs 16 of transparent electrodes / counter electrodes there. The binding domains 14 are preferably prepared by micro-stamping a configuration of self-assembled organic monolayers (composed of individual monomers) on the support surface, where the monomer has a binding moiety or biotin. Avidin or steptavidin are then linked to the exposed biotin (see, for example, U.S. Patent No. 5,093,268). Binding reagents are then applied by applying a discrete amount of a suitable biotin-labeled binding reagent such as for example biatin-labeled antibody, which can be selectively linked to the analyte of interest at the locations on the support surface where it is bound. has stamped the monolayer. Figure 1A illustrates a system comprising a cassette (Figure 1) contained in a frame (11). In certain embodiments of the invention, it is desirable to reproducibly immobilize a specific or predetermined amount of one or more reagents on a surface. Immobilization applies in general terms to any method by which a reagent is fixed on a surface, including but not limited to covalent chemical bonds; non-specific adsorption; drying a reagent on a surface; electrostatic interactions; hydrophobic and / or hydrophilic interactions; combination or drag in liquids or gels; biospecific linkage, (eg ligand / receptor interactions to good oligonucleotide hybridization); metal links; q? elation, and / or entanglement in polymers.

The amount of reagent immobilized on a surface can be predetermined in several ways. For example, the amount of reagent on a surface can be specified by one or more elements of volume and / or area in which the reagent is present. It can also be specified by the number of individual molecules of a reagent that are immobilized on a surface. The amount of reagent can be specified in terms of the density of a particular reagent in a given region. The amount of reagent can be specified as a percentage of a surface carrying a particular reagent, either in terms of the total area of the surface, or in relation to the amounts of other reagents present on the surface. The amount of reagent can also be defined as the amount of reagent that must be present on a particular surface to provide a sufficient intensity of ECL for the assay to achieve a desired specificity. In a specific example, an area of 1 cm2 of gold surface may be coated with a monolayer of alcandiales. Reagents can also be immobilized in a re-transposable manner on reverted surfaces. The coating can serve to implement the immobilization of some reagents and / or reduce or prevent the immobilization of other reagents. The surface may be fully coated or the surface may be partially coated (i.e., a configured backing). The coating may be uniform in its composition, or may contain elements of different composition. In a specific example, the coating can be a configured monolayer film that immobilizes the immunoglobulin G by covalent chemical bonds in some areas, and prevents its immobilization in others. The coating can also serve to predetermine the amount (s) of one or more reagents immobilized on the surface in subsequent steps or in subsequent processes. In addition, the amount of a particular reagent can be controlled by limiting the amount of reagent deposited. Having a surface having reagents (or a coating) immobilized in a quantitative way, repraducible provides the ability to reproducibly and quantitatively measure an ECL signal from a sample, thus allowing its calibration. Preferably, pairs of electrodes / counter electrodes 16 are less than one centimeter in size and are fabricated together with electrode connections 20 (eg, of a transparent metal film) by well-known methods for the manufacture of liquid crystal displays and electrochronic presentation panels. The electrode conductors 20 are connected by means of electrical connections 19 to a waveform generating device 18. Advantageously, the electrode / counter-electrode pairs are handled individually with computerized control in such a way that the electrical potential is applied selectively to discrete binding domains. A light detector device 22 and a digital computer device 24 are provided for recording and analyzing the results when the ECL emissions have been stimulated from a suitable marker found in a binding domain. Figure IA illustrates a system comprising a cassette, electrical conductors, waveform generator, light detection device and digitized computer in accordance with that described in figure 1, contained in the frame 11. The cassette is inserted into the frame through an opening (15). In another embodiment, a working electrode is used to simultaneously generate an ECL signal in a plurality of link domain. In this mode, the ECL signal from each link domain is identified through the use of a light image device. In general terms, assays performed using cassettes in accordance with the present invention are assays that benefit from the use of several discrete binding domains. For example, the use of such cassettes allows a rapid and / or concurrent detection or measurement of a wide variety of analytes of interest. In a preferred embodiment, the assays in accordance with the present invention are also assays that benefit from the use of a labeled reagent, analyte or linkage surface for ECL. An ECL assay according to the present invention comprises contacting a plurality of binding domain with a sample suspected of containing an analyte of interest and triggering an ECL emission from a marker of bound ECL, where the ECL marker is found in the analyte either a competitor of the analyte, in a reagent that binds to the analyte or in the plurality of binding domain. The invention also provides test methods for ECL to detect or measure an analyte of interest, comprising (a) contacting one or more of a plurality of discrete binding domains, said plurality of binding domains being immobilized in a The surface of one or more supports, wherein said contacting is carried out with a sample containing molecules linked to a luminescent electrochemical marker, where said sample does not come into contact with any electrode or counter electrodes during said contacting step.; (b) approaching an electrode to said link domain or said link domains of a plurality of link domains; (c) the application of an effective voltage waveform to trigger ECL in said link domain or in said link domains of a plurality of link domains; and the detection or measurement of ECL. In another embodiment, the present invention offers ECL assay methods for (a) contacting one or more binding domains of a plurality of discrete binding domains, said plurality of link domains (i) being immobilized in a surface of one or more supports, and (ii) is spatially aligned with and in close proximity to a plurality of pairs of electrodes and counter electrodes, wherein said contacting is performed with a sample containing molecules linked to a luminescent electrochemical marker; (b) approaching an electrode and counter electrode to said link domain or said link domains of a plurality of link domains; (c) the application of an effective voltage waveform to trigger electrochemi-luminescence in said link domain or said link domains of a plurality of link domains; and (d) the detection or measurement of electrochemi-luminescence. The plurality of binding domain in the support can interact with samples to be tested. The PMAMS may also come into contact with solutions containing reagents necessary to complete an assay. The bonding surface then comes into contact (for example by pressing) with a surface of a complementary electrode (preferably a clean or virgin electrode) which is then used to apply an electrical potential to stimulate ECL. In a preferred method to carry out an assay using the apparatus of Figure 1, a sample of which is suspected to contain an analyte of interest is applied to several binding domains 14 together with reagents labeled for ECL suitable for detection in analyte. . The support 11 and the support 12 are then joined in such a manner that each of the link domains 14 is located between the electrode and the counter electrode in a different pair of several pairs 16 of electrodes / counter electrodes and the sample is between them. It should be noted that the electrode and cantraelectrode pair n makes mechanical contact with the link domain to stimulate the ECL when an appropriate potential is applied between the electrode and counter electrode pair. A suitable electric potential waveform for triggering an ECL emission is applied by means of electrical connection 19 from a waveform generating device 18 to various electro / counter electrode pairs 16. Any signal emitted by an ECL marker present in several link domains 14 is detected by a light detection device 22 and recorded and analyzed by a digital computing device 24. The invention provides a method for detecting in a volume of? Na Liquid sample, of multiple components, a plurality of analytes of interest that may be present in the sample in various concentrations. In general terms, a plurality of analytes can be detected from a sample of multiple components at molar concentrations less than 1/1000. Preferably, a plurality of analytes can be detected in molar concentrations less than 1 / 1,000,000,000,000 from a multiple component sample. The invention offers detection from a multiple component sample that can be carried out as heterogeneous assays, ie assays in which several unbound labeled reagents are separated from several labeled reagents bound prior to the exposure of the reagents labels bound to electrochemical energy, and homogeneous assays, that is, assays in which a plurality of labeled unbound reagents and linked labeled reagents are exposed to electrochemical energy together. In the assays of the present invention, the electromagnetic radiation used to detect a particular analyte can be distinguished from the electromagnetic radiation corresponding to other analytes by identifying its. position and / or location as one or several characteristics of a pattern, said pattern corresponds to the pattern of the link domains in the PMAMS. In the homogeneous assays of the present invention, the electromagnetic radiation emitted by the labeled reagents linked either as an increase or a decrease in the amount of electromagnetic radiation emitted by the linked labeled reagents as compared to the unlabeled reagents, or by detecting the electromagnetic radiation emitted from sources that correspond in space to one or more characteristics of a pattern that corresponds to the pattern of the binding domains in the PMAMS. In a specific example of the method of the invention presented in Figure 20, a sandwich assay is carried out on a support (5) with a plurality of binding domain (BD) on its surface that are specific for binding to an analyte. particular (An). When a sample of which is suspected to contain the analyte is applied to the binding domains, the analyte is bound over the binding domains. Antibodies (Ab), which are suitable to bind selectively with the anal ito (An) and which have been marked with a portion for ECL (MARKER) to form Ab-MARKER, are then applied to the analyte in the binding domains. After the removal of the excess Ab-MARKER from the binding domains, an appropriate potential waveform is triggered on the MARKER by means of electrodes (na illustrated) to trigger the electrochemical luminescence to trigger an ECL emission from any MARKER in the link domains. The ECL signal is detected by a d &amp device; light detection and recorded by digital computer devices (for example, according to what is illustrated in 22 and 24 in Figure 1). Next, modalities, characteristics and additional variations of the invention will be described. 5.1. PREPARATION OF A LINK SURFACE In order to better understand the invention, a detailed description of the preparation of the binding domains in a support is provided. A configured set of binding domains on a surface that are specific for a plurality of analytes is known here as a surface configured from one of multiple array or PMAMS specifics. PMAMS are prepared on a support, for example, by the configuration of self-assembled monolayers ("SAMs") (Ferguson et al., 1993, Macromslecules 26 (22) ¡5870-5875; Prime et al., 1991, Science 252 : 1164-1167; Laibinis et al., 1989, Science 245: 845-847; Umar et al., 1984, Langmuir 10 (5): 1498-1511; B in et al., 1989, Angew. Chem. 101: 522-528). Methods of surface configuration also include the use of physical etching (eg, micromachining) (Abbott et al., 1992, Science 257: 1380-1382, Abbott, 1994, Chem. Mater. 6 (5): 596-602). , microl i tography (Laibinis et al., 1989, Science 245: 845-847), fixation of chemical groups on the surface by the use of photoactive volatiles (Sundberg et al., 1995, J. Am. Chem Soc. 117 (49): 12050-12057), and microstamping techniques (Ku ar et al., 1994, Langmuir 10 (5): 1498-1511; Kumar et al., 1993, Appl. Phys. Lett. (14): 2002-2004). Surface configuration include methods for the spatially controlled delivery of fluid or particles (eg, microtest deposit (e.g., using an icrofluid guide to supply a surface using XY translation)), microcapillary fill (Kim et al., 1995, Nature 376: 581), inkjet technology, or syringe suppliers. Combinations of these techniques can also be used to provide complete surface patterns. In Figure 5A, a support 600 with independent link domains is shown so that they are depicted, simply for purposes of illustration, as geometric shapes 602 to indicate that different binding specificities may be present on a single support. The surface 604 between the binding domains may alternatively be hydrophobic or hydrophilic to limit the deposit of binding reagent to form binding domains. Linking domains and / or the surface (s) between the link domains may alternatively tend to non-specific binding or be resistant to non-specific binding, and / or may tend to bind binding reagents or Resist the binding of binding reagents by means of cavaliant or non-covalent interactions. In the case in which the non-specific binding through hydrophobic interactions is not the desired method for fixing binding chemistries on the surface, detergent can be added to avoid the occurrence of incidental non-specific binding. The binding domains are, in general terms, 0.1 μm to 1 mm in width or diameter or wider dimension according to the geometry of the domain. The surfaces are selectively derivatized to have specific link components exposed for example to the ECL assay solution. Additionally, nonspecific interactions in the binding domains decrease while maintaining a specific binding moiety by incorporating portions such as polyethylene glycols on the exposed surface of the discrete binding domains (Prime et al., 1993, J. Chem. Soc. 115: 10714-10721; Prime et al., 1991, Science 252: 1164-1167; Pale-Grasdemange et al., 1991, J. Am. Chem. Ssc. 113: 12-20). PMAMS can contain approximately 2 to 200 million link domains. Preferably, the number of link domains is from 50 to 500. In other embodiments, the number of link domains is from 25 to 100. The support may be several materials including, but not limited to, glass, plastic, ceramic, polymeric materials, mate > elastomeric materials, metals, alloys, composite sheets, semiconductors, insulators, silicon and / or layered materials, etc. Derived elastameric supports can be prepared, for example, as described by Ferguson et al., 1993, Macromolecules (Macromolecules) 26: 5870-5875; Ferguson et al., 1991, Science 253: 776-778; Chaudhury et al., 1992, Science 255: 1230-1232. The surface of the support in which the PMAMS is prepared can contain various materials, for example, meshes, filters, fiber materials, gels, solids (for example formed of metals), elastomers, etc. The support surface may have various structural, chemical and / or optical properties. For example, the surface may be rigid, or flexible, pliable or deformed, transparent, translucent, partially or totally reflective to well opaque and may have composite properties, regions with different properties, and may be a composite of several materials. The surface can have glare regions with shaped surfaces and / or configured regions where catalysis according to the invention can occur on one or more surfaces, and / or on a set of electrodes to which energy can be supplied on one or more surfaces. The surfaces of the supports can be configured in any suitable manner including a flat, spheroidal, cuboid, and cylindrical surface. In a specific modality, the support that carries a PMAMS is a rod. In another embodiment, the support carrying a PMAMS contains carbon, for example graphite, glassy carbon or carbon black. In one embodiment, a support carrying a PMAMS contains one or more carbon fibers. These fibers can be amorphous or graphitic carbon. They can also be nanatubes, carbon tubes or members of the fullerenes family. In a preferred embodiment, a support carrying a PMAMS contains one or more carbon fibrils (Hyperion Fibrils (MR)) (U.S. Patent No. 4,663,230). Individual carbon fibrils (as presented in US Patents Nos. 4,663,230, 5,165,909, and 5,171,560) may have diameters that range from about 3.5 nm to 70 nm, and a length greater than 100 times the diameter, a outer region of essentially continuous multiple layers of ordered carbon atoms and a distinct central core region. Simply for illustrative purposes, a typical diameter for a carbon fibril can be between about 7 and 25 nm, and a typical range of lengths can be from 1 μm to 10 μm. Carbon materials can be made to form aggregates. As shown in U.S. Patent No. 5,110,693 and references mentioned herein, two or more individual carbon fibrils can form microscopic aggregates of entangled fibrils. These aggregates can have dimensions that are within a range of 5 nm to several cm. Simply for illustrative purposes, a type of microscopic aggregate ("cotton or CC") resembles a spindle or rod of entangled fibers with a diameter that can be located within a range of 5 nm to 20 μm with a length that can be located within a range of 0.1 μm to 1000 μm. Again for illustrative purposes, another type of microscopic aggregate of fibrils ("bird's nest, or BN") may be approximately spherical with a diameter that can be located within a range of 0.1 μm to 1000 μm. Larger aggregates of each type (CC and / or BN) or mixtures thereof can be formed (vide infra). Fibrils that can be used on a support include, but are not limited to, individual fibrils, aggregates of one or 58 more fibrils, suspensions of more or more fibrils, dispersions of fibrils, mixtures of fibrils with other materials (for example oils, paraffins, waxes, polymers, gels, plastics, adhesives, epoxies, Teflon, metals, organic liquids, organic solids , inorganic solid, acids, bases, ceramics, glasses, rubber, elastomers, molecules and biological media, etc.) as well as combinations thereof. Fibrils can be magnetic in some cases and non-magnetic in others. The magnitude at which the fibrils can be magnetized or magnetized is controlled by the amount of catalyst found in the fibril as a result of the fibril production process, such a process being presented in U.S. Patent Nos. 4,663,230, 5,165,909, and 5,171,560 . The PMAMS are located in, within or in the vicinity of the supports described above. PMAMS can be generated from different types of surface link groups. Self-assembling monolayers that can be used to form a monolayer on a surface on which they are bonded, include without limitation alkanols (which bind gold and other metals), alkyltrichlorosilane (for example, linking silicone / silicon dioxide), alkanecarboxylic acids , (for example linking aluminum oxides) as well as combinations thereof. The monolayer can be formed first and then a chemical bond used to fix the binding reagents. The derivation after the self-bonding produces a crystalline package that is the most perfect of the snocapa on a support surface with fewer holes or defects. The monolayer can be derived with the binding reagents before or after the self-blage. Regular defects in the monolayer may be desirable and may be obtained by shunting prior to assembly to the monolayer on the support surface. If the derivative group (eg, exposed linkage group) in the linking reagent is sterically large, it can create a narrow packing surface at the exposed end, but with regular gaps in the metal surface. This is useful to allow the charge to flow through these regular gaps into the portions marked for ECL attached to the part that comes into contact with the sample solution. The preparation of the incomplete monolayers is known in the art. Other procedures for the preparation of incomplete monolayers include without limitation: the formation of monolayers from diluted solutions of binding reagent, the termination of the form reaction to lz monolayer before completion, the damage of more complete nanolayers with irradiations (by ionic particles), chemical reagents or light. In one embodiment, repeated stamping without re-inking of the stamp can cause a range of defective monolayers (Wilbur et al., 1995, Langmuir, 11: 825). PMAMS can be generated on the surface of matrices. The matrices can be highly conductive with, for example, metal electrodes or conductive polymer films; or the matrices can be insulating; or the matrices can be semiconductor and a medium conductivity. The matrix material may be an ion conductor or a porous material. Such porous materials can be used as a support material and / or a conductive material and / or a filter material and / or a channeling material (for example by allowing in the passage of fluids, ionic species, etc.). The porous material can be combined with additional materials. For example, composite structures can be made of porous materials with additional porous materials, conductive materials, semiconducting materials, channeling structures and / or solutions (e.g., ionic fluids). Such compounds can be sheet structures, sandwich structures, and / or spreading compounds. A solid matrix can be used which is a material, porous supported on a metal electrode. Alternatively, a porous material is found between conducting materials, semiconductor materials or a combination of semiconductor and conductive materials. One to several link domains can be found in a continuous plate of the porous material and / or they can be located in a plurality of discrete objects in the support each with one or several link domains. The surface of porous material (gel) may be flat, hemispherical or any regular or irregular shape and / or may have a variety of physical properties (e.g., elastameric, rigid, low density, high density, density gradient, dry, wet, etc.) and / or optical properties (eg transparent, translucent, opaque, reflective, refractive, etc.) and / or electrical properties (eg conductive, semiconductive, insulating, variable conductive, wet example v. dry, etc.) A channel configuration can; be formed in the matrix. The layers of porous material can have a thickness of 5 microns at 2000 microns. The layers of porous material can also have a thickness greater than 2 mm. The pores can be partially and / or fully extended through the material or can be part of a pore network. These pores can have dimensions and are located approximately from 50 angstroms to 10,000 μm. In a preferred embodiment, the material has some pores with dimensions ranging from 200 angstroms to 500 angstroms and some pores with qcte dimensions ranging from 0.5 μm to 100 μm. The porosity of the material. It can be constant in all the material or biep to be increased to decrease depending on the position of the material. The material can have a wide range of pores of different sizes distributed in a disorganized and / or random manner. The thorny material can be a compound of more than half. For example, the material may have some pores large enough for objects as large as biological cells to pass through, some pores may be large enough for biological media of the size of proteins or antibodies to pass through, some pores may be sized to only small organic molecules (of a molecular weight <1000), and / or combinations thereof. The porosity of the materials can be such that one or more molecules, liquids, solids, emulsions, suspensions, gases, gels and / or dispersions can be dispersed in, in and / or through the material. The porosity of the material is such that biological media can be dispersed (actively or passively) to be forced by some means into, into and / or through the material. Examples of; biological means include, but are not limited to, whole blood, fractionated blood, plasma, serum, urine, protein solutions, antibodies or fragments thereof, cells, subcellular particles, viruses, nucleic acids, antigens, l. icoproteíña, 1 icarcaridos, liquids, glycoproteins, carbohydrates, peptides, hormones to pharmacological agents. The porous material may have one or more layers of different porosity in such a way that the biological media can pass through one or several layers, but not through other layers. The material. porous may have the ability to withstand a current caused by the flow of ionic species. In a further refinement, the porous material is a porous gel swollen in water, for example polyacrylamide or agar. Several other gel compositions are available (for example see Soane, DS Polymer Applications for Biotechnology, Soane, DS, Ed., Simon%> Schuster: Englewood Cliffs,, 1992 or Hydrogels in Medicine and Pharmacy, Vol. I -III; Peppas, NA Ed .; CRC Press: Boca Raton, FL, 1987). Linking domains can be fixed on matrices by covalent and non-covalent linkages. (Numerous reviews and books have been written on this subject, some examples are Tampion J. and Ta pion MD Immobilized Cells: Principles and Applications Cambridge University Press: NY, 1987, Solid Phase Biachemistry: Analytical and Synthetic Aspects Scouten, WH Ed., John Wiley and Sons: NY, 1983, Methods in Enzymalogy, Immobilized Enzymes and Cells, Pt. B Mosbach, K.

E. , Elsevier Applied Science: London, 1988; Methods in Enzymalogy, Immobilized Enzymes and Cell, Pt. C Mosbach, K. E. , Elsevier Applied Science: London, 1987; Methods in Enzymology, Immobilized Enzymes and Cells, Pt. C Mosbach, K. Ed. , Elsevier Applied Science: London, 1987; see also Hydrogels in Medicine and Pharmacy, supra). For example, a protein can be fixed on a flake ?. crosslinked polyacrylamide and N-acri loi lsuccinimide by treatment with a solution of the protein. The binding domains can also be integrated into a porous matrix in a step prior to polymerization or gelation. In one embodiment, the binding domains can be fixed on cross-linked polymers by the use of various coupling chemistries. The polymers can then be crosslinked (for example using chemistries including amide bonds, disulfides, nucleophilic attack on epoxides, etc.) (See for example: Pollack et al., 1980, J. Am. Chem. Soc. 102 (20) : 6324-36). The binding domains can be fixed on monomeric species which are then incorporated into a polymer chain during the polymerization (see Adalsteinsson, 0., 1979, J. Mol. Cata. 6 (3): 199-225). In another embodiment, binding domains may be incorporated into gels by entrapping binding domains in pores during polimerization / gelation or by permeation of binding domains in the porous matrix and / or film. Additionally, binding domains can be absorbed on the surface of porous matrices (for example gels and polymer films) by non-specific adsorption caused for example by hydrophobin and / or ionic interactions. The biotin co or the binding or binding agent can be used with advantage. Avidin, streptavidin and other biotin binding agents can be incorporated into the binding domains. r PMAMS can be generated in porous materials (eg, gels) with various pore sizes and salve content. For example, polyacrylamide gels with various pore sizes can be prepared by varying the concentration of acrylamide and the degree of reoculation. In such PMAMS with pore sizes lower than the analyte, binding reactions will occur substantially on the surface of the gel. In this case, the filtration and / or electrophoresis through the gel can be used to concentrate analytes on the surface of the gel and to modulate the kinetic aspects (for example increasing the speed) of the binding reaction. Faster kinetics are helpful in rapid tests (for example, short times to results) and can generate increased sensitivity over a shorter period of time. In PMAMS with pore sizes greater than the analyte, binding reactions may occur on the surface as well as in the medullary part of the gel. In this case, filtration and / or electrophoresis can be used to increase the link syn- thetic and remove unlinked species from the surface. PMAMS formed in gels can be stored in the wet state and / or stored in a dry state and reconstituted during the test. The reagents needed for ECL assays can be incorporated into the gel before storage. { by permeation in the gel or by incorporation during gel formation) and / or can be added during the assay. Linking domains configured from a PMAMS can be generated by the application of droplets or micraglets containing each binding domain in the matrix in a liquid form on a substrate. The solidification and / or gel formation of the liquid can then be brought about by several well-known techniques (polymerization, cross-linking, cooling below the transition point to 9 ^, heat). Agents that cause solidification or gelation may be included in the drops, such that at some point after delivery, the drops solidify and / or form gels. A subsequent treatment (for example exposure to light, irradiation and / or reduction-oxidation potential) can be used to cause sol ication and / or gelation. In other embodiments such droplets or microglasses may be in pastes, prepolymer mixtures, groups of particles, and / or substantially solid droplets. Additionally, a vapor phase deposit can be used. The configuration can also be achieved by forming a structure in layers of matrices each containing one or more binding domains. For example, bound agarose (by standard chemical methods) can be flushed with an antibody in a container and allowed to form gel by cooling. Subsequent layers containing other antibodies could then be subsequently emptied into the first layer and allowed to form a gel. The cutting of this layered structure provides a continuous surface having a plurality of different binding domains. TaleThe cuts can be sharpened and other cuts can be cut to create a PMAMS surface with an even higher density of link domains. Alternatively, lines of a matrix containing a given link element are placed adjacent to each other and / or stacked. Such structures can also be cut into sections and used as a PMAMS surface. The configuration can also be achieved by taking advantage of the capacity of some matrices to achieve separation. For example, a mixture of nucleic acid probes can be separated by electrophoresis in a polyacrylamide plate generating a surface having a plurality of different binding domains. Microfluidic guides can also be used to prepare the binding domains of PMAMS on a support. A partial list of microwire guides includes hollow capillaries, capillaries made from a matrix and / or filled with a matrix, (eg, a porous or solvent-swollen media), solid supports that can support a thin film or good drop of liquid. The capillary can be solid and the reactants can flow »along the external surface of the capillary, a reservoir of reactive fluid can be exposed to the tip of a porous matrix that comes in contact with a surface of PMAMS. For example, the reagent pool can be filled continuously or periodically in such a way that a given porous matrix tip can repeatedly deposit reagents (for example, alkanols to form mannolayers and / or binding reagents, etc.). Additionally, the variation of the porosity of the tip can be used to control the flow of reagent to the surface. Different or identical binding reagents may be present in a plurality of capillaries and / or multiple different linking agents may be present in a given capillary. The capillaries come into contact with the surface of PMAMS (eg, SAM configured) such that certain regions are exposed to the binding reagents to create discrete binding domains. Reagents of; Different bonds, each present in a different microfluidic guide, are supplied concurrently from the set of fluid guides on a metal surface, SAM, etc., as desired. Microfluidic guides can also be used for inking a micro-stage with a desired molecule before application on the support surface. For example, individual microfluidic guides can be used to apply different binding reagents linked to a portion that promotes adsorption on the surface of the support (for example a free thiol in a hydrocarbon linker that promotes adsorption on gold), to form a PMAMS. Accordingly, for example, a microplate inked by the use of microfluidic guides with antibodies of different specificities that have a linker incorporated with a free thiol can be used to apply such antibodies in desired areas on a gold surface to form discrete domains of a PMAMS link. Another approach to delivering a configured fluid includes the use of microprinting devices that provide fluid icrogates by ejecting the cat through a small orifice (e.g., an ink jet printer). The ejection of the drops in these devices can be caused by different mechanisms including heating, electrostatic charging, and / or pressure from a piezo device. The configuration of more than one liquid can be achieved through the use of multiple orifices and / or an appropriate orifice and valves. In a method for the preparation of a PMAMS, microfluidic guides are used to deliver (preferably concurrently) directly over discrete regions on a surface, droplets containing the desired binding reagents, to form discrete binding domains. The binding reagents may contain a chemical functional group that forms a bond with a chemical group on the surface to which it is applied. In another variation, binding reagents in the cat are absorbed or bound non-specifically on the surface (for example, dried on the surface). Alternatively, drop (s) deposited on a surface contains reagents that can form a matrix. This matrix can be a solid, polymer or a gel. The formation of the matrix can be carried out by evaporation of the solvent. It can be by polymerization of monamic species. It can be through the crosslinking of preformed polymers. It can be carried out by modulating the temperature (for example cooling and / or heating). It can be carried out by other methods. For example, a polymer species can be cooled through a transition cooler or by the addition of a reactive that causes gel formation. The formation of the solid matrix can be induced by the generation of reactive species in an electrode (including the substrate), by light (or other radiation) by the addition of reagents that induce solidification or gel formation. , by cooling or heating. Additionally, the surface may contain catalysts capable of initiating matrix formation (e.g., by gel formation or polymerization). In a preferred technique, hydrophilic / hydrophilic regions configured to prevent spreading of applied fluids or gels may be employed. Such fluid to gel may contain binding reagents to bind on a surface or a support to form a binding domain of the PMAMS. In this case, the use of such hydrophobic / hydrophobic edge helps limit the bond domain produced to a discrete area. Alternatively, the fluid contains reagents that can form a matrix on the surface and bind reagents contained within a defined region when deposited on a surface. For example, the hydrophobic / hydrophobic edge assist can be used to limit the drop to a defined region. Additionably, areas either hydrophilic or hydrophobic may have clumps that may be incorporated (for example covalently or non-covalently bonded) in the matrix, allowing a more stable adhesion of the matrix onto the substrate (I taya and Bard, 1978, Anal, Chem. 50 (11): 1487-1489). In another technique, the fluid or gel. applied is the sample that contains the anal, ito of interest, and the sample is applied on a prepared PMAMS. In a preferred example, capillaries containing hydrophilic solutions can be used to deposit a solution in discrete areas, creating hydrophilic domains surrounded by hydrophobic regions. Thirdly, hydrophobic linker domains surrounded by hydraphical regions can be employed with hydrophobic fluid containing binding reagents or analyte (s)). Hydrophobic and hydrophilic are relative terms, in relation to each other and / or in relation to the sample to be applied, that is, in such a way that the spreading or wetting of a sample of fluid or gel applied to the binding domains can be controlled. In addition, controlled deposition of a solution from a set of microfluids can be achieved by using surface physical characteristics (eg pazos or channels on the surface). A microfluidic guide may be included in a cassette, or more preferably, be used to apply specific reagents to a support before use. More than one chemical bonding procedure can be applied to the same support surface and / or a surface with both hydrophilic and hydrophobic binding domains? created using multiple stamps. For example, an area where a hydrophilic binding domain in a position 1 and a hydrophobic binding domain in a position 2 is desired can be prepared in the following manner. A first hydrophilic print is made which. has a disc in position 1 and a larger ring in position 2. A second hydrophobic stamp is held with a disc in position 2 that fits within the ring monolayer left by stamp 1. Finally, the surface is washed with a hydrophobic solution of monscapa components. Partially, a PMAMS is generated by microcontact printing, that is, stamping. The monolayer applied in this way is composed of a surface bonding group, for example, in the case of a gold surface, a thiol group with an alkane spacer (for example, (CH2) n)) is preferred . A spacer group is linked (preferably linked cavalently) to a linking group A. "A" can be, for example, avidin, strep >tavidine or biotin or any other suitable linking reagent with a complementary "B" linker available. The A: B linkage can be covalent or navalent and some chemical chemistry techniques known in the art can be employed in accordance with what is presented, for example, by Bard et al. (US Patents Nos. 5,221,605 and 5,310,687). "B" is further linked to a binding reagent such as an antibody, antigen, nucleic acid, pharmaceutical substance or other suitable substance to form a binding domain that can be linked to one or more analytes of interest in a sample try. B can also be linked to an ECL MARKER or marker. Linkage group B can be supplied to the SAM by means of a set of microfluidic or capillary guides (Figure 5A-5C) which can place a plurality of reagents "B" with different surface specificities of linkage in the eplace "A" of monolayer A and B can also be linked before being fixed on the monolayer. In Figure 5A, shape-independent linking domains are depicted, simply for the purpose of illustrating as geometric shapes 602 to indicate that different binding specificities may be present in a single support 600. Figure 5B provides a top view of a set 606 of microfluidic guides (for example, capillary). The points 610 are the guides in court. Figure 5C provides a side view of the assembly 608 of microfiber guides. The lines that arise from the upper part and from the lower part are the individual microlide 610 guides. The geometric shapes 612 in the. lower aspect represent specific binding domains formed by supplying the binding reagent from each individual capillary. By way of example, after the first stamping presented above, the bare surface regions (eg, gold) can react with a second alkathiol which does not have the chemical bonding properties A and is hydrophobicity / idropicity opposite to the first monolayer. previous. In this way, specific binding domains are prepared on a surface. A binding reagent that is specific for an analyte of interest may be used for each binding domain or it may be possible to employ a binding reagent that specifically binds with several apallites of interest. In another variant, a support surface may be stamped several times by materials (eg, linkage reagents, ECL markers, SAMs) having different binding chemical properties and / or different binding portions as shown in the figure 5A above. The binding reagents which are configured can be stable and / or robust chemical groups (for example, which survive the conditions to which they are subjected) which are subsequently linked with less stable or robust linking groups. Multiple links can be used to optimize the conditions of each step in the preparation and on the surface of PMAMS and / or simplify the fabrication of the PMAMS surface. For example, a first surface of PMAMS can be manufactured generically and then modified to create different surfaces of PMAMS. In another example, a generic PMAMS surface may react with a mixture of solution or link reagents that contain linker domains that are directed to particular regions (eg, linker domains) on the surface of PMAMS. For example, a linkage domain pattern each representing a different aligo (n? Cleotide) sequence is linked to the surface. This surface is then treated with a solution containing a mixture of secondary binding reagents, each linked to an oligo sequence (nucleotide) complementary to a sequence on the surface. In this way, the configuration of these secondary link elements can be achieved. Preferably, the sequences of the igo-nucleotides) are DNA 6-30mers. Some 6-30mM sequence sets may contain substantially similar sequence complementarity such that the approximate binding constants for hybridization are similar within a given set and discernibly different from less complementary sequences. In another embodiment, the secondary binding elements are proteins (eg, antibodies).

Methods described to inhibit the dilution or dispersion of applied reagents or samples on a surface are described in section 5.13 below, and such methods can also be used in the preparation of PMAMS (and / or sample application). The applied potential (eg from the pair of electrodes / counter electrodes) can be used to additionally control the deposition and / or the dispersion of reagents r and / to samples (see, for example, Abbott et al., 1994, Langmuir 10 ( 5): 1493-1497). The PMAMS binding reagents can be located in carbon-containing materials. They can also be located in individual carbon fibrils, or the PMAMS binding reagents can be used in aggregates of one or more fibrils. In these embodiments, the PMAMS binding reagents can be located in suspensions of one or more fibrils, dispersions of fibrils, mixtures of fibrils with other materials (described by way of example above) as well as combinations thereof. The PMAMS binding reagents can be located in a plurality of individual fibrils and / or aggregates of fibrils located in or on or in the vicinity of a support. In one example, the binding reagents are located in scattered individual fibrils or in aggregates of fibrils. These fibrils or these aggregates of fibrils can be spatially located in different domains on a support, and can constitute a link domain as defined in this application. In another example, such individual binding domains or a plurality of such binding domains; located in spatially different regions of the support. As a non-limiting axis, such individual link domains to joint linkage dams can be located in depressions, cavities and / or holes in the support. In another additional example, individual linking domains or a plurality of domain can be located in water cats, gels, elastomers, plastics, oils, etc., which are located on the surface of the soup. In yet another example, individual binding domains can be located on the support by a coating (which may be configured) having different binding affinities for different binding reagents and / or sets of binding reagents / fibrils. The binding domains are preferably located in a plurality of individual fibrils and / or aggregates of fibrils and can be prepared in a biscuit by means of one or more microfluidic guides (for example, a capillary). Different or identical binding reagents may be present within or on a plurality of microfluidic guides and / or multiple distinct binding agents may be present either inside or on a given micofluid guide. The capillaries may come into contact with the soparte (mottled) and / or they may supply the reagents while either the microfluidic guide and / or the surface is being scanned or moved in relation to the other (ie, a writing method). similar to a pen). The microfluidic guide can supply the binding reagents located in the fibrils on the support in such a way that certain support regions are exposed to the reactive fibril-binding complex (s) for cr & ) discrete link domain (s). In a preferred embodiment, different binding reactants, each present in a different microfluidic guide, are supplied concurrently from the set of guides in the support. In one example, binding reagents and / or the fibrils in which they are located are derived with a chemical functional group that forms a bond (eg, covalent or non-cavalept interaction) on the surface of the support. In some embodiments, the binding reagents and the fibrils bind non-specifically or adsorb on the surface. In a further aspect, the binding reagents located in the fibrils can be delivered in depressions, cavities and / or holes in the surface of the support. In another example, the binding reagents are delivered to a surface coated with a material having a stronger or weaker binding affinity for certain binding reagents or binding / fibril reagent assemblies and thus create domains of the reagents that are used spatially and distinctly from other binding reagents. The binding reagents are located in one or more individual fibrils or aggregates of magnetic fibrils. In such a case, a magnetic support can attract the binding reagents located in magnetic fibrils to the support. The support can contain several different magnetic regions and surrounded by regions that are not magnetic. Linkage reagents located in magnetic fibrils can be located in magnetic support regions. In addition, the support may contain one or more distinct regions that are magnetic and surrounded by regions that are not magnetic, and the strength of the magnetic field in the magnetic regions may be modulated or switched. In this aspect, the. The use of such a modulated or switchable magnetic field helps to fix or release the binding reagents located in fibrils from the surface of the support and in this way can serve to adjust or mix said domains. In general terms there are from 2 to 100 million linking domains and preferably from 25 to 500 domains. The binding domains can be located in working electrodes and / or the counter electrode.The different embodiments described herein for different types of PMAMS, supports, and electrodes and configurations thereof may also be practiced in combination with each other. The PMAMS supports can be preserved (for example, by surface protective coatings, surface drying, robust vacuum packing or inert atmosphere, cooling and related methods) for later use. 5.2. LINK REAGENTS The binding domains of the invention are prepared to contain binding reagents that specifically bind to at least one analyte (ligand) of interest. Linkage reagents in discrete binding domains are selected such that the binding domains have the desired binding specificity. Binding reagents can be selected from any molecule known in the art that can, or can putatively, bind specifically to an analyte of interest. The analogous, interesting item can be selected from those described in section 5.10 below, "ECL tests that can be carried out." Accordingly, the binding reagents include receptors, ligands for receptors, antibodies or binding portions thereof (eg, Fab,. {Fab) '2), proteins or fragments thereof, nucleic acids, or oligonucleotides , glycoproteins, polysaccharides, antigens, epitopes, cells and cellular components, subcellular particles, carbohydrate moieties, enzymes, enzyme substrates, lec, protein A, protein G, organic compounds, organometallic compounds, viruses, prions, viroids, líp dss, fatty acids, 1 ipopal isacápdos, peptides, cellular etabolites, hormones, pharmacological agents, tranquilizers, barbiturates, alkaloids, esreróides, vitamins, amino acids, sugars, nonbiological polymers, tai atina, avidina, streptavidin, compounds of organic link with, for example, polymer resin, 11pop, rotates, cytokines, lymphokines, hormones, synthetic polymers, organic and inorganic molecules, etc., without imitate these reagents. Nucleic acids and oligonucleotides can refer to DNA, RNA and / or oligonucleotide analogues including, but not limited to, oligonucleotide sites containing modified bases or modified sugars, or oligonucleotides containing structural chemistries other than polynucleotides. and phosphodi ester linkages (see, for example, Nielsen, PE (1995) Annu Rev. Biophys, Bio Cl., Street, 24 167-183), and / or oligonucleotides, which have been synthesized = or modified to present groups chemicals that can be used to form fixations (covalent or non-covalent) with other molecules (where we define a nucleic acid or igo-nucleotide) as containing two or more nucleic acid bases and / or nucleic acid base derivatives). The PMAMS of the present invention may have a plurality of described binding domains comprising at least one binding domain containing binding reagents that are identical to each other and which differ in specificity from the binding reagents contained within other binding domains. link domains, to provide the link of different analysts of interest through different link domains. By way of example, such PMAMS comprises a binding domain containing antibody to the thyroid stimulating hormone (TSH), a binding domain containing an Igonucleotide sl hybridizing with the hepatitis C virus (HCV), a binding domain that contains an oligonucleotide that hybridizes with HSV, a binding domain that contains an antibody against an HIV protein or gl. icoprotein, a binding domain containing? n antibody to the prostate specific antigen (PSA), and a binding domain containing an antibody against the hepatitis B virus (HBV), or any subset of the foregoing. A PMAMS may have a plurality of discrete binding domains comprising some a binding domain that contains within it binding reagents that differ in terms of binding specificity, in such a way that a single binding domain can be linked to several analytes of interest. By way of example such PMAMS comprises a binding domain containing either antibody to a T cell antigen receptor or antibody to a T-cell surface antigen, for example, CD4. A PMAMS may have a plurality of discrete link domains comprising <i) at least one ing domain containing ing reagents q? e are identical to each other and differ in specificity from at least one of the ing reagents contained within the other ing domains; and (ii) at least one link domain that contains within it. ing reagents that differ in terms of ing specificities. By way of example, a PMAMS is made which has (a) at least one ing domain containing ing reagents of a single identity, eg, antibody against a T cell antigen receptor, eg, antigen receptor from alpha T cell, beta to well gamma-delta T cell antigen receptor, thus allowing this at least one ing domain to to all cells expressing this receptor of T-cell antigen; and (b) at least one ing domain containing two different ing reagents, for example, antibodies to T cell antigen receptor and antibodies to CD4, thus allowing this at least one ing domain to to CD4 + T lymphocytes. that excrete this T cell antigen receptor (i.e., a subpopulation of T lymphocytes). In another embodiment, at least one ing domain contains ing reagents which are different molecules but which have the same ing specificities (for example ing reagents such as epidermal growth factor bed and epidermal growth factor receptor antibody). A plurality of ing reagents can be selected such that even when the linking reagents are different and have different ing specificities, they recognize the same analyte (in an alternative embodiment, different analytes are recognized). For example, when the analyte is an analyte that has numerous ing portions (eg, a cell having different cell surface antigens), different ing reagents that to different ing portions will recognize the same analyte. As another example, antibodies from different cell surface antigens in a single cell will recognize the same cell. As an additional example antibodies of epitopes other than a single antigen can be used as ing reagents to recognize the antigen. In another additional mode, only link reactive (s) that are specifically linked to an anal. Only one of interest are present in one or several link domains. Alternatively, ing reagents that speci? Cally to more than one analyte of interest are present in one or more ing domains (eg, a cross-reactive antibody). In a particular design, ing reactions linking a class of analytes, for example, with similar characteristics can be employed. Linking domains can also be incorporated into? N PMAMS containing ing reagents that are specific for a desired standard analyte and that are employed as an internal standard (for example, a ing domain that may be in contact with a sample containing a defined amount). of an analyte to which the ing reagents are linked). Multiple ing domains containing specific ing reagents for the same analyte (s) may also be incorporated into a PMAMS to allow statistical averaging of the analytical results. The ing reagents do not have to be only specific for the same analyte but can be identical, thus recognizing the same ing portion in the analyte. Accordingly, several ing domains (for example within a range of 2 to 100 million) can be prepared that specifically to the same ing portion, such that the ECL readings can be statistically averaged to control variation and improve the accuracy. The plurality of link domain in a PMAMS may be specific for a control apalite or an analyte of interest, or both, in a single support. With another example, one or several discrete link domains can be prepared with a known initial concentration of ECL markers. The integrated ECL layer serves as a control to monitor, for example marker degradation and the effects of temperature. A binding reagent can be used which is a substrate-specific enzyme is the analyte of interest), wherein the product of the enzymatic reaction on the substrate is a reporter agent (an agent that can be detected), for example, a product that triggers an ECL reaction, a fluorescent molecule, a substrate that changes color upon contact with the appropriate enzyme (for example a cramogenic substrate for horseradish peroxidase), etc. In one example of such an embodiment, the enzyme used as a binding reagent is glucose dehydrogenase (GDH) which can be used to detect or measure glucose in a sample. An ECL marker is located within or near the link domain that contains the GDH. NADH is produced by the action of the enzyme on glucose, NADH can react with ECL markers to promote ECL (Martin et al., 1993, Anal. Chim. Acta 281: 475).

Linking domains that contain linkage reagents that increase the linkage of fando (ie, bind to a binding portion present in the analyte of interest as well as other analytes in the sample) can be used to increase signal ratios and noise during the detection or measurement of the electroqimicoluminiscence. By way of example, when the analyte of interest is a specific cellular subpopulation (e.g., CD4 + cells) and r the sample is a fluid sample (e.g., blood) containing cells from a patient, acid antibody can be employed. sialic as a binding reagent to increase background binding for all the cells in the sample (since sialic acid is a component of virtually all the superficial glycoproteins of cells), and an antibody of a surface antigen cell-specific for the cellular subpopulation (eg, antibody to CD4) can then be used as a reactive binding (in the same binding domain or in a binding domain different from that containing the sialic acid antibody). 5.3. VOLTAGE WAVE FORM The shape of the volta e (change in potential / electrical voltage) printed on the plurality of electrode and counter-electrode pairs of the ECL cell must be sufficient to trigger an ECL reaction. This voltage waveform usually has the form of a uniform voltage sweep that starts at a first voltage, constantly shifts! towards a second voltage, it returns through the first voltage to a third voltage and then returns back to the first voltage. For example, the waveform can start at a first voltage within a range of -0.5 to 0.5 volts, up to a second voltage located within a range of 1 to 2.5 volts, and return through the first voltage to a third voltage located within a range of 0.0 to -1 volt. In another example, in simpler waves, the voltage can be modified from 0.0 to +3.5 to 0.0. Voltage waveforms may incorporate linear ramps, step functions, and / or other functions. Voltage waveforms can incorporate period of time when the. voltage remains fixed at a potential. The applied potential can be controlled in relation to one or more electrodes, or the use of reference electrodes can be dispensed with. Additionally, a negative potential can be used. Accordingly, the voltages used to induce ECL emissions from the cassette of the present invention will be easily selected to achieve an optimum ECL signal intensity and specificity for the ECL marker and the assay medium. In some applications, the voltage varies preferably as the light emitted from the link domain is measured. This is important to determine the threshold value of the electric field necessary to cause the link domain to emit light. In this case, the electrical potential applied to the link domain starts at a value that is lower than the threshold required to emit light, and a first measurement of the emitted light is made. If no light is emitted, or if the light is below a predetermined threshold, the electric potential applied through the pair of electrodes is increased under computer control, as for example by means of a voltage source controlled by computer and another measurement of the light is made. This process may be repeated until the appropriate predetermined amount of light is received. In this way, the applied voltage can be used as the test signal. The ECL signal can be generated from an AC voltage applied to the pairs of electrodes. the person with certain knowledge in the art familiar with the voltage and current environments in accordance with the presented, for example, in US Pat. Nos. 5, 324,475 and 5,068,088 will be able to easily select the optimum operating voltages and the voltage sweep to trigger an ECL emission. The potential required to generate ECL can be generated by illumination of the working electrode surface if the working electrode is a semiconductor or contains another portion that generates an electric current in response to light. 5.4. LEADING ELECTRODES AND METHODS FOR USING THEM Many methods can be used to supply power to the pilurality of electrode / counter electrode pairs. Various illustrative techniques are presented in figures 14-r 18. In these figures, an example of 4 pairs of electrode / counter electrode (101, 102, 103, 104 and a waveform generator that is typically a digital computer and which is preferably the same computer used to process the ECL detected by the detection means In Figure 14, each pair of electrodes (counter electrodes 101-104 is individually directed by a pair of lines connected to the waveform generator. By way of example, the lines 105, 106 have access to the pair of electrodes / counter electrodes 101. An appropriate waveform can be supplied by the waveform generator at any given time to one or more of the pairs of lines connected to the several pairs of electrode / counter electrode To reduce the number of connections required to supply power to the electrode pairs, alternatives to the direct connection scheme of 7 are provided.

Figure 14. For example, an access scheme of rows and columns to provide electrical power to some or all of the electrodes is illustrated in Figure 15. In this scheme, one of the electrodes 201, 202 in each column of the plurality of electrode pairs / counter electrode is connected to a common electrical conductor 205 on a support 200, and each of the counter electrodes in each row of the plurality of pairs electrode / counter electrode is connected to a conductor 207, 208 in the holder 200. The conductors 205, 206 are connected to the connections Cl, C2, respectively, on the supporting edge 200 and the conductors 207, 208 are connected to the connections Rl, R2, respectively. Each of these connections is then connected by a separate line to the waveform generator. As a result, in the configuration of Figure 15, the number of required connections and signal lines from the waveform generator are reduced from 8 to 4. To allow a fast and sequential supply of energy to each pair of electrodes , a computer controlled switching device is beneficial. The configuration of Figure 16 shows a plurality of electrodes connected to a first multiplexer 310. Several counter electrodes are connected to a second multiplexer 320. The first iplexer is also connected to a first pole of a voltage source 330 which typically supplies the electrical potential that varies with the passage of time described infra. The second multiplexer is also connected to a second pole of the voltage source. Using the address lines A0-A3 electrically connected to each of the multi-connectors and connected to a latch 340, a computer processor 350 can direct the multiplexers to selectively connect any or all of the first electrodes to the ppmer pole of the voltage source and any or all of the second electrodes to the second pole of the voltage source. As shown in Figure 17, vain voltage sources are connected through separate sets of multiple iplexers to each of the electrodes. If a first electric potential or range of electric potentials is required in a particular pair of electrodes, the multiplexers 410, 420 associated with the voltage source 430 providing this potential are directed by the computation processor 350, typically by means of of a bolt 340, thus connecting this particular source of voltage with the pair of electrodes in question. If a different electrical potential or a range of different electrical potentials are required for another pair of electrodes, the iplexaruses 440, 450 associated with these different voltage sources 460 are directed by the computer processor, thus connecting this source of power. voltage through the associated multiplex iplexers 440, 450 to the pair of electrodes. If the set of electrodes in this mode has at least a part of the pairs of electrodes that can be propelled indepently, as shown in the figure 14 or 15, for example, one pair of electrodes can be driven by one voltage source while another pair of electrodes can be driven simultaneously with another voltage source. Alternately, the two voltage sources of Figure 17 can be replaced with a single source of; voltage connected to both sets of multiplexers in parallel, allowing two pairs of electrodes to be driven from the same voltage source. Instead of a duplicate set of multiplexes for each voltage source as shown in Fig. 17, a plurality of voltage ftests 520, 530 can be provided as shown in Fig. 18. These voltage sources can be connected through a 510 computer-controlled electrical switch or switches will provide a unique combination of 310, 320 multiplexers. As shown in FIG. 18, the computer could direct the 510 switch to connect a particular source of voltage to the multiplexers., and could also direct the many iplexers (through the criminalization of their address lines A0-A3) to connect the selected sources of volt e with the specific pair of desired electrodes. Alternatively, the electrical potential applied to each of the electrode pairs in one embodiment can be varied. This is especially beneficial when a cassette having a plurality of different link domains is employed. Such a cassette may refer to a different range of electric potential applied in different binding domains. Several different modalities capable of varying the electrical potential adjusted to each electrode are contemplated. A computer-controlled voltage source can be used to advantage. A computer controlled voltage source is a source of voltage that can be controlled by a computer to select a particular electric power supply. Al ernatively, it can be programmed to sequentially apply a particular range of electrical potentials for a predetermined period of time. In such a system, electrically connected address lines between the computer and the voltage source allow the computer to program the voltage source so that it produces the particular electrical potential for its application to the pair of electrodes that must receive power. Additional methods for supplying power to the plurality of pairs of electrodes can also be used. For example, a plurality of reference electrodes may be placed in the vicinity of each of the various electrode and counter electrode pairs to detect the voltage applied there. In this way you can keep an additional control of the form of; volt je wave. Figure 36 shows atra mode of the invention; electrode assemblies (3600, 3601) are supported on each of several surfaces (3602, 3603) separated by a pattern of holes in an insulator 3604 (for example a plastic sheet with perforated holes 3605). Each electrode can pass in a plurality of holes. If a potential is applied between an electrode of each surface, the current can only pass through a range that is in contact with both electrodes, thus limiting the location of; any electrochemistry or ECL that may occur. In the preferred embodiment shown in the figure, the electrodes (3600, 3601) are sets of lines in a support. The two sets of electrodes on the two surfaces are oriented perpendicularly between them. Intervals in the isolation sheet are located only at the intersection of the electrodes of each surface. This modality has the advantage compared to the pairs of individually directed electrodes that require a smaller number of electrical conductors. In an alternative embodiment, the insulator 3604 is omitted and the surfaces collide in a close proximity such that there is only a narrow gap between the two surfaces. In this mode, an applied potential between electrodes on each surface will cause the current to pass at the intersection of the electrode (for example, where the distance between the electrodes is minimal) thus limiting the location of any electrochemical phenomenon or ECL that can occur. 5.5 DETECTION OF THE LIGHT The light generated by the emission of ECL triggers is detected by an associated detector of light or detectors placed adjacent to the apparatus of the invention. The light detector can, for example, be a film, a photomulphometrical tube, a photodiode, an avalanche photodiode, a charge coupled device ("CCD") or another light detector or camera. The light detector may be a simple detector for detecting sequential emissions or it may be a plural detector for detecting and resolving spatially simultaneous emissions at single or multiple wavelengths of emitted light. The light emitted and detected may be visible light or it may be emitted as non-visible radiation such as infrared or ultraviolet radiation. The detector or detectors can be stationary or mobile. The emitted light or other radiations can be conducted to the detector or detectors by means of lenses, eyes, as well as fiber optic light guides or light conduits (single, multiple, fixed or mobile) positioned in either adjacent to the cassette link surface or the detector can directly receive the light. In addition, the PMAMS supports and electrode surfaces themselves can be used to guide or allow the transmission of light. The PMAMS can be formed on the surface of a set of light detectors in such a way that each detector receives only the light coming from a link domain. The set of light detectors may be a CCD chip, and the binding domains may be fixed (using standard coupling chemical reactions) on the surface of the semiconductor device. Gates deposited in the link domains, or in a second nearby surface, can be used as microlenses to direct or control the emitted light. Alternatively, a light detector can be oriented directly in front of the cassette; and vanes light focusing device, such as for example parabolic reflectors or lenses can be used in place of a light conduit to direct light from any of vain domains linking to the detector. The emitted light from at least two discrete link domains can be measured simultaneously CJ either sequentially. The error caused by thermal displacement, the aging of the device, or else the electrical noise inherent in the light detectors can be controlled by means of a "cutter" device between the light measuring device and the link domain being measured. The cutter can be any of the common metallic cutters well known to people with certain cuts in the art, such as a rotating disk with slits or cutouts that allow the passage of light. Alternatively, the light can be cut by an LCD shutter, a set of LCD shutters, a valve or solid state light valves or the like. Alternatively, a flat set of LCD shutters or solid state light valves such as those known in the optical computation art can be employed. These devices are preferably located between the plane of the cassette and the light conduit (or conduits) or light focusing devices directing the light from the link domains to the light detector. In one modality, a shutter is located above each of the link domains. When an LCD shutter or a light valve is used, the shutters can be modulated at different frequencies to simul- taneously provide different cutting speeds for different light emission link domains. Using this technique, a plurality of different light signals can be superimposed and said signals measured simultaneously by means of a single detector. An electronic bandpass filter electrically connected to the light detector can then be used to sepia the single electrical signal in several electrical components, each corresponding to one or more of the individual r components of the light. By cutting off the light, as mentioned above, or using another mechanism well known in the art, an AC light waveform is created which allows the electronic noise elimination of the CD noise component. Likewise, the ECL signal can be calibrated by comparing previously determined results with standard reagents to correct for signal modulation due to reagent depletion. 5.6. ECL SEDAL ANALYSIS Signals from a given link domain can have a range of values, and these values correlate with a quantitative measurement to provide a signal "analog". In technical atra, a "digital" signal is obtained from each domain to indicate that an analyte is present or not. Statistical analysis is used for both techniques, and is especially useful for translating a plurality of digital signals to provide a quantitative result. Some analytes, however, require a digital signal present / not present indicating a threshold concentration. "Analog" and / or "digital" formats can be used separately or in combination. Other statistical methods can be used with PMAMS. For example, it is possible to create gradients of PMAMS concentration on a surface (Chaudhury et al., 1992, Science 256: 1539-1541). This technique is used to determine concentrations by statistical analysis of the link in the gradient of concentrations. Multiple linear sets of PMAMS with concentration gradients can be produced with a multiplicity of different specific binding reagents. The concentration gradients may consist of discrete binding domains that have different concentrations of the binding reagents. The presence of the control test systems in the cassette binding surface is an important element to ensure the uniformity of each analysis to control the variation of signals (for example, variations due to degradations, fluctuations, aging of the cassettes and others). components, thermal changes, noise in the electronic circuit and noise in the fatodetección device, etc.). For example, multiple redundant binding domains (containing identical binding reagents or different binding reagents that are specific for the same analyte) for the same analyte can be used. The other example uses analytes of known concentration or control domains of a PMAMS are covalently linked to a known amount of an ECL label or a known amount of ECL label in solution is used. The tests carried out in accordance with the present invention quickly and efficiently collect large amounts of data that can be stored, for example, in the form of a database consisting of a collection of chemical information or research. The collected data can also be used for a quick personal or forensic identification. For example, the use of a plurality of nucleic acid probes when exposed to a human DNA sample can be used for a signature DNA fingerprint that can be easily employed to identify clinical or research samples. 5.7 PREPARATION OF MULTIPLE ELECTRODE TESTS The electrodes can, in general terms, have a width or diameter of 0.01 to 10 mm. In a preferred range, the pairs of electrodes are 0.01 to 1 mm in terms of their dimension (width or diameter or larger dimension according to the geometry of the electrode piers). s: Preferably, the electrodes are fabricated from suitable conductive materials, such as for example transparent metal films or semiconductors (for example, gold to either indo-tin oxide, respectively, as is well known in the art, for example, for the manufacture of liquid crystal displays and the like In the assembled form of the cassette, there is sufficient space between the first support and the second support to contain an analytical sample such as, for example, a thin film or a wet surface. Electrodes can be manufactured from materials containing carbon, carbon fibers, carbon nanotubes and / or aggregates of the above.The electrodes can be manufactured from carbon fibrils One or several individual fibrils and / or one or more aggregates fibrils can be processed to form a larger aggregate (US Patent No. 5,124,075) This larger aggregate is a mat to good mesh (hereinafter referred to as "fibril mat") where the fibrils may be entangled or woven. The fibril mats typically have a surface area of between 50 and 400 m2 / gram. As an e plo, a fibril mat can be used as a working electrode, a counter electrode or a reference electrode in analytical and / or preparation electrochemistry. In one example, the fibril mat is started as an electrode for electrochemiluminescence (ECL). The binding domains of the PMAMS may be supported by a fibril mat. The PMAMS of the present invention has a plurality of discrete binding domains, among which das or more may be identical to each other or may be different. The fibril mat supports one or several link domains. One or more screening guides can be used to prepare a plurality of binding domains in a fibril mat. Different or identical binding reagents may be present in a plurality of multiple different microlide guides and / or binding agent may be present in a guide of my solution. In FIGS. 22A and 22B, several microfluidic guides 2201, preferably a set, are used to supply, preferably concurrently, to the regions of the fibrous mat 2200, drops containing the desired binding reagents to form discrete binding domains. 2202. The binding reagents form a bond with portions present in the fibril mat. The binding reagents can be adhered non-specifically to the mat or dried on the surface. The desired binding reagents are supplied to the fibril mat while a suction filtration is applied to the mat. In this case, the suction filtration draws part, all or none of the binding reagents into or through the mat, and thus reduces the amount of lateral expansion of the binding reagents on the mat surface during the configuration process. The fibril mats are prepared by compressing suspensions of carbon fibrils in a substrate through which the liquid in the suspension can pass (for example, a filter). Examples of filters that can be used to form fibril mats include filter paper, filters formed from palm-palm membranes (for example, nylon), metal microwires, ceramic filters, glass filters, elastomeric filters, glass fiber filters and / or a combination of two or more such filter pads. One skilled in the art of filtration will recognize that these materials are presented only by way of examples of the many possible materials suitable for the filtration of solids suspensions. Figures 23A and 23B illustrate a mode in which fibril mats can be manufactured by suction filtration. A dispersion and / or suspension of carbon fibrils 2301 is filtered using a filter 2300 equipped optionally with a filter membrane 2303 and / or a filter soup 2302. The suspension is filtered using suction applied by a vacuum source 2305 to the filter by, for example, a filter flange 2306. A fibril mat 2304 collects on either of the membranes or on both filter membranes 2303 and / or the fi ber carrier 2302. The fibril mat 2304, with or without the 2303 filter membrane it can be removed from the filter. In another embodiment, fibril suspensions are passed through a filter by the use of pressure. In one example, pressure is exerted on a limited suspension of fibrils by compressing a limited layer of air and / or liquid above the suspension with a disc. In a specific example, the suspension of fibrils is limited in a syringe, the piston is a syringe plunger and the filter is a disposable syringe filter (many filters of this type are well known to one skilled in the art). Fibril suspensions are pushed into a filter by capillary action or are filtered by wicking the suspension in or through a filter. In another modality, individual fibrils or aggregates of fibrils are covalently re-named in mats. Fibrilas de <Rivadas with photosensitive portions are palmerised when they are exposed to light they radiate with light. The filter can be used to trap the fibrils in their pores to form a composite mat where the filter acts as a support. In Figure 24, a fibril mat 2400 can be peeled by passing a fibrous paste 2401, supplied by a source 2402, between two large rollers 2403. In this process, which may be analogous to processes found in the manufacture of sheets of paper or polymer, the rollers push the liquid out of the suspension and a large, continuous mat of fibrils is produced from which smaller mats can be cut. The fibril mats can be free (for example, without support) or supported. The filtration rate can vary to achieve desired varieties on the mat. For example, properties may be varied including the uniformity or non-uniformity of structure, the amount of entanglement of the fibrils or aggregates of fibrils, the thickness, the porosity of the mat, and / or combinations thereof. The suspensions of carbon fibrils are limited and the liquid in which the fibrils are suspended is removed. For example, the liquid in which the fibrils are suspended evaporates. In another example, the liquid is removed by heating. In another axis, the suspension is subjected to centrifugation and the resulting liquid (for example, the supernatant) is removed. In another example, the liquid is removed by evacuation.

The suspension can be placed in one or more of the filters described above, and the suspension dried by evaporation. The suspension can be dried by heating or baking in an oven or the liquid can be removed by freezing and extracting the liquid. In another example, the liquid is removed by evacuation with a pump. Many other well-known methods by one skilled in the art are available to remove liquids from a suspension. Fibril suspensions suitable for carrying out fibrillation mats for filtration can be formed by the dispersion of one or more carbon fibrils in a liquid, almost solid or appropriate gel. Examples of suitable liquids include, but are not limited to, water, ethanol, methanol, hexane, methylene chloride, buffered solutions, surfactants, organic solvents, solutions containing biological media (e.g., protein, antibodies or fragments thereof). , cells, subcellular particles, viruses, nucleic acids, antigens, 1 ipoproteins, polysaccharides, lipids, glycoproteins, carbohydrates, peptides, hormones or pharmacological agents, solutions of small molecules, polymer precursors, solutions of acids to bases , oils and / or combinations thereof). A suspension of fibrils can be prepared by dispersing > carbon fibrils in an aqueous solution by means of sonication. In another embodiment, a surfactant and / or detergent may be added. The fibril mat may have a thickness of approximately 0.01 μm to 10,000 μm. In preferred embodiments, the fibril mat has a thickness comprised between 1 μm and 100 μm. Especially preferred are embodiments, in which the fibril mats are located from 10 mm to 20 < "<mm width or diameter The fibril mat can be repeatedly washed and filtered again to remove residual materials remaining from the suspension.Fibrillar mats prepared by filtration or evaporation are heated (for example, in an oven) to remove residual liquid from the suspension not removed by successive filtration steps can be used to form mat fibrils composed of one or several different layers that are either in contact with one or more other layers or that are in Very narrow proximity to one or several other layers.The layers can be distinguished by vain properties, including, without limitation, differences in porosity, density, thickness, decrease in sizes of individual fibrils and / or microscopic aggregates of fibrils , the type, number, and / or size of the aggregates of fibrils, the chemical derivation of the fibrils (vide fra), and / or in the presence of other material fixed on the fibrils. Figure 25 is a multilayer fibril mat 25 0 which is prepared by successive filtration steps. A layer of thickness from 0.5 μm to 100 μm 2501 of flat fibrils forms the first layer; a layer with a thickness of 0.5 to 10 μm of fibrils 2502 incorporating portions, for example polymethylglycolics) that resists the adsorption of proteins and other molecules form the second layer; a layer thickness of 0.5 to 5 μ 2503 that incorporates one or several link domains' vide supra) forms the third layer. The binding domains contain one or several 2504 antibodies, which can be linked to an analogue 2505. This analogous or analogous complex can bind a labeled antibody 2506. The label can be a marker of ECL. In other modalities, the marker may be one or several markers described elsewhere in this application. Such a multilayer mat may be independent or well supported in one of several possible supports described herein. Multiple-layer mats can be formed in which combinations of layers exist, in which some or all of the layers may be different. The filter used to form the fibril mat, the fibrils and / or the fibril mat can be coated.

In particular modalities, the metallic san coatings. These reversals can be configured in such a way that certain parts are coated and other parts are na. In one example, the coating is applied by elect rocle > ptós? to In another example, the coating is applied by deposit without electrodes. The filter is coated with a metal, and the fibril is derived with a chemical functional group that forms a bond with said metal. The filter is a metal screen or a sheet of metal. The fibril mat may be flat or well deformed, regular or irregular, round, oval, rectangular, or of any of numerous shapes, rigid or flexible, transparent, translucent, partially or totally opaque and may have composite or composite designs. regions of different compound or individual properties. The mat can be a disc or a piece of a ho. A plurality of fibril mat may be manufactured, preferably, concurrently, and preferably in an assembly. In one example, a set of microfluidic guides forms a plurality of fibril mats in a support as described above. In another, a set of filters, or a filter configured (for example, with regions of different porosity) is used to prepare a set of fibril mats. A mask with a set of orifices (for example, a screen) is used to cover certain parts of a filter or support, and a plurality of discrete fibril mats are made concurrently either by filtration and / or evaporation. Fiber mats may have a density of 0.1 to 3.0 grams / c 2. The mat may have a variable density. For example, mechanical force or pressure can be applied to the mat at different times to increase or decrease the density. Fiberglass mats can have pores. These piaros can be extended partially and / or totally through the mat or they can be part of a network of pores. These pores can have dimensions that are located in general terms from 50 angstroms to 1000 μ. In a preferred embodiment, the fibril mat has pores with dimensions ranging from 200 angstroms to 500 angstroms. The porosity of the mat may depend on the density of the mat, among other factors. The porosity of the mat can be constant throughout the mat, it can be increased or decreased depending on the position on the mat. The fibril mat may have a wide variety of pores of different sizes distributed in a disorganized or random manner.

The fibril mat may contain different regions of different porosity. For example, the fibril mat may have one or several layers, each having a different porosity. Fibrillating mats may have columns of different porosity running through the mat. The porosity of the mat can vary by including different amounts of carbon fibril aggregates, where the aggregates have different sizes, shapes, compositions or combinations. In a particular example, a mat is prepared from individual fibrils, CC fibrils (described above) and BN fibrils (described above), or different combinations. Because of the location, the fibril mat may have some pores large enough to pass objections of the size of biological cells, some pores may pass through biological media of the size of protein to antibodies, some pores may pass only small organic molecules (with a weight molecular weight below 1000), and / or combinations thereof. The porosity of the mat can be of such magnitude that one or several molecules, liquids, solids, emulsions, suspensions, gases, ge > and / or dispersions may be dispersed in, in, and / or through the mat. The porosity of the fibril mat is such that biological media can be dispersed (actively or passively) or they can be forced by some means in, inside and / or through the mat. Examples of biological agents include, but are not limited to, whole blood, fractionated blood, plasma, serum, urine, protein solutions, antibodies or fragments thereof, cells, subcellular particles, viruses, nucleic acids, antigens, poprsteins, 11 postaccharides, lipids, glycoproteins, carbohydrates, peptides, hormones or pharmacological agents. The fibril mat may have one or several layers of porosity di ff erently such that a material may pass through one or several layers, but not through other layers. The fibril mat is supported by or on another material. By way of example, the support material can be a metal, plastic, polymer, elastomer, gel, paper, ceramic, glass, liquid, wax, oil, paraffin, organic solid, or a mixture of two or more of them. The material can be solid or liquid. If it is in a solid state, it may contain one or several holes or pores. In specific examples the support can be a metal mesh, a nylon filter membrane or a filter paper. The soup can be a conductor, semiconductor and / or insulator. In a modality presented in the North American Patents No. 5,304,306 and 5,098,771, fibrils can be dispersed in another material. For example, fibrils may be dispersed in oils, waxes, paraffin, plastics (eg, ABS, polyester, polyethylene, acrylonitrile, etc.), ceramics, teflon, polymer, elastomers, gel, and / or combinations thereof. Fibril dispersions in other materials are conductive. Fiber dispersions in other materials can be molded, pressed, formed, squeezed, spun, woven, and / or thrown in such a way as to form objects of a desired shape and / or configuration. The fibril mat may incorporate other material, for example thin fibers, fragments or metal balls. to increase the conductivity of the mat. In another example, the fibril mat can; incorporate other carbon, glass and / or metal fibers of varying sizes, shapes and density to create a different porosity that can be achieved with fibrous rooms. In another aspect, the mat can incorporate magnetic beads (for example, DYNAL accounts). In this last example, the accounts can either serve to change a property on the mat, or they can use themselves as supports to immobilize link domains. Other carbon fibers (for example, carbon nanostructures, carbon nanotubes, buckminsterful lenses, b? Ckytubes, fullerenes or combinations thereof) can be used in place of carbon fibrils. Carbon fibrils with chemical functional groups fixed covalently on their surface can be prepared. Camo is described in International Publication No. WO 90/14221, these chemical functional groups include, but are not limited to, COOH, OH, NH2, esters of N-hydro? Isuccinimide (NHS), poly i- (eti-legl icoles) , thiols, alkyl groups (CH 2) n), and / or combinations thereof. These and other chemical functions can be used to fix other materials on the surface of fibrils. Some chemical functional groups (eg, COOH, NH2, SH, NHS esters) can be used to connect other small molecules to the fibrils. There are many possible combinations of such chemical functional groups and small molecules. In many embodiments, ester groups of NHS are employed to fix other molecules or materials that carry a chemical functional group nueelaflies (eg, an amine). In a preferred embodiment, the nucleophilic chemical functional group is present in / or within a biomodula, either naturally and / or by chemical derivatization. Suitable bio-oleoplasm axes include, but are not limited to, amino acids, proteins and functional fragments thereof, antibodies, antibody binding fragments, enzymes, nucleic acids, and combinations thereof. This is one of many possible techniques and is generally applied to the examples given here and many other analogous materials and / or biomolecules. In a preferred embodiment, reagents that can be used for ECL can be affixed to the fibril by means of NHS ester groups. An antibody that can be used; in an ECL assay it can be fixed on one or more fibrils or a fibril mat by covalent bonds (for example, reaction with an NHS ester) by reaction with an appropriate linker (vide supra), by a specific na bond, and / or by a combination thereof. Nucleic acids and / or cells can be fixed; on fibrils to either fibril mats by covalent bonds with NHS ethers fixed on the fibrils. It may be desirable to control the magnitude of the non-functional bond of materials on fibrils and / or fibril mats. Simply by way of non-limiting examples, it may be desirable to reduce or avoid the specific adsorption of proteins, antibodies, fragments of antibodies, cells, subcellular particles, viruses, serum and / or one or more of their components, ECL markers ( for example Ru? (bpy) 2 and Rui 11 (bpy) 3 derivatives), oxalates, trialq? i laminae, antigens, analytes, and / or combinations thereof. In another example it may be desirable to increase the binding of the biaminoles. One or more chemical portions that reduce or avoid non-specific binding may be present in, in, or in the vicinity of one to several fibrils, one or several aggregates of fibrils, and / or a fibril mat. The non-specific binding is controlled by the covalent attachment of PEG portions on one or several fibrils and / or fibril mat. Charged residues, for example, phosphates, ammonium ions, can be fixed covalently on one or several fibrils or a fibril mat. Materials used in the support, electrodes and / or binding domains can be treated with surfactants to reduce the non-specific binding. For example, fibrils or fibril mats can be treated with well-known surfactants and / or detergents by a person with certain knowledge in the art (for example, the Tween, Triton, Span, Brij senes). The fibrils or fibril mats are washed, soaked, incubated, zoned and / or a combination thereof with patent solutions and / or detergents. Solutions of PEGs and / or molecules that behave similarly to PE (for example, oligosaccharides or polysaccharides, other hydrophilic oligomers or hydrophobic polymers) ("Polyethyi lene glycol chemistry: Bioteehnical and biomedical appl icans, (Chemistry of poly speak: bi-technical and biaedic applications) Harps, JM Editor, 1992, Plen? m Press) can be used in place of and / or in combination with surfactants and / or detergents. The specific binding of certain entities, such as those mentioned above, can be blocked by competitive specific adsorption.This competitive binding species can be immunoglobulin G (IgG) of bovine serum albumin (BSA). - CHANNEL can be reduced by chemical modification of the MARKER, for example, the MARKER can be modified to increase its hydrafiity, (for example by the hydrophilic hydrogen bond, pol ar and / or functional groups charged to the dipindyl ligands in R? (bpy3)) and consequently reduce the non-specific binding of the MARKER to another surface. It may be desirable and mobilize bia aléculas or else; media on fibrils or fibril mats. One can fix antibodies, fragments of antigens, proteins, enzymes, enzyme substrates, inhibitors, cofactors, antigens, hapten, lipoproteins, 1 icarcinoids, cells, subcellular components, cell receptor, viruses, nucleic acids, antigens , liquids, glycoproteins, carbohydrates, peptides, amino acids, hormones, protein binding ligands, pharmacological agents, and / or combinations thereof. It may also be desirable to use biological entities such as, for example, without limitation, polymers, elastomers, gels, coatings, ECL labels, active reduction-axification species (eg tripropy sheet, oxalates), inorganic materials, chelating agents. , linkers, etc. on fibrils). One or several of a plurality of species can be linked non-specifically (eg, adsorb) on the surface of the fibrils to either fibril mats. Biological molecules or other media can be fixed on fibrils or fibril estetrate by non-specific adsorption. The extent of the nonspecific adsorption r for any given fibril, fibril mat and / or biomolecule is > It will end with certain properties of each one. Certain chemical functional groups or biological portions present in fibrils can reduce or increase the specific binding. The presence of hydrophobic and / or hydrophilic parts on the surface of a protein can increase or reduce the nonspecific binding of the protein on fibrils or fibril mats. Hydrophilic and / or hydrophobic parts are used to control the specific binding in controlled areas. Fibrils can be derived from alkyl chains (CH2) and / or carboxylic acid groups to increase non-specific binding of biological molecules to media or other materials. Figure 26 illustrates the above embodiment schematically in the case of a single fibril. A fibril 2600 is derived with an alkyl chain 2601. Biomolecules 2602, 2603, and 2604 are non-specifically bound to the alkyl chains. It also links pol. 2605 elastomer / elastomer. Non-derived fibrils, fibril aggregates and / or fibril mats are used for the immobilization of biomolecules, biological means, and other materials by non-specific binding. The ECL MARKER contains charged waste. The ECL MARKER is made to be selectively attracted to a support and / or electrode. For example, a derived ECL MARKER having a net negative charge may have a relatively low affinity for an electrode at a more reducing potential and then have a higher affinity for an electrode as the electrode potential becomes more oxidizing. The affinity of the ECL label and / or the electrode binding reagent is elaborated to modulate, for example, to decrease affinity during binding and / or wash steps to increase the affinity of the ECL label and / or binding reagents to increase the. effective potential felt by him. ECL marker during an ECL reading. In Figure 28 molecules (both biological and non-biological) can be fixed on fibrils by means of a covalent bond. Fibrilas 2800 that carry chemical functional groups of NHS ester can form covalent bonds. 2801 with iornoléetelas or biological means 2802, 2803. These biological means can employ an amino group to form a covalent bond by reaction with the ester group of NHS. The polymer 2808 is immobilized. A person with certain knowledge in the art will recognize the generality of the NHS ester groups as coupling agents for molecules and will be able to select both the appropriate baryelic and appropriate reaction conditions to achieve immobilization. A pair of portion and / or molecules "MI" and "SI", of which one or more are fixed on a fibril, have a mutual affinity or a binding capacity. Ml / Sl can be antigen / antigen, antigens / hapten, enzyme / substrate, in? Ima / cafactor, enzyme / inhibitor, lectin / carbohydrate, receptor / hormone, receptor / effector, nucleic acid / nucleic acid, pratei na / nucleic acid, virus / ligand, cell / cell receptor, etc. Many combinations of "link pairs" Ml / Sl and you can select appropriate combinations to achieve the desired link. Either MI and SI or both MI and SI can be fixed on one or more fibrils. Figures 27 and 28 illustrate some of the many possible configurations with this modality. In Figure 27, a fibril 2700 derived with alkyl chains 2701 binds nonspecifically to a molecule 2702 that is: has a mutual affinity or a binding capacity for another molecule 2703. Molecule 2703 is also fixed on another molecule 2704. A blocking molecule 2705 p? ede? adsorbed specifically on fibrils. A blocking polymer 2706 and / or a polymer 2707 having a ligand (2708) having an affinity for a molecule 2709 are non-specifically adsorbed. In Figure 28, a fibril 2800 is covalently linked through 2801 to biamololecules 2802 and 2803, and a linker molecule 2804. Linker molecule 2804 has a mutual affinity or binding capacity for another biomolecule 2805. biomolecule 2803 has a mutual affinity or binding capacity for another linker molecule 2806, which is covalently linked to 2807. Polymer 2808 with a ligand 2812 specific for a binding partner 2809 is covalently linked to a fibril. Blocking molecules (eg, BSA) 2811 and blocking polymers 2810 are bound covalently. A fibril can be derived with biotin and / or a biatinylated linker and avidin and / or streptavidipa can bind to this linker. Avidin and / or streptavidin can bind to fibril, and a biatinylated antibody and / or proteins can be linked. The avidin and / or streptavidin can be immobilized in the fibrils either by specific nc bond, covalent bond, other coupling pair or the same coupling pair, or a combination thereof. The use of (strep) avidin and biotin as "binding pairs" is a widely applied method for fixing biomolecules or biological media on other materials and is well known to those skilled in the art (Sprinke et al., 1993, Langmuir 9: 1821). A binding pair can be a monaclanal antibody and an antigen that binds with this antibody. Multiple link pairs (for example, M1 / S1 / M2) can be formed. MI is a monoclonal antibody, SI is an antigen for MI, and M2 is an antibody that binds with SI. This complex may constitute a complex "sandwich" antibody / antigens / antigens (such antibodies can be monoclonal). M2 can be an antibody labeled with an active label for ECL (vide supra), a fluorescent label, a radioactive label, an epzymic marker, and / or combinations thereof. MY p? Ede could be a portion that can form complexes with a metal, metal ion, or orthano metal compound (a "chelating agent") and SI is a metal ion, a well composed organometallic (a "chelate"). ) that forms a complex with MI, and M2 is a portion in a biological molecule that binds with the Ml / Sl complex (Gershon and Khilko, 1995, Journal of Immunoal- gical Methods, 7371).

The fabrication of patterns of metal electrodes and conductive elements to decrease the electrical current to such electrodes on a surface is carried out by means well known in the art (see, for example, Leventis et al., US Patent No. 5,189,549). . The preparation of metallic films on transparent surfaces is used to produce liquid crystal displays and is easily adapted for the preparation of electrodes according to the invention. Haneko, 1987, 'Liquid Crystal TV Displays, Prineiples and Applications of Liquid Crystal Displays, KTK Scientific Publishers, Tokyo, D. Reidel Publishing. Transparent electrode surfaces can also be prepared, for example, in accordance with the method of DiMilla et al., 1994, J. Am. Chem. Soc. 116 (5): 2225-2226. 0.5 nm of titanium and 5 nm of gold are deposited on transparent substrates (glass or plastic). A thin layer of gold in accordance with that prepared by the DiMilla method, supra, can be used to prepare a transparent electrical structure by means of the Kumar method, supra. Modifications to this method to increase the thickness of the conductive layers for an increased capacity of current transport while preferably maintaining the transparency are desirable and apparent to the person with some knowledge in the art. Such techniques can be employed to prepare electrode surfaces that are aligned with discrete binding domain or in the vicinity of such domains of a PMAMS. In addition, the films and / or monalaps may be composed of portions that facilitate the transfer of electrical potential from the electrode surface to the ECL marker, instead of using insulating portions (eg, alkyl chains) in accordance with that presented. by Zhang and Bard. For example, an orbital web of pi in extensively conjugated systems can be used for transference of electrates. Such transfer of orbital electrons pi is provided by poly-pyral or other conjugated rings or double bonded structures. You can use ol. iganucleotides to modulate electron transfer. For example, pi-junctions in double-stranded DNA can be used to increase the electron transfer capacities. Oligonucleotides linked on an electrode surface can be used as a binding agent in a binding domain. When linking a oligonucleotide sequence sequence a double strand with an organized splice pi, bonds are formed. In a particular embodiment, an immobilized igonucleotide or primary oligonucleotide primer (eg, covalently bound to a support) is labeled for ECL. In another embodiment, a secondary secondary Igonucleotide or an Igonucleotide sequence partially complementary to the primary Igonucleotide is labeled for ECL. A tertiary oligonucleotide complementary or partially complementary to the secondary oligonucleotide ol is labeled (eg, a sandwich assay). It is also possible to use branched chains of the igonucleotides. A variety of oligonucleotides and / or oligonucleotide mimics can be used (eg, oligonucleotides with modified bases and / or modified structures containing eg nitrogen and / or sulfur). Differential studies can be carried out. The variable stability of the pi junction in oligonucleotides and / or oligonucleotide complexes can be monitored through electron transfer modulation. The signal (eg, generated ECL light and / or impedance measurements) generated by a pair of double-helical oligonucleotides labeled for pi-stabilized ECL can be correlated against the signal and / or the expected signal from a to the igonucléat gone of single more messy thread. The variation in the ECL signal between a double-stranded oligonucleotide labeled for fully complementary ECL and an ol. double-stranded igonucleotide labeled for partially complementary ECL can be correlated. Additionally, multiple oligonucleotide oligonucleotide complexes can be employed. For example, triple helices can be employed. The modulation of the electrode transfer rates can be measured using ECL detection as well as electronic devices. Markers for ECL can be covalently linked with strands of oligonucleotides and / or associated in a non-cavalent manner (eg, interspersed). DNA can be coupled to the electrode without the use of a linker (eg, 5 'adsorption of thiolated DNA in gold) to a short linker (less than 10 ta) to ensure low resistance to electron transfer of DNA towards the electrode. A link chain can be employed which can efficiently transport electrons from the electrode to the strand of DNA (eg, a polyacetylene chain). A mixed monolayer and / or film can be used in which at least one constituent of the monolayer or film, as the case may be, facilitates the transfer of the electrical potential. Finally, a molecule or particle that facilitates the transfer of electrical potential is adsorbed on the monolayer or film. With or examples of the foregoing, monolayers conjugated with and / or conductive microparticles which adsorb to and / or are close to the surface of the electrode may be employed. Regularly configured spaces are created in the monolayer and / or film. By using controlled patterns of spaces in a substantially ordered perpendicular SAM composed of long-chain alkanols (ie, insulator) to which ECL markers have subsequently been set, the effective potential imposed on the ECL markers can be controlled. For example, Figure 11 shows a cassette 1200 formed of a single soup 1202 with a metal layer 1204, a SAM pattern 1206 and spaces 1208 between the SAM standards. The proteins labeled for ECL can be covalently linked to a monolayer surface. A protein labeled for ECL can be adsorbed onto the surface of a gold surface derived with methyl-terminated alkanols. The gold surface can act with either the working electrode or the counter electrode. A plurality of link domain may be incorporated in a single support as shown in Figures 11-13. In preferred embodiments, the binding domains contain labeled and / or unlabeled proteins and / or nucleic acids and / or cells and / or chemical species. Alternatively, the length of the components of the monolayer (for example, the length of the alkane chain in the monolayers of alkynyl) can be varied to control the effective potential on the exposed surface of the monolayer In general terms, al.cantiol.es can have carbon chains of a length comprised between 1 carbon atom and 100 carbon atoms. In a preferred embodiment, the carbon length of the alkanol contains between 2 and 24 carbon atoms. The length of the carbon chain of the alkynyl is between 2 and 18 carbon atoms. The length of the carbon chain is between 7 and 11 carbon atoms. Such alkanols may have several head cores exposed to the test media including methyl groups, hydraxy groups, amines, carboxylic acids, oligo (ethylene glycol), phosphate groups, phosphoryl groups, biotin, acid or tri-lotic acid, glutathione, epoxides, dinitrophenyl, and / or NHS esters. Other head groups include ligands frequently employed for the purification and immobilization of recombinant fusion proteins (eg, Sassenfeld, 1990, TIBTECH 8: 88-93). The binding domains can be derived in various degrees to achieve variable densities of binding reagents. For example, different densities of activatable chemical agents can be used and / or derivations can be carried out in several measures. Mixed chemical elements can be used to create desired bond densities. Mixed monolayers can be used to control the density of activatable groups and / or binding reagents. The density of link groups is controlled by optimizing the relationship between the ECL signal and the noise. The total number of link sites within a link domain is controlled to optimize the strength of the ECL light signal relative to other ECL light signals. from other link domains such that ECL light signals are detected sequentially or simul- taneously and / or in relation to the light detection device. The voltage waveform can be applied to activate ECL markers associated with a binding domain within a PMAMS one or several times. An electronic potential sufficient to activate a generation of ECL light can be applied several times to the same surface derived from alkalyol with labeled ECL to generate multiple ECL light signals. An electronic potential is applied suffi- ciently to generate a reversibility of ECL. The potential is applied to generate an almost reversible ECL. In an almost reversible series of voltage waveforms, the eplace domain within which the ECL label is associated (for example, it is linked), can be chemically and / or physically altered. The waveform series of applied voltage can provide an irreversible generation of ECL light. In addition, sufficient electrical potential to release the components of the monolayer can be applied. It is desirable to release such monolayer components where the volume above the electrode surface is small (eg, another support or plate resting on the electrode surface). In this way, as the monolayer is disrupted, even some ECL markers that are not efficiently excited can be excited by the electrode surface to generate the electrochemiluminescent signal and the ECL markers are restricted to a small volume which restricts the infusion from of the electrode. Several monolayer compositions can be used to control the degree of disorder of the monolayer for a given potential. Mopocapas with components with a strong intercomponent affinity will be more resistant to the monocapta disorder. Longer chains of alcaptioles resist the disorder more effectively than short chains of alcantiols. By varying the length of the chain, the desired stability can be achieved. The modification of the link domains within a PMAMS can be used to modulate the ECL signal. A series of voltage waveforms is applied to generate a multiplicity of ECL signals. Such a multiplicity of ECL signals can be used to achieve extra and / or better results. A statistical analysis of the modulation speed of the ECL signal can be correlated with u; the global quality of a link domain or of several link domains. Additionally, said multiplicity of ECL signals can be used to increase the signal-to-noise ratio by, for example, filtering certain ECL signals of a series. In addition, multiple electron potential waveform pulses can be employed to reduce undesirable signal modulation due to non-specific binding. An electronic potential can be applied to avoid the non-specific binding of certain charged species. Additionally, the electronic potential can be applied to promote the location near a binding domain of certain analytes or chemical species of interest. The applied voltage waveform provides a large overpotential (eg, a potential higher than what is required to generate ECL). Overheating can be used to modulate the ECL signals in a series of voltage waves or in a single impulse of voltage waves. Additionally, overpotences can be used to modulate the kinetics of the ECL reaction and / or modulate the chemical-binding potential physically and / or physically. In addition, one or more voltage waveforms and / or other electronic probes known to those skilled in the art can be used to evaluate and / or correlate and / or extrapolate information regarding the quality and / or electronic properties of a electrode or several electrodes. Preferably, the efficiency of the ECL reaction can be increased by extending the surface area of the working electrode by providing an additional conducting device in contact with the electrodes. Projections or extensions from the electrode (for example, wiring or fibers) of conductive materials or conductive particles can be used to increase the. Surface area of the electrodes, in such a way that the electric field is closer to the ECL marker. Alternatively, indentations or wells in the electrode structures can serve the same purpose. Particularly, conductive particles can fill the spaces in the electrode surface and / or cover the monolayer support or in such a way that the electric field around the ECL marker is increased in proportion to its absolute magnitude, as shown in Figure 12 These conductive particles extend the surface area of the electrode and therefore increase the efficiency of the ECL reaction. Figure 12 shows a cassette 1300 having a biscuit 1302 carrying a SAM 1306 configured in a metal layer 1304 and indicating conductive microparticles that fill the spaces (eg, 1208 in Figure 11) and which extends above the surface between the SAM configurations. In the case of magnetic conductive particles, a magnet or magnetic field can be used to attract the particles to the surface. The conductive particles can also be used in accordance with that described to extend the electrical potential between the electrode surfaces and the binding domain of a PMAMS with two approximate supports. In Figure 8, cassette 900 consists of a first biscuit 902 having a multiple set of electrodes, and a second holder 904 having a PMAMS. Conductive microparticles 906 are positioned between the opposing surfaces to extend the electrical potential towards the ECL marker in the link domains (not shown). Alternatively, conductive copalmers grow from the spaces exposed on the surface of the electrodes to facilitate the extension of the electrical potential around the ECL marker of the sample as shown in Figure 13. Figure 13 shows a cassette 1400 having a support 1402 carrying a metal layer 1404 on a configured SAM surface 1406. Conductive polymers 1408 grow on the SAM surface to extend the electric field provided by a single set of electrodes (not shown) to link domains (not illustrated) on the SAM surface. The conductive polymers can also be employed as described to extend the electrical potential between the electrode surfaces and the binding domains of a PMAMS of two approximate supports as illustrated in Figure 7. In Figure 7, the cassette 800 consists of approximate supports 802 and 804. Copol conductive monomers 806 grow between the opposing surfaces to extend the electrical potential towards the ECL marker in the binding domain (not illustrated). Figure 9 illustrates a cassette 1000 formed with a first support 1002 having a multiple electrode arrangement, a second support 1004 having a PMAMS link surface, where conductive projections (1006) (e.g., thin wire or other protuberances) of the working electrode extend the electric field around the ECL marker in the binding domains of PMAMS. The pairs of electrodes can be created in various configurations. The simplest configurations, presented in the figures accompanying this presentation, are made of metal and / or metal oxide film and / or semiconductor films applied on a non-conductive flat surface. The electrodes of these pairs of electrodes preferably define a region of relatively constant width between them thus providing a fairly constant electric field. Other configu- rations of the electradas are provided. Several of these configurations appear in the lists in 11" plant in figures 19 (a) - (e). Figure 19 (a) shows a pair of electradas in the form of an interdigitated comb 1. In this structure, each electrode has a plurality of fingers that extend from the conductor which creates a comb shape. The electrode and counter electrode pair can be positioned adjacent to a binding domain, or a link domain can be positioned between an electrode and counter electrode. Figure 19 (b) shows a pair of concentric electrodes, one circular and one semicircular. Figure 19 (c) shows two semicircular electrodes with their edges straight in front of each other. Figure 19 (d) shows a pair of rectangular electrodes. Figure 19 (e) shows a pair of interdigital electrodes having complementary opposite curved surfaces to form an unused path between the las. Electrode / contract! Ectrode pairs can also be formed into specific complementary forms of shapes on the PMAMS bond surface for alignment purposes. Exemplary forms appear in Figure 6B. A support 712 is shown carrying pairs of electrodes 714-720. The electrode pairs may be, for example, circular 714, interdigitated 716, triangular interdigitization 718 or interdigitization of multiple electrodes 720.

In the modalities shown in figures 14-19 presented above, the pairs of electrodes are located on a single support. Alternatively, the pairs of electrodes are located in a first support and a second opposite support as shown in Figure 2. 5.8. CASSETTES Cassettes contain one or more supports of the invention. The cassettes may include a plurality of link domains and one or more working electrodes. Figure 2 presents a cassette where each of several link domains 30 in support 26 are adjacent to an electrode different from the several electrodes 32. Csntra electrodes 38 are formed in a second support 28. An ECL assay is carried out as required. previously described by placing a sample in link domain 30 and then by shifting together these supports 26 and 28 in such a way that the counter electrodes 38 are adjacent to each of the link domains 30 and an ECL reaction can be triggered in accordance with that described above by a waveform generating device 39, through a conductor 34, and a detected ECL signal recorded by a light detecting device 40, cable 41, and digital computerized device 42. Figure 3 illustrates a cassette where each of several link domains 48 have a different pair of several electrode / counter electrode pairs 50 adjacent thereto in support 44. Support 46 can optionally be placed adjacent to support 44 in such a way The support 46 forms a device containing sample adjacent to several link domains 48 and several electrodes 50. Accordingly, an ECL reaction can be triggered by electrical connection 52 by a waveform generating device 54, and a sign of ECL detected by light detecting device 56 and recorded and analyzed by a digital computing device 58. A cassette is provided that contains one or more pairs of supports as shown in Figure 21, each support pair being located in; such that the surface of a first support 1501 containing binding domains faces the surface containing binding domains in the second support 1502, wherein each surface contains electrodes 1504 and binding domains 1506; such that each binding domain in the first support faces and is aligned with an electrode in the second support, and each binding domain in the second support faces and is aligned with an electrode in the first support. Figure 4 illustrates a cassette where the ECL electrodes are optional. Link domains 64 in support 60 are in contact with a sample of which is suspected to contain an analyte. Regions 66 in support 62 contain reaction medium to detect either measuring an analyte of interest or to carry out a desired reaction. Port 60 and 62 are brought together in such a way that the link domains 64 and regions 66 are in contact and the presence of an analyte or reaction product is determined by means of a reporter system, for example, a calorimetric or fluoroscent chemistry-luminescent signal r can be detected by photodetector device 60 and recorded and analyzed by digitized computing device 70. In a preferred embodiment, a cassette or apparatus of the present invention comprises a device for supplying samples in the plurality of discrete link domains (see, for example, element 1 in Figure 1 of U.S. Patent No. 5,147,806; Element 1 in Figure 1 of U.S. Patent 5,068,088; each of which is incorporated by reference in its entirety). The device for the delivery of the samples can be a stationary or mobile device and can be any device known in the art, including without limitation one or more entrances, orifices, pores, channels, ducts, microfluidic guides (for example, capillaries). ), tubes, taps, etc. The fluids can be moved through the system by several well-known methods, for example: pumps, pipettes, syringes, gravity flow, capillary action, wicking, electrophoresis, pressure, vacuum, etc. The device for the movement of fluids can be located in the cassette or in a separate unit. The sample can be placed in all the link domains together. Alternatively, a sample may be placed in particular binding domains by a capillary fluid transport means. Alternatively, samples may be placed in the monitor by means of an automatic pipette control device to deliver fluid samples directly to the PMAMS on a stand, or in a reservoir on a cassette to a good cassette holder for delivery back directly to the bond surface. Brackets can be prepared from materials including, without limitation, glass, plastic, ceramics, palmeric materials, elastomeric materials, metals, carbon or materials containing carbon, alloys, composite sheets, silicone and / or layered materials. The supports can have a wide variety of structural, chemical and / or optical properties. They may be rigid or flexible, pianos or deformed, transparent, translucent, partially or totally reflective or opaque bodies and may have composite properties, regions with different properties, and may be a composite of more than one material.

Reagents for carrying out assays can be stored in the cassette and / or in a separate container. Reagents can be stored in a dry and / or wet state. In one embodiment, dry reagents in the cassette are rehydrated by the addition of a test sample. In a different mode, the reagents are stored in solution in "blister packs" that open due to the pressure coming from a moving roller or piston. The cassettes may contain a waste or sponge compartment for the storage of liquid waste after the test is completed. In one embodiment, the cassette includes a device for the preparation of the biological sample to be tested. It is possible to include a filter to remove cells from the blood. In another example, the cassette may include a device such as, for example, a precision capillary for the measurement of a sample. The plurality of linking domains and the plurality of electrodes / counter electrodes in the supports are typically placed in a corresponding proximity to each other by mechanical means, by the use of guide posts, alignment pins, hinges (between each support) or edges. of gluttony The optical guide device can be used to position both supports and electronic devices using optical guide marks defined on the supports. Other systems that use electrical adaptation devices; or magnetic are also available. The cassette holders can be configured to protect the electrode pairs from contact with the sample until it is required to trigger an ECL reaction. For example, the electrodes can be kept separate from the surface of the binding domain until contact of the electrodes with the sample is required by the use of various mechanical devices such as, for example, removable electrode protection device. A cassette or apparatus of the present invention comprises reference electrodes, for example, Ag / AgCl or a saturated calomel electrode (SCE). The supports can be held together by means of clips, adhesives, rivets, spikes or any suitable mechanical fixation. It can also be held together by the surface tension of a liquid sample or by a compression device placed remotely on opposite sides of the two supports. The cassette may also comprise more than two supports with, for example, alternative layers of binding domains and electrodes on multiple supports that both comprise a bonding surface and an electrode surface on a single support. This will form a three-dimensional set of ECL analysis cells. All the previous components of the cassette are transparent, except, optionally, some areas between the link domains. For example, multiple transparent bonding surfaces, electrode surfaces, and supports can be stacked. The first support and the second support can be flat and opposite to define a volume that contains the sample between them. Alternatively, the first support layer and the second support layer may be formed into other suitable shapes including spheroidal, cuboidal, cylindrical shape, provided that the two supports, and the other components thereof, conform in form. For example, Figure 10 shows a cassette 1100 formed of two sockets 1102 and 1104 na adjacent planks. Each support has a surface complementary to the other in terms of conformation. Each soup can have a surface of PMAMS or a set of multiple electrodes or both. One or both supports can be elastomeric to conform to the shape of the other support. The supports or cassettes may also be prepared in a pre-cut format, or supplied in a suitable length from a supplier of rails. The cassette may further include a device for receiving samples such as for example a volume which receives a sample and slots, channels, indentations and the like for sample distribution. Figure 37 shows a cassette in which link domains (3702) in and / or on a matrix (3703) are presented on a surface (3701). A second surface <3700) that supports a working electrode (3704) and a counter electrode (3705) is positioned in such a way that the link domains are close to the working electrode. Ba o Ganditions that lead to the generation of light from the ECL marker linked to the link domains, light can be detected through any of the surfaces or both surfaces. A set of light detectors (3706, for example, a CCD array, an intensified CCD array, or an avalanche photodiode array) is used to measure the plurality of light signals from each of the domains. of link. The set of light detectors provides an image of the light generated from the link domains. Lenses, reflectors and / or optical guides can be used »to increase the image. In other examples, light detected from regions or regions of light detectors (e.g., a light that detects pixels (s)) correlates with one or several link domains. An image analysis can be used to help correlate the detected light with the link domains. In a preferred embodiment, the surface is elastomeric or deformable and can therefore establish intimate contact with the electrode surfaces. The binding domains are linked to polymers capable of carrying ionic currents from the counter electrode towards the working electrode. In a more preferred embodiment, san polymeric objects swollen in water capable of carrying an ionic current from the counter electrode to the locking electrode. Figure 38 shows a cassette in which the link domains (3805, 3806, 3807) are presented on the surfaces of different objects (3808, 3809, 3810) supported on the counter electrode (3800). A working electrode (3801) is placed in the vicinity of the surface of the objects. Ba or conditions that lead to ECL from labeled groups linked to the binding domains, light can be detected through any of the electrodes or both electrodes (if one or both electrodes is transparent or semi-transparent) and / or the side. A set of light detectors (3802) is used to simultaneously measure the plurality of light signals from each of the link domains. The objects can be elastomeric and / or deformable and can therefore form an intimate contact with the working electrode. The objects can be polymers capable of carrying ionic currents from the counter electrode to the working electrode. The objetos can be polymers swollen in water capable of carrying a 12 ionic current from the counter electrode towards the. working electrode. A transparent substrate containing one or more binding domains comes into contact with a fibril mat electrode. The reagents can flow either between the binding domains / supports and the fibril mat, or through the mat to the binding domains. The light can pass from the link domains, through the transparent support to a detector. In another preferred embodiment, an electrode is coated with an optically translucent or transparent layer of carbon fibrils, to increase the effective surface area of the electrode. Advantageously, the PMAMS supports and / or cassettes of the present invention can be tested in the form of sets of elements. The set of elements comprises one or more supports of PMAMS prepared in accordance with the present invention to carry out ECL reactions including tests, controls and the like. Reagents may optionally be included in the set of elements, including control reagents, ECL assay and calibration reagents and the like. A mixture of reagents may be included which contains a plurality of specific binding reagents for a plurality of different analytes. . 9. APPARATUS FOR CARRYING OUT ECL REACTIONS In one embodiment, the PMAMS in sopo is, and cassettes containing the same, are designed to be inserted in an apparatus, which contains a device for applying one or more test samples in the domains of PMAMS link and initiate a plurality of ECL reactions. Such an apparatus can be derived from conventional apparatus suitably modified in accordance with the present invention to carry out a plurality of ECL tests based on a support or cassette. The invention provides various apparatuses adapted to carry out ECL assays using each of the specific methods of; PMAMS described in the previous sections. Zoski et al. (U.S. Patent No. 5,061,445) present an apparatus for carrying out ECL reactions. Required modifications include the provision of support and / or cassette handling, provision of multiple samples, multiple electrode exchange by a source for a voltage waveform and acquisition and processing of several ECL signals. Illustrative apparatus elements in accordance with the present invention appear in Figure 6A. Such an apparatus 700 comprises upper and lower supports 702, 704 and an electrode shield 710. The upper saver carries a plurality of electrode / counter electrode pairs (not shown). The lower support carries the link domains 706. The apparatus can remove the electrode protection of the cassette and position the electrode / counter electrode pairs to contact the bound analyte in the link domains. A reagent or fluid flow space 708 is adjacent to the support carrying the link domains. The apparatus may also simultaneously or sequentially send an identical or individually determined voltage wave to each of the plurality of pairs of; electrode / counter electrode to trigger ECL reactions in the cassette and then measure the emitted ECL radiation, by means of a photon detector, for example, a light detector device. The apparatus may further comprise a temperature control device for maintaining the temperature of the support and / or cassettes, or the. environment there and to adjust the temperature as required to optimize the ECL reaction conditions. The temperature control devices are preferably a heating and cooling device, for example, electrical resistance heating elements, cooling fans, cooling devices, and any suitable source of heating or cooling. The temperature control device also includes temperature sensors, for example, a thermostat or thermocouple device, and devices for turning on and off the heating device or the cooling device in response to detected changes in temperature. The aparata offers; also a device for holding, moving and manipulating one or several supports or cassettes to carry out the ECL reactions. The apparatus may further comprise a stationary or mobile sample delivery device for placing a sample in the PMAMS binding domains, in accordance with that described for the above cassettes. The apparatus may comprise an electrode contact device capable of electrically connecting the set of steerable electrode connections separately from the cassette to an electronic voltage waveform generating device, for example, a potentiostat (see for example FIG. of U.S. Patent No. 5,068,088). The waveform generating device delivers signals sequentially or simultaneously to independently trigger a plurality of ECL reactions in the. cassette During an ECL test, an ionic current between the working electrode and the counter electrode can flow through ionically driven liquid (e.g. water containing ionic salts), through a thin film of such liquid, and / or through an ionically conductive solid matrix. Accordingly, an apparatus for measuring the electrochemi-luminescence in a sample may comprise a plurality of cells to contain at least i? to. shows, where a cell can be formed from one or more electrodes and one or more counter electrodes and a first support comprising a plurality of discrete link domains. The electrodes and counter electrodes may be provided on the surface of the first support or on the surface of a second support where the second biscuit is in close proximity to the binding domains on the first support. The electrodes and cantraeleeves can occur in pairs. The cell may further comprise a plurality of censoring electrodes for detecting the. voltage adjacent to the work electra. The cassette may further comprise a cell containing a reference electrode. The apparatus further comprises a light detecting device that can detect ECL reactions carried out in the cassette, for example, by a detector device or by several detector devices. Such detector device includes, simply by way of example, a set of fiber optic channels in correspondence with the set of adjacent electrodes and passivated there, connected to a set of photodetector devices, or to a single light detecting device that can; explore the set of ECL signals as they are issued. The apparatus comprises apcionally a digital computer or a microprocessor to control the functions of the various components of the apparatus. The apparatus also comprises a signal processing device. In one embodiment, and simply by way of example, the signal processing device r comprises a digital computer for transferring, recording, analyzing and presenting the results of each ECL test. Alternatively, the apparatus comprises an electrode translation device, for example, for scanning one or more electrode / counter electrode pairs through the link surface to trigger ECL sequentially. Size exclusion filters can be used in a parallel set of PMAMS. 5.10. ECL TESTS THAT CAN BE CARRIED OUT ECL markers for use in accordance with the present invention can be selected from ECL markers known in the art (see section 2.2, above, US Patent No. 5,310,687). The ECL label can comprise, for example, an organic compound containing metals, where the metal is selected within the 13; group consists of ruthenium, osmium, rhenium, iridium, radium, platinum, palladium, molybdenum, tecnetium and tungsten. Suitable chemical bonding reactions for preparing ECL marker reagents are well known in the art, and presented, for example, by Bard et al. (US Patents Nos. 5,310,687 and 5,221,605). The ECL label binding device on a binding reagent can be covalent and / or covalently covalent. An ECL label can be linked in a non-cavalry manner with a binding reagent (for example, by hydrophobic effects or ionic interactions). In other examples of non-covalept fixation, ECL marker (s) are linked. { covalently or pa covalently) on a complex which is in turn non-covalently bound to a binding reagent. A more specific example would be the covalent attachment of Ru (bpy) 3 through a linker with a complex of Ni (11) -trini trilatriacetic acid. This molecule is fixed on binding reagents that include a sequence of peptides that contain a plurality of his id ies. Other pairs of receptor ligands are known in the art and can be used similarly (Sassenfeld, 1990, TIBTECH 8: 88-93). In addition, a marker of ECL can be used which contains a multiplicity of organometallic compounds (for example containing Ru) configured as a branched network (for example, through a network of hydrocarbon linkers). Such branched networks containing a multiplicity of organometallic portions capable of ECL can be fixed once or fixed in a plurality of positions in a molecule to be labeled for ECL. In another embodiment, the ECL label containing a multiplicity of compounds organometallic is a linear polymer with the organometallic groups fixed in a plurality of positions along the length of the polymer chain (for example, linear, branched or cyclic polymers). A plurality of binding domains can be employed in a variety of additional ECL assay formats well known in the art. In quantitative assays, a known amount of labeled reagent for ECL is employed and the amount of ECL. measure correlates with known standards to calculate the amount of analyte present. Direct, inverse, competitive and sandwich tests can be carried out by methods well known to those skilled in the art. In the case of competitive assays, for example, a method for quantitatively determining the amount of an analyte of interest in a multi-component liquid sample volume is performed in the following manner. The binding surface comes into contact concurrently with (a) a known amount of a labeled ligand for ECL that can compete with the analyte of interest for binding with a piresent binding reagent in the binding domains, and (b) sample of which it is suspected that it contains the analyte of interest; contacting is effected under appropriate conditions such that the analyte of interest and the ligand bind competitively with the binding reagent. The presence of the analyte in the sample will reduce the amount of ligand labeled for competitor ECL that binds to the binding domain, network like this (compared to the level, when no analyte is present in the sample) the resulting amount of ECL. The ECL. in the resulting binding domain it is triggered and the amount of light emitted is determined quantitatively, thus quantitatively determining the amount of the analyte of interest present in the sample. Alternatively, the sample may be in contact with the binding surface before the binding surface comes in contact with the ligand labeled for ECL; the ligand labeled for ECL will then compete with the previously bound analyte from the sample on the surface of PMAMS and displace some of the previously bound analyte. In an alternative embodiment, the sample can be treated in such a manner as to capture substances / molecules that are labeled for ECL, and a standard amount of analyte of unlabeled interest can be in contact with the interface surface; before or concurrently with the contacting of the interface surface with the sample to carry out a competition test. In a sandwich assay, the labeled ligand for ECL is a binding element that specifically binds to a second binding portion in it. analyte of interest. Therefore, when the analyte that binds specifically to a binding reagent in the binding domain of a PMAMS is present in a sample, a "sandwich" is formed, which consists of the binding reagent in the domain of link, linked to the analyte from the sample, linked to the corresponding part of the link marked for ECL. In another competitive sandwich assay, copies of the analyte itself are fixed on the binding domains of the multiple-set bond surface prior to exposure to the sample. The sample then comes into contact with the bonding surface. A labeled linkage for ECL (which can bind specifically to the analyte) will bind to the analyte in the absence of free analyte (from the sample) in the assay solution, but will be competitively inhibited in the presence of free analyte (from the sample ) in the test solution. In modalities to the ernativas, a sequential dizziness is carried out. For example, in a particular modality of a sandwich assay, the analogous link to the link domain se- lectially contacts a plurality of link partners marked for ECL. of the analyte. The ECL measurements and the optional washing steps are carried out between the contacts with each different link partner. In this way, an ECL measurement of several different binding portions of an analyte (e.g. CD8 +, T cell antigen receptor positive for T cell a, b) can be made. Additionally, ECL markers. multiple, each emitting light at a distinguishable wavelength can be linked to a different binding reagent specific to a different portion in an analyte. In addition, a plurality of distinguishable reporter devices (eg, ECL marker, fluorescent label and enzyme linked label) each fixed on a different binding reagent specific for a different binding portion of an analyte can be used, for example, for distinguish a CD4 +, a positive cell for T cell antigen receptor a, b from a CD8, cell positive for T cell antigen receptor a, b. As two binding domains contain labeled proteins and / or nucleic acids and / or cells and / or chemical species. Such labeled components (eg, labels for ECL can be added to the binding domain during manufacturing, before the start of the assay, during an assay and / or at the end of an assay.For example, multiple labeled components can be added at various times and Sequential readings can be taken, such readings can provide cumulative information.In atra mode, the binding domains of the PMAMS can be reused several times.After a given trial, the surface can be washed under conditions that reduce the activity of a binding domain or of several binding domains on the surface of PMAMS For example, some binding reactions can be reversed by changing the ionic strength of the reaction solution. dissociate link structures Some link domains can be inherently self-renewing Link domains containing Catalytic features (eg, enzymatic) can be used more than once. The binding domains are used continuously, and therefore can be used in biocenter applications. Aditionally, the. The test can be set up in such a way that the binding reagent fixed on the surface configured with multiple fixes is marked for ECL. By linking certain analytes of interest in a sample, the ECL signal will be modulated quantitatively. For example, the labeled binding reagent for ECL fixed on the surface may be specific for an analyte on a cell surface, plate axis, antigens such as for example antigens of alpha-T cells, receptors, or biep aptigens of CD4 to CD8. When exposed to a mixture of cells, the cells bound on the surface will sterically prevent the ability of an electrostatic surface, approached to a multi-stipulated surface of multiple arrays, to excite the eplace reagent labeled for ECL thereby regulating descending the signal, of ECL. Homogeneous and heterogeneous assays can be carried out. In heterogeneous assays, the unbound labeled reagent is separated from the bound labeled reagent (eg, by a washing step) prior to the exposure of the labeled reagent bound or unbound to an electrical potential. In homogeneous assays, the unbound labeled reagent and the linked labeled reagent are exposed together to an electrical potential. In homogeneous tests, the intensity or the spectral characteristics of the signal emitted by the linked labeled reagent is either greater than the intensity of the signal emitted by the labeled reagent unbound or lower than said intensity. The presence or absence of linked and unlinked receptive components can be determined by measuring the difference in intensity. Once the desired steps of contacting the binding reagents with the analyte or competitor thereof and any binding partner have been completed, it is then ensured that the ECL marker is subject to an environment conducive to ECL. . Suitable ECL assay means are known in the art. Such a test medium preferably includes a molecule that promotes the ECL of an ECL label, including, but not limited to, oxalate, NADH, and with a higher degree of preference tripropyl sheet. Such a "promoter" molecule can be supplied free in solution, or it can be provided by means of a link during production in (for example, as a product of a chemical reaction) the surface of PMAMS, a monolayer on the surface, the binding domain , the electrode surface, a binding reagent, and / or an ECL marker, etc. If the environment surrounding the ECL marker attached to the link domains resulting from the contacting steps is conducive to ECL, no media change is required. Alternatively, the medium can be adjusted or replaced to provide an environment conducive to ECL. An electrode and counter electrode are already in the vicinity of the link domain, either approaching or contacting the link domain, applying a voltage waveform, and detecting or measuring the ECL. Preferred embodiment of the invention, the steps described above of contacting the reagents binding the analyte to a competitor thereof and any binding partner thereof are carried out in the absence of electrodes and counter electrodes, ie of such that the sample is not in contact with the electrode or counter-electrode. Subsequent to these contacting sample steps, the electrodes and counter electrodes are sufficiently close to the ECL tag attached over the binding domain to trigger an ECL reaction. A support having a PMAMS can be used to sequence nucleic acid strands. For example, a PMAMS with a plurality of binding domain is prepared with different oligonucleotide probes of known sequence of nucleotides as binding reagents in different binding domains. That is, d? Fe >These binding domains will contain different known nucleotide sequence binding reagents. The chain of the igonucleotides or fragments of the oligonucleotide chain can be sequenced and then left bound (hibpdar) with the binding domains of PMAMS. The nucleic acids to be sequenced are labeled for ECL. The binding assays are carried out in the PMAMS and the distribution of the ECL signals of the discrete binding domains in the PMAMS is used to sequence the oligonucleotide chain. The method described above is based on the ability of short oligonucleotides to hybridize with their complementary or substantially complementary sequence in another nucleic acid molecule (see, for example, Strezoska et al., 1991, Proc. Nati. Acad. Sci. USA 88: 1089-1093; Bains, 1992, Bio / Technalogy 10: 757-58, which are hereby incorporated by reference). You can select conditions in such a way that the. The desired degree of sequence complementarity is necessary for successful hybridization. Hybridization of a DNA molecule of unknown sequence with a probe of predetermined sequence detects the presence of the complementary sequence in the DNA molecule. The method is preferably practiced in such a way that the hybridization reaction is carried out with the oligonucleotide probes linked to the binding domains and the sample DNA in solution.

A PMAMS can also be used to isolate, sift and / or select a novel molecule or a complex of desired function (e.g., linkage or catalysis). A PMAMS can be used to isolate compounds and / or carry compounds for therapeutic uses. A PMAMS containing a plurality of peptides, nucleic acids, viral vectors, or polymers, synthesized by a variety of combinatorial chemistries can be made using the methods of the present invention. A large variety of such treated supports for PMAMS can be used to screen rapidly to determine, for example, the binding to a cell receptor labeled for ECL. In one method, a PMAMS with a large diversity of unrelated peptide sequences is used to isolate the leader link peptide sequences. Then, a PMAMS is used with peptides from sequences related to those that showed binding to the molecule of interest (eg, a cellular receptor) in the first PMAMS. The process is repeated until a peptide with the desired binding characteristics is found . An analyte of interest may be, for example, an entire cell, a subcellular particle, virus, prion, viroid, nucleic acid, protein, antigen, 1 ipoprotein, 1 ipapol isaccharide, lipid, glycoprotein, carbohydrate moiety, derivative of cellulose, antibody or fragment thereof, peptide, hormone, pharmacological agent, cell or cellular components, organic compounds, biological polymer, synthetic organic molecule, organometallic compounds or an inorganic molecule present in the sample. The sample can be derived from, for example, a solid, emulsion, suspension, liquid or gas. In addition, the sample can be derived from, for example, body fluids or body tissues, water, food, blood, serum, plasma, urine, feces, tissue, saliva, oils, organic solvents or air. The sample may comprise a reducing agent or an oxidizing agent. Tests to detect or measure the following substances can be carried out by the present invention by incorporating a specific binding reagent for said substances in the binding domains of the binding surfaces of the invention: albumin, alkaline phosphatase, alt / SGPT, ammonia, amylase, AST / SGOT, total bilirubin, used nitrogen of blood, calcium, carbon dioxide, chloride, total cholesterol, creatinine, GGT, glucose, HDL cholesterol, iron, LDH, magnesium, phosphorus, potassium, prstein total, sodium, triglyceride, uric acid, drugs of abuse, hormones, modulators of the cardiovascular system, tumor markers, antigens of infectious disease, antigens that cause allergies, immunoproteins, cytokines, anemia / metabolic markers, carbamazepine, digoxin, gentamicin, lithium, phenobarbital, phenytoin, ida procaine, quinidine, theophylline, tobramycin, valproic acid, amphetamines, an idepresi ve, barbiturates, benzodiaz epinas, capabinoides, cocaine, LSD, etadona, metac lona, opiates, fenelindina, fropo ifena, ethanol, salicylate, acetazone, estradiol, progesterone, testosterone, hCG / bhCG, follicle stimulation hormone, luteinizing harmony, prolactin, thyroid hormones such as thyroid stimulation hormones, T4, TUP, total T3, free T4, cortissl, creatinine kinase-MB, total creatinine kinase, PT, APTT / PTT, LD ISOs, creatine ISOs or nq? nasa, myoglobin, chain of mioluz, troponin 1, troponin T, chlamydia, gonorrhea, herpes virus, Ly disease, Epstein Barr virus, I9E, Rubella-G, Rubeala-M, CMV-G, CMB-M, toxo-G, toxo- M, HBsAg (surface antigen of hepatitis B virus > , HIV 1, HIV 2, anti-HBc, anti-HBs, HCV, anti-HAV IgM, anti-HBc, anti-HAV, HBeAg, anti-HBeAg, TB, specific antigen of the prostate, CEA, AFP, PAP, CA125, CA15-3, CA19-9, microglob? Li na b2, hemo lobulin, red blood cells, HBcAb, HTLV, ALT, STS-syphilis, ABO blood type antigens and other blood type antigens, omeg lovi rus, ferritin, B-12, falate, glycated hemoglobin, amphetamines, antidepressants and other p icotropic pharmaceutical products. The ECL measurements in different binding domains can be carried out sequentially or simultaneously. A PMAMS specific for an analyte of interest which is a cell surface protein is first exposed to a sample containing cells, where it is desired to count the cells in the sample. In a preferred embodiment, a known and / or diluted sample volume is exposed to a PMAMS having a multiplicity of binding domain specific for at least one cell surface antigen. The linked cells can then be quantified by the fi xation of a secondary linking group linked to an ECL label. It is a group capable of interacting with a wide range of cell types, for example, a marker of ECL linked to a hydrophobic group capable of inserting itself into a cell membrane or onto a cell directed against cell surface sugars. The ECL tag is ligated onto a secondary antibody directed against a cell surface antibody. In a more specific embodiment, vain cell types linked over the same domain can be distinguished by the use of multiple secondary antibodies labeled with ECL. It is preferred to ensure that the number of discrete binding domains that were spiked for a given analyte on the surface of a cell exceeds the average number of cells that will bind that are present in the sample. Statistical techniques can then be used to determine the number of cells per sample volume. This technique can also be used, for example, to count other particles such as for example virus, wherein the binding reagent recognizes an antigen in the virus. The domains can be small compared to the size of a cell in such a way that only one cell can be linked by domain, thus leading to a digital signal for cad ^. domain that can then be analyzed in the sum of the domains using statistical methods. The domains are large compared to the size of the cell in such a way that multiple cells can bind with one domain. In this case, the signal level from each domain can be calibrated to provide the number of cells per sample volume. An image analysis using a set of lumen detectors (for example, a CCD camera a b in a set of avalanche photodiodes) could be used to count cells and determine cell morphologies. The invention also preferably offers methods for carrying out ECL reaction, eg tests, at a rate of 1000 ECL reactions in a period of 5 to 15 minutes. 5.11. PMAMS FOR USE WITH OTHER ANALYTICAL AND / OR ECL METHODS The techniques described for ECL-based detection can be used in combination with other assay techniques, for example, as domains where catalysis and other chemical reactions occur. Discrete binding domains in accordance with the present invention can be used in other assay techniques, for example chemistry to chemistry chemical assays, eg electrolyte determinations, clinical enzyme determinations, blood protein determinations, glucose determinations, urea and creatimna, and the like. Other assay techniques that can be combined with ECL assays and / or used alone with the PMAMS of the present invention include labeling based on chemistry iniscenci, fluorescence based assays, enzyme linked assay systems, electrochemical assays, see, for example, Hickman et al., 1991, Science 252: 688-691) and / or resonance detection test systems for example, acoustic technique and super plasm). Supports of PMAS can drops can be used in the cells there is a plurality of different chemical elements within the set of drops. Each drop may contain different binding reagents and / or different chemical tests (ie, reaction medium for it). For example, the droplets may be hydrophilic, leaning on hydrophilic surface binding domains surrounded by hydrophobic surface regions. The drops are protected by a hydrophobic solution that covers the top. The hydrophobic solution to be tested is suspended in a second PMAMS with hydrophobic linking domains surrounded by hydrophobic regianes. The two surfaces are correspondingly accepted to prevent contact of the hydrophilic domains on the apiuetas surfaces and a esptectral analysis is carried out to detect the products of the reaction of the chemical tests. The fibril mats may be such that there is a plurality of discrete hydrophobic and / or hydrophobic domains surrounded by hydrophilic and / or hydrophobic domains. Drops of aqueous solutions containing binding reagents can be supported in hydrophilic regions and be limited by adjacent hydrophobic regions. These drops may contain, for example, fibrils, aggregates of fibrils, reagents of; linkage, ECL reagents, reagents for assays, surfactants, PEGs, detergents, a plurality of biological molecules mentioned above for example, and / or combinations thereof. The hydrophobic solution that covers the first PMAMS is removed in a controllable way (by pillar axis, it evaporates, it is satiated to wicking process) to expose only a part of the hydrophilic drops in the upper parts towards the environment. A hydrophilic solution to be tested for an optimal chemical reaction is then exposed to the surface of the PMAMS - the hydrophilic microgags and the solution to be tested is mixed and the analysis is carried out (for example, spectral). The binding domains of PMAMS can also be used as a prefilter with a good filter. For example, a cellular specific PMAMS can be used in certain cases only as a filter for certain cell types as well as in combination with a size exclusion filter. The resulting solution of analytes is exposed to a PMAMS specific for a matter in subcellular particles (for example virus). The submicellular PMAMS in the form of particles and / or a size extrusion filter is used to generate a solution of small molecule enzymes (eg, protein, small chemical entities). Through the use of a semen PMAMS assay system the analyte solution can be sequentially purified to decrease the interactions of specific analytes. The optical opacity of a material used for a support, electrode and / or link domain can be used to achieve the desired properties. Such material may be translucent, transparent or substantially opaque, depending on the thickness, composition and / or optical density of the material. The optical opacity of fibrillated mats increases with the increasing thickness of the mat. Very thin mats are optically translucent. Thicker mats can be substantially opaque. In some examples, mats having a thickness in the range of 0.O1 μ to 0.5 μm are substantially trapslucepts. In other examples, mats with a thickness greater than 20 μm are substantially opaque. Mats with a thick between 0.5 μm and 20 μm have an intermediate opacity, which increases with the increased thickness of the fibril mat. The optical opacity of a particular thickness of an ester may depend on the composition, density, derivatization, number of layers, types and amounts of materials dispersed in the mat, and / or a combination thereof. It can also detract from the wavelength of the light used. If a material is substantially translucent in a given thickness and substantially opaque in another thickness, the light emitted from a certain depth in the material can exit the material while the light emitted from another depth (for example greater) it can be substantially absorbed or dispersed by the material. In one example, the 'variable opacity of a material allows the material to be used as an optical filter. Light emitted at a certain depth on a fibril mat may substantially pass through the mat and may be observed with a detector placed on or near the surface of the fibril mat. The light emitted from another depth can be substantially absorbed and / or scattered by the mat and not be observed by a detector placed on the surface of the mat or in the vicinity of said surface. This property of the fibril mat (and / or optically similar materials) can be used to distinguish between linked and bound reagents in the ECL assay. Some reagents can be dispersed (actively or passively), pulled (for example, either by filtering by suction and / or by capillary action), undergoing a wicking process, or by pressing to a sufficient depth in a porous material in such a way that the light emission of these reagents is substantially or totally absorbed or scattered on the mat. In an example, a fibril mat acts as a physical filter and optical filter through which certain reagents pass, certain reagents are entrained and / or certain reagents are bonded to a very thin layer either on the surface of the mat or in the vicinity of the surface of the mat. Diffusion, pulling, etc. is avoided in or through the reagent mat linked to one or several binding domains and / or species linked to species linked to one or more binding domains (these domains are located either on the surface of the fibril mat or on a very thin layer of the surface of the mat in the PMAMS). Reagents and / or other solutions flow or are suspended on the surface of the fibril mat and / or on the surface of the fibril mat in such a way that the reagents bind only to a very thin layer on the surface of the mat. . Reagents can be washed through the mats, once or several times, in one direction. Reagents can bind in the fibril mats, one to several binding domains, other reagents or the same reagents linked to one or several binding domains, being dragged within the mat, passing through the mat, or a combination of the isma. Porous materials used in supports and / or electrodes may have more than one layer in which the upper layer has binding domains and other layers within the mat have binding domains. In a pure axis, a fibril mat (illustrated schematically in FIG. 29), the upper layer 2900 is su ciently thick to prevent the passage of light originating in the layers 2901, 2902 r from the mat under the This captures. The light 2903 that originates from the sources 2904, 2905 linked to this upper layer can be detected by means of detector 2906 located in the uppersurface of the mat or close to that surface. Light originating from sources 2907, 2 ^ 08, 2909 in lower layers 2901, 2902 is absorbed and / or dispersed by any of the layers or all layers and can not be detected by the detectors 2906, 2910 A prefixing step can be used to select sizes, types, fibril derivatives / or aggregates of particular fibrils prior to the manufacture of the mat. The filter agent used to filter a fibril suspension is a fibril mat having a porosity or several porosities. A porous material (for example, a fibril mat) can act as the support for the binding domains, an electrode that can be used for ECL or other electrochemical applications, a filter that can be used to control the supply of reagents, and / or an optical filter that can transmit, absorb and / or scatter light in several degrees. 5.12. ELECTROCOMPONIC ECL PRESENTATION PANELS The invention also allows the production of isolated electrochemical pixels for use in flat panel displays. Lithographic techniques have been proposed for use in presentations of planar panels in electrochromic reactions and electroquimics luminescence to create pi s that, when directed electronically, have limited effect on nearby pixels (ie, limited crosstalk) (see US patent No 5,189,549). One limitation of the lithographic technique to reduce such crosstalk is that the electrolyte material must be able to change its conductivity when exposed to light. It is a feature of the present invention to reduce crosstalk between pixels without the need to use materials capable of modulating photo-induced conductivity thus allowing the use of a wide range of solutions, gels or different films. The two electrode surfaces that are the active region of pi! > They are found on two surfaces facing each other in a sandwich configuration. The electrode surfaces are coated, for example, with complementary electrochromic materials. To reduce crosstalk, a conductive electrolytic film is placed between the electrode surfaces with non-conductive regions between different pairs of electrodes (i.e., between pixel-s elements). If the coated electrode surfaces are hydrophobic, then the areas of the surfaces around the electrodes are made to be hydrophobic, for example, by stamping or depositing through a mask) and small conductive droplets. Hydraphiles are placed in the electrode on the first surface (for example, half a set of fluids) and then the second surface is automatically aligned and comes into contact with the first surface in such a way that the electrodes are in correspondence . The small electrolytic droplets can therefore be limited to the area within a pixel without any conductive material between the pixels. The pairs of electrodes of a pixel are side by side in close proximity on the same surface. If the pairs of coated electrodes are hydrophobic, the area covered by both electrodes is made to be hydrophilic with a hydrophilic ring around the hydrophilic area of the electrode (for example, by stamping or depositing through the electrode). of a mask). The small droplets described in the two previous modalities are stabilized using hydrophobic solutions. The viscosity of the solutions can be increased to increase the stability of the sets of small droplets. The hydrophobicity and hydrophobicity can be reversed. In other embodiments, the small droplets may contain solutions capable of polymerization to increase the stability and / or conductivity (eg, conducting polymers) of the film between or on the electrode pairs. Adiciona 1-menteStructured characteristics can be used to limit the aphonia between pi eis. For example, an elastomeric stamp (e.g., pol i (dimet i lsi loxane)) with ring-shaped stamp-shaped protrusions capable of circling side-by-side pairs of electrode pixels on a surface can be used to isolate solutions, gels or electronic films between pixels. Alternatively, pairs of side-by-side electrode pixels can be placed in structures in the form of electrically insulating wells on one surface, electrolyte solutions, gels or films placed in the wells above the electrodes, and the entire surface covered or coated to isolate and contain the electrolyte components of each μixel. 5.13. POPULAR POPULATIONS FOR USE IN OTHER CHEMICAL REACTIONS The PMAMS of the present invention can also be used to carry out chemical reactions not in combination with other chemical reactions.

ECL. For example, all non-ECl techniques and tests presented in section 5.1t arpba can be used. A cassette is provided to detect or measure an analyte of interest in a sample, which comprises: (a) a first support having a plurality of discrete link domains on the surface d > - The same to form at least one binding surface, at least some of the »discrete binding domains?» are of binding specificities different from the other binding domains, each of the plurality of »discrete binding domains is hydrophilic and surrounded by hydrophobic regions, and (b) a second support "having a plurality of hydrophobic domains comprising suitable reaction media to conduct a chemical assay there to form a test surface, wherein the plurality of domains of discrete binding and the plurality of reaction means may come into contact in such a manner that an analyte sample present in each binding domain comes in contact with a reaction medium to detect or measure an analogous of interest. Alternatively, the binding domains may be hydrophobic, and the second support has a plurality of hydrophilic domains containing re-ion means. The invention also provides a method for detecting or measuring ana les of interest in a sample comprising: (a) the droplet placement of a sample containing an analyte to be detected or going into a plurality of dt domains. discrete links in a support surface, wherein the plurality of discrete link domains compose at least one link domain containing link reactors that are identical in them and that differ as to the specificity of the links of links contained within the other link domains, each of the domains of link challenges is characterized as either hydrophobic or hi drof i 1 ico, a con ición that the region of »the support surface surrounding each domain The hydrophobic linkage is the hydrophobic and the linkage domain and the hydrologic domain, and (??) hydraflies and the binding domain is hydrophobic, to allow one or several analytes of interest in the sample to be link oon the domains of the ce, and (b) contacting the drops in the first support with a surface of a second coparte that has a plurality of discrete hydrophobic domains that comprises suitable means of replenishment to carry it? perform a chemical test there, and (c) determine the presence of 1 cv = > Analytes of interest that are linked to the domain of link. A method is also provided for detecting -or I am going to be interested in a sample, which comprises f) the placement of drops of a sample containing an analyte to detect or to go in a plurality of domains of interest. discrete bonds in a support surface wherein the plurality of discrete binding domains comprises at least one binding domain that contains binding reagents that are identical to each other and that differ in terms of the specificity of the binding reagents contained within other link domains, each of the discrete binding domains is characterized as either hydrophobic or hydraphilic, provided that the region of the support surface surrounding each of the domains of linkage is (i) hydrophobic and the domain The link is hydrophilic, and (ii) hydrophilic if the binding domain is hydrophobic, to allow one or several analysts of interest in the sample to bind to the binding domains, and (b) to place droplets of a reaction medium on the drops shows; and (c) determining the presence of analytes of interest that are linked over the binding domain. In a particular example of this aspect of the present invention, binding domains, each of which incorporates a different enzyme that employs a sequential intermediate in a chemical reaction as a substrate, are located on a PMAMS surface., such that the product of a given enzymatic reaction, which is the reagent for a subsequent enzyme, flows to the next enzyme in the reaction path. The invention also provides bulk immobilization. of enzymes in monolayers of a? to assembly, for example, for industrial application, using methods described above. For example, sheets with such enzymes immobilized on one or both sides can be stacked to achieve high proportions between the surface area and the volume of solution. Alternatively, such immobilized enzymes can be fixed on porous materials. Further, such immobilized enzymes can be found in rods, stirring agents, in the walls of tubes or capillaries, or in the walls of reefers as for example an incubator chamber. In an alternative aspect of the invention, non-ECL assays. such as those described above can be carried out in PMAMS analogs, said PMAMS analogs differ from the PMAMS linkages described above in that the PMAMS analogs contain discrete domains to carry out non-ECL reactions, the discrete domains do not have incorporated necessarily a binding reagent and therefore are not necessarily binding domains. Such PMAMS analogs have discrete domains to carry out reactions and are prepared to inhibit the expansion and / or diffusion of fluid applied to the discrete domains. In one embodiment, the domains are either hydrophobic or hydrophobic in relation to the surrounding regions on the support surface, to help contain the reaction medium and / or sample in the discrete domains. The use of wells, deposit of reaction medium or sample in felts or porous materials, desiccated deposit of reaction medium or sample in gel.es, films, etc., can be used to inhibit expansion or diffusion. Each of said discrete domains has a diameter or width of less than 1 mm, preferably within the range of 50 nm to 1 mm, with a greater degree of preference within the range of 1 m to 1 mm. The same reaction medium or different reaction medium can be deposited in each of the discrete domains before the application of the sample, or the application of the sample can precede the deposit of the reaction medium. In a preferred aspect of the use of PMAMS analogs to carry out non-SL assays, droplets of reaction medium are placed in a plurality of discrete domains, preferably supplied concurrently from a set of microfluidic guides? and then, optionally, to increase the stability and / or protect the drop, a more viscous solution (for example, oil) is placed in the upper part of the reaction medium or, at the end, between the discrete domain; and then the sample containing analyte to be detected or measured is applied to each domain, either by discrete application to each discrete domain to good, in bulk, by exposing the entire surface of the PMAMS analog containing the domains a a sample of fluid. Any resulting reaction in the binding domains is allowed to proceed, and the results are observed by the use of a reporter and detection system selected from those known in the art. The invention is further described in the following examples whose purpose is not to limit the scope of the invention in any way. 6. EXAMPLES 6.1. PREPARATION OF A MAB PMAMS SURFACE THROUGH MICROESTAMP DO A matrix of exposed and revealed fibrous substance of 1-2 micrometers thickness is prepared according to well-known procedures in a square arrangement pattern. A 10: 1 mixture of silicone elastomer SYLGARD 184 (poly (dimethylsilane) available in Daw Corning) and the corresponding curing agent SYLGARD 184 is emptied into the matrix and cured. The SYLGARD 184 poly mer is carefully removed from the silicon matrix. The resulting elastomeric pattern is "inked" by exposure to a hydrophilic OH-terminated alkathiol, SH (CH2) 11- (0CH2CH) 60H, in an ethanolic solution Q-10 mM), which is automatically contacted corresponding to the " spike with an aligned gold surface, and stir, the substrate is then washed for a few seconds (for example, 1-20 seconds) with a solution of a alacantiol with hydrophobic CH3 terminus, SH (CH2) 10CH3 (1-10 M) in ethanol) (Kumar et al., supra and Prime et al., Science 252: 1164-7). The resulting surface is then dried gently under a flow of nitrogen. A set of capillaries containing a hydrophilic solution automatically contacts the spike with the surface aligned by aligning the capillaries with the SH (CH2) 11- (0CH2CH2) 60H domains. Each capillary in the capillary array contains monolayer antibodies (MABs), specific for an analyte of interest, capable of covalently linking to the reactive OH groups in the hydrophilic domains via an amide bond. 6.2. PREPARATION OF A MAB AND SURFACE OF NUCLEIC ACID PMAMS THROUGH MICRO-STAMPING A matrix of exposed and revealed fato-hardenable substance of 1-2 microns thick is prepared in accordance with well-known procedures in a square arrangement pattern. A 10: 1 mixture of silicon elastomer 184 SYLGARD and the corresponding curing agent SYLGARD 184 is emptied into the matrix and cured. The polymerized SYLGARD 184 is carefully removed from the silicon matrix. The resulting elastomeric pattern is "inked" by exposure to an alkalinity with OH hydrophilic termination, SH (CH2) 11- (0CH2CH2) 60H, in an ethanolic solution (1-10 mM), automatically placed in pin contact with a surface of gold aligned, and removed. The substrate is then washed for a few seconds, (for example 2-10 seconds) with a solution of an alkalinity terminated in hydrophobic CH3, SH (CH2) 10CH3 (1-10 mM in ethanol) (Kumar et al., Supra and Prime et al., Science 252: 1164-7). The resulting surface r is then dried gently with nitrogen flow. A set of capillaries containing hydrophilic solutions is then contacted auto matically in spikes with the surface aligned by aligning the capillaries with the SH (CH2) 11- (0CH2CH2) 60H domains. Each capillary in the set of capillaries contains antibodies or modified nucleic acids, specific for an analyte of interest, capable of covalently linking with the OH reactive groups in the hydrophilic domains via amide linkages. 6.3. PREPARATION OF A SURFACE OF PMAMS BY CHEMICAL ATTACK A clean gold surface is exposed to a hydrophilic OH-terminated alkali, SHI.CH2) 11- (0CH2CH2) 60H (Prime et al., Science 252: 1164-1167) in a solution Ethanic (1 -10 mM). A linear array of fine-tipped etching tools comes into contact with the robot ica epte corresponding automatically to a surface; of gold aligned, and the linear set is used to chemically attack on both the X and Y dimensions of the surface by creating a two-dimensional network set of SH (CH2) 11- domains. { 0CH2CH2) 60H. The substrate is then washed for a few seconds (for example 2-10 seconds) with a solution of a hydrophobic SH (CH2) 11- (0CH2CH2) 6CH3 (1-10 M in ethanal). The resulting surface is then gently dried under a flow d? nitrogen. A capillary set containing hydrophilic solutions then enters corresponding spike contact automatically with the surface aligning the capillaries with the SH (CH2) 11- domains. { QCH2CH2) 60H. Each capillary in the set of capillaries contains antibodies or nucleic acids, specific for an analyte of interest, capable of covalently binding with the OH receptive moieties in the hydrophilic domains. 6.4. SQUARING TESTING ON A PMAMS SURFACE A transparent surface of PMAMS is made in accordance with what is described above, which is substantially transparent with a set of specific shapes of primary antibodies bound to the surface. The support is selected, set of electrodes, Monologue surface in such a way that they are transparent. The PMAMS surface then exposes a sample of solution suspected of containing an analyte of interest for its assay. The sample is then washed leaving the antibody bound to the analytes on the surface. The surface of PMAMS is then exposed to a solution that contains antibodies labeled as ECL. secondary specific for analytes bound on the surface. This solution is then washed from the surface of PMAMS by labeling labeled secondary ECL antibodies to the domains where the analyte is present. The set of electrodes is protected by a removable barrier to avoid. Premature contact of the sample with the electrode surface to avoid contamination defects. The barrier is then removed and the electrode assembly, if it is moistened with the test regulator, comes into contact with the surface of the PMAMS. The electrode assembly is connected to a waveform generator of electronic potential, and potential is applied to pairs of working / counter electrode electrodes. A CCD then reads the emitted light and the signal is sent to a microprocessor that converts the signal into the desirable readable form. The reading is compared to the reading obtained using controls in the form of known amounts of an analyte of interest to calculate the actual amount of analyte. 6. 5. TESTING ON A SURFACE OF A FIRST PMAMS AND SECOND PMAMS A transparent PMAMS surface is prepared in accordance with that described above with a highly specific set of primary antibodies bound to the surface. The surface of PMAMS is exposed after a sample of solution of which, it is shown that it contains an analyte of interest to be tested. The sample is then washed by dumping the antibody bound to the analytes on the surface. A second PMAMS is provided, under protective cover, with an alternative hydrophobic / hydraphical pattern wherein microdrops of a plurality of secondary antibodies labeled with SL are formed. The barrier that protects the second PMAMS in correspondence with the first PMAMS is removed and the microtas fall in correspondence with the primary antibody binding domains in the first PMAMS. The second PMAMS is removed from the set of electrodes and comes into contact in line with the first surplus of PMAMS. The electrode assembly is connected to an electric potential generator, and the potential is applied to the working electrode / counter electrode pairs. A photomultiplier tube then reads the emitted light and the signal is sent to a microprocessor that converts the signal into the desired lexible form. The reading is compared to the reading obtained using controls in the form of known amounts of an analyte of interest to calculate the actual amount of analytes. 6.6. NUCLEIC ACID ESSAY ON A SURFACE OF PMAMS A transparent PMAMS surface is made in accordance with that described above with a highly specific set of single-stranded nucleic acid probes linked to the surface. The probes are complementary to the 5 'region of a nucleic acid analyte of interest. The surface of PMAMS is then exposed to a sample of solution of which, it is suspected that it contains a rattle of interest of hybridizable nucleic acid to be tested, the sample has previously been denatured, ie, treated to render the analyte of interest of single strand. The sample is then washed leaving analytes hybridized on the surface. The PMAMS surface is then exposed to a solution containing secondary ECL labeled nucleic acid probes specific for the 3 'end of the surface linked nucleic acid analytes. This solution is then washed from the surface of PMAMS leaving labeled nucleic acid probes for ECL over the domains where the analyte is present. The barrier protecting the second PMAMS in correspondence with the first PMAMS is removed and the microdroplets enter into correspondence with the primary antibody binding domains in the first PMAMS. The second PMAMS is removed and the electrode assembly comes into contact with the surface of the first PMAMS. The set of electrodes is connected to a waveform generator of electronic potential, and potential is applied to the pairing / counter-electrode pairs of electrodes. A CCD reads the transmitted light afterwards and the signal is sent to a microprocessor which converts the signal into the desired form of reading. The reading is compared to the reading obtained using controls in the form of known amounts of an analyte of interest to calculate the actual amount of analytes. 6.7. COMPETITIVE ESSAY ON A SURFACE OF PMAMS WITH A F0T0MULTIPL ICATOR DETECTOR A transparent PMAMS surface is prepared in accordance with the above described with a specific set of primary antibodies, specific for an analyte of interest, linked to the surface. The surface of PMAMS is then exposed to a sample of solution to be tested which is a mixture of a sample suspected of containing the analyte of interest and a known quantity of a molecule labeled for ECL competitive with the analyte of interest for its link with the antibodies. The sample is then washed by leaving analysts bound to antibodies and / or co-labeled linkers on the surface. The set of electrodes is protected by a removable barrier to avoid contact of the sample with the surface of the electrodes in order to avoid contamination effects. The barrier is removed afterwards and the set of electrodes, which is moistened with a test regulator, comes into contact with the surface of PMAMS. The electrode assembly is connected to a waveform generator of electronic potential, and a potential is applied to the working electrode / counter electrode pairs. A photomultiplier tube then reads the emitted light and the signal is sent to a microprocessor that converts the signal into the desired readable form. The reading is compared to the reading obtained using controls in the form of known quantities of an analyte of interest to calculate the actual amount of analytes. 6.8. COMPETITIVE ESSAY ON A SURFACE OF PMAMS WITH A CCD DETECTOR A transparent PMAMS surface is made in accordance with the above described with a multirespecific set of primary antibodies bound to the surface. The surface of PMAMS is then exposed to a sample of solution which is suspected to contain the analyte of interest to be tested. The sample is then washed leaving antibodies bound to analyses in the surface. A second PMAMS, under protective cover, is provided with an alternative hydrophobic / hydrophobic pattern in which microdrops of a plurality of a known amount of a labeled ECL molecule are formed competitive with an analyte of interest. The protection barrier of the second PMAMS corresponding to the first PMAMS is removed and the microgags enter into correspondence with the primary antibody binding domains in the first PMAMS. The second PMAMS is remoulded and the electrode assembly comes in contact with the surface of the PMAMS. The electrode assembly is connected to a waveform generator of electronic potential, a potential is applied to the working electrode / counter electrode pairs. A CCD then reads the emitted light and the signal is sent to a microprocessor that converts the signal into the desired readable form. The reading is compared to the reading obtained using controls in the form of known amounts of an analyte of interest to calculate the actual amount of analyte. 6.9. PREPARATION OF A SURFACE OF MAB PMAMS BY MICROESTAMP DO WITH AN ALCANTIOL SH (CH2) 10CH3 A matpz of exposed and exposed fato-hardenable substance of 1-2 microns thick is prepared according to well-known procedures in a square arrangement pattern. A 10: 1 mixture of silicone elastomer 184 SYLGAPD (pol i) d? Met i lsi loxane); available in Done Corning) and the healing agent SYLGARD 184 is emptied on the matrix and cured. The SYLGARD 184 pallet is carefully removed from the silica matrix. The resulting elastomeric stamp is "inked" by exposure to a hydrophilic OH-termination alkali, SH (CH2) 110H, in an ethanolic solution (1-10 M), which comes into corresponding tenon contact automatically with an aligned gold surface, and stir. The substrate is then washed for a few seconds (for example 2-10 seconds) with a solution of aleantiol with hydrophobic CH3-termination, SH (CH2) 10CH3 (1-10 mM in ethanol) (Kumar et al., Supra). The resulting surface is then dried gently under a flow of nitrogen. A set of capillaries containing hydrophilic solutions then enters corresponding pin contact automatically with the alized surface aligning the capillaries with the SH (CH2) 110H domains to place specific antibodies in each domain. Each capillary in the set of capillaries contains monoclonal antibodies, specific for an analyte of interest, capable of covalently linking with groups 17: OH reagents in the hydrophilic domains. 6.10. PREPARATION OF A MAB AND A SURFACE OF NUCLEIC ACID PMAMS BY MICROESTAMP WITH AN ALCANTILE SH (CH2) 10CH3 A matrix of exposed and revealed photocurable substance of 1-2 microns in thickness is prepared according to well-known procedures in a square array pattern. A 10: 1 mixture of silicone elastomer 184 r SYLGARD and the. corresponding healing agent SYLGARD 184 is emptied into the matrix and cured. The polymerized SYLGARD 184 is carefully removed from the silicon matrix. The resulting elastomeric stamp is "inked" by position to a hydrophilic OH determination alkapiol, SH (CH2) 110H, in an ethanolic solution (1-10 mM), automatically contacted with spigot correspondence with an aligned gold surface , and it is removed. The substrate is then washed for a few seconds (for example, 2 to 10 seconds) with a solution of alkydiol with hydrophobic CH3 terminus, SH (CH2) 10CH3 (1-10 mM in ethanal> (Kumar et al., Supra) The resulting surface is then dried gently under a nitrogen flow.A set of capillaries containing hydrophilic solutions are automatically contacted correspondingly in spike with the surface aligned by aligning the capillaries with the SH (CH2) 110H domains, to place specific antibodies and / or hybridizable nucleic acids in each domain Each capillary in the set of capillaries contains antibodies or modified nucleic acids, specific for an analyte of interest, capable of covalently linking the reactive OH groups in the hydrophilic domains to through amide bond links 6.11 PREPARATION OF A PMAMS SURFACE USING AN ESTREPTAVIDINE-BIOTIN LINK A matrix of photocurable substance; Exposed and revealed 1-2 mm thick is prepared according to well-known procedures in a square arrangement pattern. A 10: 1 mixture of silicone elastomer 184 SYLGAR and the corresponding curing agent SYLGARD 184 is emptied into the matrix and cured. The SYLGARD 184 imerized polymer is carefully removed from the silicon matrix. The resulting elastomeric stamp is "inked" by exposure to a mixture of ercaptoundecanol and 12-mercapto-B-biotamido-3,6-dioxaoct i 1) dodecanamide where the mole fraction of the thiol. biotinylated is 0.1 (see Spin e et al., 1993, Langmuir 9: 1821-5 and Spinke et al., 1993, J. Chem. Phys. 99 (9): 7012-9). The substrate is then washed for a few seconds (e.g., 2-10 seconds) with a solution of alkaliol terminated in hydrophobic CH3, HS (CH2) 10CH3 alkynyl (1-10 mM in ethanol) (see Kumar et al., Biebuycl , Whitesides). The resulting surface is then dried gently or a flow of nitrogen. A capillary assembly containing a streptavidin solution in each capillary is then automatically contacted in a spikewise fashion with the surface aligned. Each capillary in the set of capillaries is aligned and comes in contact with a biotinylated domain and the capillary array is removed and the surface washed. A second array of capillaries containing a multiplicity of biotinylated antibodies and solutions of nucleic acid nucleic acids then enters into corresponding pin contacting automatically with the surface aligned to place specific antibodies and specific nucleic acids in each domain. 6.12. PREPARATION OF A SINGLE MAB SURFACE A joint of electrodes of working electrode and counter electrode pairs in a silicon gold surface is manufactured by methods known in the art (for example see Kumar et al. Supra). In this example, the electrode array and the discrete link domain array existp on the same support surface. A matrix of exposed unhardened photoresist of 1-2 microns thick is prepared in accordance with procedures well known in the art of working electrode patterns. A 10: 1 mixture of silicone elastomers 184 SYLGARD (pal i (d imet i Isi laxapo (PDMS)) available from Dow Corning) and the corresponding curing agent SYLGARD 184 is emptied onto the matrix and cured. The polymerized SYLGARD 184 is carefully removed from the silicon matrix. The resulting elastomeric stamp is "inked" by exposure to a hydrophilic OH determination alkali, SH (CH2) 11- (0CH2CH2) 60H, in an ethanolic solution (1-10 mM), automatically contacted in correspondence of the esptiga with the working electrodes aligned on the surface of gold electrode arrays, and then removed. An array of capillaries containing hydrophilic solutions is then automatically contacted with spike correspondence by aligning the capillaries with the SH (CH2) 11- (0CH2CH2) 60H domains on the electrode array surface to place specific antibodies in each domain . Each capillary in the. The arrangement of capillaries contains monoclonal antibodies, specific for an apalite of interest, capable of coextensively linking to the reactive OH groups in the hydrophilic domains through an amide bond. 6.13. TEST PERFORMED ON THE UNIQUE SURFACE OF MAB A support is manufactured in accordance with what is described in 6.12, supra. A PDMS stamp is manufactured in accordance with what was previously described from a matrix of; photoepdureable substance configured as rings each circumscribing independently a pair of working electrode / counter-electrode. The surface of the. The electrode array is then exposed to a sample to be analyzed, washed with a mixture of secondary antibodies labeled for ECL, and then washed with an assay regulatory solution containing triproi sheet. The PDMS stamp is then aligned and in corresponding contact by aligning the rings of the PDMS stamp to circumscribe and define individual elements of assay controller volume above each pair of electrodes. An overpotential is applied to the pairs of such electrodes. In order to release the monolayer from the surface, expose the working electrode to secondary antibodies labeled for ECL. A photoprint tube then reads the light emitted through the transparent PDMS and the signal is sent to a microprocessor that converts the signal into the desired readable form. The reading is compared to the reading obtained using controls in the form of known quantities of an analyte of interest to calculate the actual amount of analyte. 6.14. PREPARATION OF A UNIQUE SURFACE WITH WORK AND CONTRA ELECTRODE ELECTRODES An array of electrodes of working ring electrodes and of interdigital counter electrodes with link domains; of gold between the interdigit electrodes on a silicon gold support is manufactured by methods known in the art (for example see Kumar et al., supra). In this example, the set of electrodes and the. set of discrete link domains exist on the same surface. A photoprotective substance matrix exptuejsta and revealed of 1-2 microns of thickened pyrepara in accordance with well-known procedures in the pattern of the binding domains between the pairs of interdigitalization electrodes. A 10: 1 elastomer blend was 184 silicone SYLGARD (poly i (dimethylsiloxane (PDMS)) available in ow Corning) and the corresponding healing agent SYLGARD 184 is flushed into the matrix and cured. The SYLGARD 184 magnet is carefully removed from the silicon matrix. The resulting elastomeric stamp is "inked" by exposure to a hydrophilic alcantiol determination OH, SH (CH2) 11- (0CH2CH2) 60H, in an etacolic solution (1-10 M), put into corresponding spike contact in an automatic way the gold link domains aligned on the electrode array surface, and then removed. A set of capillaries containing hydrophilic solutions then enter corresponding spike contact automatically, aligning the capillaries with the SH (CH2) 11- (0CH2CH2) 60H domains on the surface of sets of electrodes to place specific antibodies in each domain. Each capillary in the capillary array contains antibodies specific for an analyte of interest, capable of covalently linking to the reactive OH groups in the hydraphidic domains via an amide bond. 6.15 TEST CARRIED OUT ON A SINGLE SURFACE WITH WORKING AND CONTRA ELECTRODE ELEMENTS A support surface conforming to that described in 6. 14, supra is manufactured by the methods described. The prepared surface is exposed to a sample to be analyzed, washed with a mixture of secondary antibodies labeled for ECL, and then washed with a test regulatory solution containing tppropylamin. The electrode assembly is connected to an electronic potential waveform generator, and a potential is applied to the work electrode / counter electrode pairs. A photopolymer tube then reads the emitted light and the signal is sent to a microprocessor that converts the signal into the desired reading form. The reading is compared to the reading obtained using controls in the form of known quantities of an anitole of interest to calculate the actual amount of analyte. 6.16. PREPARATION OF A SURFACE WITH CONTRA ELECTRODES A matrix of photo-hardening substance exposed and developed from 1-2 microwaves of squeeze is prepared according to well-known procedures in a square arrangement pattern. A 10: 1 mixture of SYLGARD silicate elastomer 184 and the corresponding SYLGARD 184 curing agent is emptied into the matrix and cured. The SYLGARD 184 polymer is carefully removed from the silicon matrix. The resulting elastomeric stamp is "inked" by exposure to a hydrophilic alkali metal OH, SH (CH2) 11- (0CH2CH2) 60H determination, in an ethanolic solution (1-10 mM), it is automatically contacted with a spigot contact. with a configured counter-electrode aligned, and a square link domain on a gold surface, and removed. The configured gold surface consists of steerable ring counter electrodes circumscribing the link domains where the SH has been stamped. { CH2) 11- (0CH2CH2) 60H. A gap to well spaced gap exists between each ora counter electrode and each square gold substrate for each monolayer binding domain. A set of capillaries containing solutions of the binding reagent is then automatically contacted in a corresponding manner with the aligned surface matching the capillaries with the SH (CH2) 11- (0CH2CH2) 60H domains to place antibodies specific or nucleic acids in each domain. Each capillary in the set of capillaries contains antibodies or nucleic acids, specific for an analyte of interest, capable of covalently linking with the reactive OH groups in the hydraphidic domains. 6.17. TEST CARRIED OUT ON A SINGLE SURFACE WITH WORKING ELECTRODES AND CONTRA ELECTRODES ON DIFFERENT SURFACES The support surface described above in 6.16 is exposed to a sample solution to be analyzed. The support surface is then washed and exposed to a solution containing a plurality of monoclonal antibodies labeled for ECL or labeled ECL nucleic acids of different specificity and then washed with an assay buffer containing tr ipropylamin. A set of steerable transparent working electrodes is fabricated with each working electrode in the set corresponding to a discrete link / counter electrode region in the support in accordance with that described in section 6.16 above. The two supports are moistened with the test regulator and put into contact with corresponding formal alignment automatically. The electrode assemblies are connected to a waveform generator of electronic potential, and a potential is applied to the aligned pairs of working electrodes / counter electrodes creating a potential field between the two supports. A CCD then reads the light emitted through the transparent working electrode and the signal is sent to a microprocessor which converts the signal into the desired reading form. The reading is compared to the readout using controls in the form of known quantities of an anabolic of interest to calculate the actual amount of analyte. 6.18 MANUFACTURE OF A SCREEN OF FIBPILES (SCATTERED) CC BY VACUUM FILTRATION An aqueous paste of DC fibrils, with a solution of 1 mg of fibplas / mL was prepared by mixing 0.1% w / w of CF / water fibrils deionized. The CC fibrils were dispersed (the largest aggregates, on a scale of miera were dispersed in small aggregates or individual fibers) in the paste by immersion of a sanitization horn of 4 <.X »wats in the paste for a period of 10 minutes to 1 hour. The spread of the dispersion was monitored by optical microscopy. A naylon filter membrane (pore size 0.47 μm, diameter 25 mm) was placed in a 25 mm diameter glass frit filter. The dispersed fibril paste was filtered through the membrane / filtration system by suction filtration (Figure 23A9) Aliquots of the paste (5 ml) were diluted with 20 ml of deionized water, then filtered through a membrane / f 11 tro installation For a mat averaging approximately 0.25-0.3 grams / cc, a mat of approximately 100 μm required 6 aliquots.

The suction filtration continued until all the water in the dispersion was removed on the mat (with visual inspection). The mat was peeled (by hand) directly from the filter membrane. The mat was dried in an oven for approximately 10-15 minutes at a temperature of 60 ° C. The mat was cut, punched or otherwise sectioned for its use. 6.19. MANUFACTURE OF A MATRIX OF FIBRILS IN A METAL MESH SUPPORT THROUGH EVAPORATION An aqueous paste of CC fibrils, with a solution of 1 mg of fibrils / mL, was prepared by mixing 0.1 * / * weight / weight of CC / water fibrils deionized. The CC fibrils were dispersed (the largest aggregates, on the scale of the miera were dispersed in small aggregates or individual fibers) in the paste by immersing a 400 watt sounding horn in the paste for a period of time from 10 minutes to 1 hour. The spread of the dispersion was monitored by optical microscopy. A 1 cm2 section of stainless steel mesh (count 400) was placed on a paper filter with a diameter of 25 mm. A 5 ml aliquot of the paste was placed with a pipette on the surface of the screen / filter paper assembly. The water in the paste was evaporated either at room temperature and pressure, or in a heated oven. Once the fibril mat was dry, additional aliquots were added. Fibrils and screens were detached in the form of a single unit of the filter paper. The mat was cut, pinched or otherwise sectioned for use. 6.20 AVIDINE IMMOBILIZATION IN FIBRILLS THAT CARRY FUNCTIONAL GROUPS ESTER OF NHS Fibrils derived with COOH (supplied by Hypejrion Catalysts Inc.) were suspended in anhydrous dioxane at approximately 10 mg / ml under constant agitation. A 20-fold molar excess of N-hydroxus? -ceinimide was added and allowed to dissolve. Then, a 20-fold molar excess of et i 1-diamino-propi.1-carbodiimide (EDAC) was added, and the mixture was stirred for 2 hours at room temperature. After stirring, the supernatant was aspirated and the solids were washed three times with anhydrous dioxane, once with anhydrous methanol, and filtered on a polysulfone membrane of 0.45 μm. The filtrate was washed with additional methanol and placed in a glass flask under vacuum until no further weight reduction was observed. 10.4 mg of NHS ester fibrils were washed with PBS-1 (approximately 70 mM phosphate, 150 M NaCl) (reactive ORIGIN 402-130-01, pH 7.8, IGEN, Inc.). The washed fibrils were suspended in 2.3 ml of avidin solution (8.3 mg of avidin / ml of PBS-1). The suspension will be; or stand at room temperature for 1.5 hours, with constant rotation of the. piara flask provide agitation. After 1.5 hours, the suspension was stored for 16 hours at a temperature of 4 ° C, and then it was brought to room temperature and washed with PBS-1 and stored at a temperature of 4 ° C in the form of a suspension in PBS-1. 6.21. IMMOBILIZATION OF MONOCLONAL ANTIBODY (ANTI-AFP) IN CARBON FIBRILLES r Carbon fibrils operated with NHS esters were prepared in accordance with what is described in example 6.20. 14 mg of NHS-ester fibri were mixed with 500 ml of PBS-1 buffer. The mixture was blended for 20 minutes until it became a viscous paste. An additional 500 ml of PBS-1 buffer was added. A total of 1.6 mg of apti-AFP antibody was added . { alfafetal protein) in 80 ml. of PBS-1 to the previous paste.

The reaction was allowed to stand at room temperature during 2. 5 hours. 6 ml of PBS-1 buffer was added and the reaction mixture was centrifuged at a temperature of 4 ° C for 5 minutes. The supernatant was removed by a pipette.

This procedure was repeated 9 times. After the final wash, the supernatant was removed, and the product ibri la-ant iAFP was stored at a temperature of 4 ° C. 6.22 VOLTAMOGRAMOS CÍCOS ICOS DE ESTERAS DE FIBRILAS: COMPARISON OF STEREO OF FIBRILES WITH ELECTRODES OF LEAF GOLD Cyclic bouquets of 6 M of Fe +++ / ++ were measured (CN) 6 in 0.5 M of K2S04. In Figure 30A, the CV for a simple DC fibril mat (dispersed) was measured at 0.10 mA / cm at 10, 25 and 50 mV / sec. The mat was manufactured in accordance with what was described in Example 6.18. In Figure 30B, the CV was measured for a gold leaf electrode at 0.05 mA / cm at 10, 25 and 50 mV / sec. All potentials are in volts Vs. Ag / AgCl. 6.23. ELECTROCHEMICAL PROPERTIES OF FIBRILL ESTERS ELECTRODES: ANODIC PEAK CURRENT COMPARISON WITH THE MATTER THICKNESS Cyclic vol tamograms of 6 mM Fe +++ / ++ (CN) 6 were measured in 0.5 M K2S04 pi fibril mats of the same geographical area (0.20 cm2), but with different thicknesses. The anadic peak current (figure 31) was increased with the thickness of the mat for thicknesses ranging from 24 μm to 425 μm. For each thickness, the anodic peak current was also increased with the increase of the exploration speed (for speeds that were between 10 mV / sec and 150 mV / sec). The speed of increase of the anodic peak current, as a function of the thickness, is It also increased as the thickness increased. The fibril mats that had a thickness of 24 μm were comparable in comparison to the gold leaf electrodes. 6.24. NON-SPECIFIC LINKAGE OF PROTEINS ON FIBRI AS The protein-specific na bond on carbon fibrils (c) was measured as follows: i) a solution of labeled proteins Ru (b? Py) +++ ++ ("MARKER 1") was exposed to an amount known carbon fibrils until reaching equilibrium; 11) the labeled protein / fibrils solution was centrifuged, and the supernatant was collected, and iii) the amount of labeled prstein which remained in the supernatant was assayed using electrochemicolum or ICEL (echoline). To generate the curve shown in Figure 32, anti-CEA antibodies fixed on the derived MARKER 1 (carcinoembryonic antigen antibody fixed on an ECL MARKER MARKER 1) at 3 μg / mL, was added to vain dilutions of CC (simple) fibrils. in potassium phosphate buffer 0.1 M at a pH of 7. The fibrils were removed by centrifugation after vortexing for 20 minutes. ECL assays that measured the amount of protein (unbound) remaining in the supernatant were carried out in an analyzer- ORIGIN 1.5 (IGEN, Inc.) ep aliquots of the supernatant of the reaction mixture diluted 5 times with ORIGEN assay buffer. A decrease in the ECL signal (in relation to the ECL signal for an object in the reaction mixture that had been exposed to fibrils) resulted from an increased epl ce of protein marked with a MARKER 1 derived when a concentration was present. highest carbon fibrils. 6.25. REDUCTION OF THE NON-SPECIFIC LINKAGE OF PROTEINS WITH FIBRILLS WITH DETERGENTS / SUPPLACTANTS Using the method described in Example 6.2.4, the effect of surfactant on the protein binding on »fittplas was analyzed. Triton X-100 was added to the fixed anti-CEA to derive mixtures of MAPCADOP 1 / fβpla, the f fe solution incubated for 20 minutes, the tubes were centrifuged, and aliquots of the sobrenadapte diluted 5 times with assay regulator were analyzed ORIGIN. The results appear in the following table and in figure 33. Number of (T-X100), Intensity Prot-MARKER 1 (GF), tube ppm peak μg / ml ppm 19 1674 1611 2.65 52 1 188 8 83377 1634 2.65 52 17 418 1697 2.65 52 16 209 15e 2.65 52 105 1772 2.65 52 14 52 1463 2.65 52 1 133 2 266 627 2.65 52 12 13 23 2.65 52 A curve resulting from the plotting of the ECL intensity of a protein marked with a MARKER 1 derived in solution versus Triton X-100 concentration appears in Figure 33. A signal. of ECL. highest corresponds to. more pratein marked with the MARKER 1 derived in the sobrenadapte, what corresponds to less protein marked with MARCADOR 1 derivative linked to the fibrils. Triton X-100 concentrations that were used at 10 ppm 100 ppm reduced the extent of the binding; he. Increasing the concentration from 100 to 2000 ppm did not further reduce the magnitude of the link. 6.26. ECL OF FREE MARKER IN SOLUTION WITH FIBRILL ESTERA ELECTRODE A fibril mat prepared in accordance with the. Example 6.18 was installed in the mounting area 3403 of the work electrode fastener 3401 of the "Fibril Cell" installation shown in Figure 34. The fastener 3401 was slid into the bottom of the compartment 3400 of the electrochemical cell. The reference electrode 3 M Ag / AgCl (Cyprus Na. EE008) was installed in the compartment of the electrochemical cell through the reference cell hole 3402. The cell was filled a test regulator (IGEN No. 402-005-01 lot No. 5298) and fixed on the PMT 3404 fastener. Using a universal programmer.

Model 175 of EG &G PARC and a Potenc ost a / G 1 goes to model 175 of EG &6, the potential was swept from 0 V to + 3 V versus Ag / AgCl at 100 mV / sec. The average pair ECL of Hamamatsu R5600U-01 that received 900V energy was measured through a photometer 126 model of Pacific Instruments. The analog data were recorded at 10 Hz by a CI0-DAS-601 A / D board driven by HEM Spap-Master. The Fibril Cell was drained, rinsed 1000 pM of MARKER 1 (IGEN No. 402-004-C lot No. 4297), and filled 1000 pM of MARKER 1. The potential was btarred as the assay regulator. Figure 35 shows the ECL traces (measured at 24.0 +/- 0.2 C) for the 3501 test controller and 1000 pM of the REGULATOR 1 3502. The peak area of corrected dark ECL was 22.10 nA for the regulator- and 46.40 nAs for 1000 pM of MARKER 1, 6.27. ECL OF ABSORBED MARKED ANTIBODY FIBRILL ESTERA ELECTRODE Fibril matting was elaborated to a thickness of 0.00889 cm from simple dispersed fibrils c in the manner described in Example 6.18. The dried mats were then punched in 3 mm discs and mounted on soptops. The supports used in this e- < Cucumbers were manufactured from 0.0762 cm psi-ester housings, con- figured by conductive gold ink printed on the screen.

This conductive gold ink formed the counter electrode, reference electrode, and provided conductors for the work electrodes and other electrodes. Two discs from e.te > of fibrils were mounted on each configured support using conductive tape that contained carbon on both sides (Adhesives Research). After assembly, the discs were mottled 0.5 μl of 10 μl / l of anti-TSH antibody bound on the MARKER 1 derived in deionized water (R? -TSH mono 1: 2 June 26, 1995, IGEN, Inc.) or 0.5 μl of »10 μg / ml of captur-a antibody labeled anti-TSH MARKER 1 in disiuminated water (TSH poly 25 of June 1995, IGEN, Inc.) and allowed to dry. After drying, the mats were soaked IGEN assay regulator. The mats soaked in supports were placed in an instrument based on Origin 1.5 of IGEN and the ECL was read using a scanning speed of 500 mV / s from 0 to 4500 mV. Figure 43 compares the peak ECL signals from the mats 4301 containing the antibody MARKER 1 and the mats 4302 contained the capture antibody labeled MARKER 1 '. 6.28. ECL USING FIBRILL ESTERA ELECTRODE PAPA SANDING TESTS Anti-AFP capture antibody was immobilized in fibrils in accordance that described above. The anti-AFP fibrils were washed in deionized water (di) and resuspended in 1: a density of 3 mg / ml. A 4-layer fibril mat was produced using vacuum filtration in accordance that described in Example 6.18. Milligrams of anti-AFP fibrils were added to 3 mg of simple DC dispersed fibrils and the mixture was diluted to a total volume of 20 ml in di. The diluted mixture was filtered on a 0.45 μm nylon filter. This mat of initial mat was then followed by two core layers, each consisting of 5 mg of simple dispersed DC fibrils. The mat core was then covered a mixed fibrous cape identical to the initial layer. This had or resulted in a fibril mat having approximately 40% anti-AFP fibrils on the upper surface and on the lower surface and approximately 100% of simple fibrils in the nucleus. This mixed mat was air dried under vacuum and pouched in 3 mm discs. These discs were then mounted on supports in accordance what was described in Example 6.27. Dry anti-AFP mats, supported were soaked with calibrators of AFP A, C, and F (IGEN, Inc.) and allowed to incubate for 15 minutes at room temperature in the upper part of the bank. After incubation, supported electrodes were washed with a deanised water flow for 10 seconds and then dried with a lint-free dryer. The fibril mats were then soaked with apti-AFP bound to antibody labeled with MARKER 1 derivative (IGEN, Inc.) and incubated for 15 minutes at room temperature in the upper part of the bank. After incubation, the sopiortados electrodes were washed with deionized water and dried with a drier. The fibril mats were then soaked with a >regulator; IGEN test and were read in accordance with what was described in Example 6.27. 6.29. DETECTION OF AVIDINE ECL MARKED WITH MARKER 1 ON A PQL IACRI LAMIDA SURFACE A reticulated polyacrylamide gel containing covalently linked biotin was prepared by acplamide copolymerization, bi-acp lick, and N-acp loi 1-N '-biotini 1-3, 6-d? oxaoctan-l, 9-d? am? na (biotam linked to an acplamide portion through a tp < i lepgl icol)) using well-known conditions (initiation with ammonium persulfate and TEMED). In this experiment, the concentrations of the three monamépca species were 2.6 M, 0.065 M, and 0.023 M respectively (these concentrations of acplamide and bis-acr i lamda are reported to result in gels with smaller pore sizes than most). ls proteins). The polymerization of the solution containing the monomers between two glass piles spaced at a distance of approximately 0.07 mm resulted in the formation of a gel plate with the same thickness. After the completion of the polymer reaction, any unincorporated biotin was removed from the gel in four PBS changes. Avidin labeled with a derivative MARKER 1 (where avidin refers to neut rav id ina, a modified avidin designed to present a reduced NSB, was used in this experiment) was bound to the surface of the gel by immersing the gel in a solution that contained the protein at a concentration of 50 μg / mL in PBS for 20 minutes. Avidin labeled with excess MARKER 1 was removed by washing the gel in four changes of ECL assay regulator (200 mM sodium phosphate, 100 mM tppropí lamin, 0.02% (w / v) Tweep-20, by immersion of the gel, pH 7.2). As shown in figure 39, the gel (3900) was placed in contact with gold working electrodes (3901) and against the ectrodes (3902) configured on a glass support (3903). Increasing the potential between the two electrodes from 0.0 to 3.0 V and returning it to 0.0 V at a speed of 500 mV / s produced an ECL light signal in accordance with that measured in a PMT (3904) placed on top of the gel. { figure 40). A gel prepared without inclusion of biotin containing derivative of acp lamida did not provide ECL signal (Figure 41). This signal obtained from the biotin-singred polymer was indicative of the presence of an almost complete protein monolayer on the third surface of the gel. 6. 30. IMMUNOASSAY IN ECL SANDING ON A SURFACE OF PO IACPI LAMTDA A pol I? C gel? 1 crosslinked amide containing covalently bound biotin was prepared in accordance with that described in Example 6.29. Streptavidin is adsorbed on the surface of the gel to form an elliptical domain capable of capturing biotin-labeled species. The surface is treated with a solution containing tpprop and 1 amine, an unknown concentration of X? GX analyte, an antibody labeled with biotin against the analo tite, and a different antibody labeled with ECL MARKER 1 against the analyte. The presence of the analyte causes the formation of a complex of the analyte and the two antibodies which are then captured on the surface of the analyte are rep a id i na. ECL MARKER 1 linked to secondary antibody present on the surface is measured in accordance with that described in Example 6.29, 6.31 MULTIPLE EMLLOVING IMMUNOASSAYS OF ECL ON POLY CRYLAMIDE SURFACES SUPPORTED ON AN ELECTRODE A matrix of substance fotoendur-ec Exposed and disclosed 1-2 micron thickness is prepared in accordance with procedures well known in the art for proving a pattern of circular depressions arranged in a set. A 10: 1 mixture of SYL GARD silicone elastomer 184 and corresponding cure agent SYLGARD 184 is emptied into the matrix and cured. The polymerized SYLGARD is carefully removed from the silicon matrix. The resulting elasto-eric print is "inked" by exposure to a solution containing the hydroxyl-terminated thiol HS- (CH2) 11- (0CH2CH2) 3-0H (1-10 mM) in ethanol, therefore in contact with a gold substrate aligned and removed. The substrate is washed for several seconds with a solution containing the thiol HS- (CH2) 10-CH3 (1-10 inM ethanol). The resulting surface is then rinsed with ethanol and dried aunt or a flow of nitrogen. The treatment of the surface has a solution containing acylloyl chloride and tpetilamipa in dioxane leads to the functionalization of the domains terminated with hydroxyl with acrylate groups. A pool of capillaries containing mixtures of acrylamide, b-acrylate, N-ar-11-iso-succinic acid, α-bis-cyanovaleric acid, and antibodies exhibiting amine groups then comes into contact with the aligned surface by aligning the capillaries with the acrylate-terminated domains to place pre-ionic solutions containing specific antibodies in each domain. Each capillary in the set of capillaries contains antibodies specific for an analyte of different interest. The exposure of the small drops of pre-polymer confgurated to ultraviolet light causes the formation of cross-linked gels on the substrate each presenting a surface binding domain. The assay is carried out by treating the substrate with a mixture of analysts capable of binding to one or more of the binding domains presented on the gel surfaces in a regulated solution containing tpprapi lamina and secondary antibodies labeled with MARKER 1 of ECL. The binding domains (420, 4201, 4202) (in polyacid lick drops (4203) at a time electrode Í4232) are then placed in the vicinity of an ITO 4204 working electrode (as shown in Figures 42A). B. The emitted light from each of the binding domains is quantified using a CCD camera (4205) and compared with the link domains for internal standards included in the sample solution 6.32 MULTIPLE ECL EN COMPETITIVE IMMUNOASSAYS SURFACES OF POL IACRILAMID SUPPORTED IN A EIECTR0D0 A matrix of exposed and revealed photocurable substance of 1-2 micras of e-spiesor is prepared in accordance with well-known procedures to give a pattern of circular depressions arranged in a set. A 10: 1 mixture of silicone elastomer 184 SYLGARD and the corresponding curing agent SYLGARD 184 is emptied into the matrix and cured. The polymerized SYLGARD is carefully removed from the silicon matrix. The resulting elastomeric stamp is "inked" by exposure to a solution containing the thiol with hydroxyl termination HS - (CH2) 11- (0CH2CH2) 3-0H fl-io mM) in ethanol, it is contacted with a substrate of gold lined and removed. The substrate is washed for a few seconds with a solution containing the HS-INCH2) 10-CH3 (1-10M in ethanol). The resulting surface is then rinsed with ethanol and dried under a stream of nitrogen. The treatment of the surface with a solution containing acplayl chloride and tpeti lamina in dioxane leads to the functionalization of the r hydroxyl terminated domains with acp groups. A set of capillaries containing mixtures of acp lamida, tais-acp lamida, N-acp loi lsuccipimida, azo-bis-c and anovalépco acid, and then enters antibodies in contact with the aligned surface aligning the capillaries with the domains terminated in acplato to place special solutions that contain specific antibodies in each domain. The capillaries in the set of capillaries contain specific antibodies for different analytes of interest. The exposure of the small prepaid iris drops configured to ultraviolet light causes the formation of crosslinked gels in the substrate each having a binding domain in the supe fi c. The assay is carried out by treating the substrate with a mixture of analytes capable of binding to one or more of the binding domains presented on the gel surfaces in a regulated solution containing trprap and lamium and analogs labeled with MARKER 1 ECL of the ani cles (that is, stable: it establishes a competition between analysts marked with MARKER 1 for ECL and analysts not marked for the link on the link domains). The binding domains (4200, 4201, 4202) (in drops of pollen lick (4203) at an electrode of or (4232)) are then placed very close to a working electrode IT0 4204 (as shown in the figure). 42. The light emitted from each of the binding domains is quantified using a CCD triad (4205) and compared to the link domains for internal standards included in the sample solution 6.33 MULTIPLE TESTS OF ECL POPE LINKING THE CELLS IN POL IACRILAMIDE SURFACES SUPPORTED IN AN ELECTRODE A matrix of exposed and exposed photoephedrible substance of 1-2 microns thick is prepared in accordance with well-known procedures to provide a pattern of circular depressions arranged in a set. A 10: 1 mixture of elastomer 184 of silicopa SYLGAPD and the corresponding curing agent SYLGARD 184 is emptied into the matrix and cured. The polished SYLGARD is carefully removed from the silicon matrix. The resulting elastomeric stamp is "eptinted" * by exposure to a solution containing the hydroxyl-terminated thiol HS- (CH2) 11- (0CH2CH2) 3-0H (1-10 mM) in ethanol, and contacted with a gold substrate aligned and removed.The substrate is .00 wash for several seconds with a solution containing the thiol HS-ÍCH2) 10-CH3 (1-10 M in ethanol). The resulting surface is then rinsed with ethanol and dried under a stream of nitrogen. The treatment of the surface with a solution containing acryloyl chloride and triethylamine in dioxane leads to the functionalization of the hydroxyl terminated domains with acrylate groups. A set of capillaries containing mixtures of acrylamide, bis-acp lamide, N-ac ri loi Is? Ccinimide, azo-bis-cyanovaleric acid, and antibodies directed against cell surfaces then come into contact with the aligned surface by aligning the capillaries with the acrylate-terminated domains to place prepolymer solutions in each domain. The exposure of the small prepolymer cats configured to ultraviolet light triggers the formation of crosslinked gels on the substrate each having a surface binding domain. The assay is carried out by treating the binding domains first with a cell suspension, then with a mixture of binding reagents capable of binding one or several of the cells attached to the gel surfaces in a regulated solution which contains triprapi lamina and secondary antibodies marked with MARKER 1 for ECL and / or other binding reagents specific for analytes. The binding domains (4200, 4201, and 4202) (in polyacrylamide drops (4203) at a gold electrode (4232) are then placed very close to an ITO 4204 working electrode (as shown in FIG. Figure 42. The light emitted from each of the binding domains is quantified using a CCD camera (4205) and compared with the pair-to-internal standards domains included in the sample solution 6.34 MULTIPLE TESTS OF ECL PAPA LINKING ANALYTES ON CELLS ON POLYACRILAMIDE SURFACES SUPPORTED ON AN ELECTRODE A matrix of exposed fataendurec] b exposed to 1-2 microns thick is prepared in accordance with well-known procedures to provide a patterned pattern of circular depressions in a set, a 10: 1 mixture of elastomer 184; Silicon SYLGARD and the corresponding healing agent SYLGARD 184 is emptied into the matrix and cured. The polymer SYLGARD is carefully removed from the silicon matrix. The resulting elastomeric stamp is "inked" by exposure to a solution containing the hydroxyl-terminated thiol HS ~ (CH2) 11- (0CH2CH2) 3-0H (1-10 M) in ethanol, put in contact with a substrate gold aligned and removed ». The substrate is washed for several seconds with a solution containing the tial HS- (CH 2) 10-CH 3 (1-10 M in ethanol). The resulting surface is then rinsed with ethanol and dried under a stream of nitrogen. The treatment of the surface has a solution containing chlorine of a ri 101 la and triethylamine in dioxane leads to the work of the domains terminated with hydroxyl with acnlate groups. A set of captures containing mixtures of acne lick, bis-acri lamide, N-acploilsuccini ida, Acido aro-b i is aova 1 érico, and cells are then put in contact with a surface aligned by aligning the capules with the domains terminated with acplato to place prepolymer solutions containing specific cell types in each domain. The capillaries in the set of capillaries contain cells with different surface structures that are linked to different analytes. The exposure of the small prepolymer drops configured to ultraviolet light causes the formation of crosslinked gels in the substrate, each having a surface binding domain. The test is carried out by treating the gels with a sample containing a mixture of analyses capable of binding to one or more of the binding domains presented on the surfaces of gels in a regulated solution containing tripoproteins. lamí na and antibodies marked with MARKER 1 for ECL and / or other specific binding reagents for the apalitos. The link domains (4200, 4201, and 4202) (in drops of pollane lick (4203) in? O: A gold electrode (4232) is then placed in close proximity to an ITO working electrode (4204R) as shown in Figure 42. The light emitted from each of the binding domains is quantified using a CCD camera (FIG. 4205) and it is compared with the link domains for internal standards included in the sample solution. 6.35. MULTIPLE ESSAYS OF COMPETITIVE HYBRIDIZATION OF ECL IN POL IACRILAMIDE SURFACES SUPPORTED ON AN ELECTRODE A matrix of exposed and revealed photocurable substance of 1-2 microns thick is prepared in accordance with well-known procedures to provide a pattern of circular deptresses arranged in a set. A 10: 1 mixture of silicone elastomer 184 SYLGARD and the corresponding curing agent SYLGAPD 184 is emptied into the matrix and cured. The polymerized SYL GAPD is carefully removed from the silicon matrix. The resulting elastomeric stamp is "inked" by exposure to a solution containing the hydroxyl-terminated thiol HS- (CH2) 11- (0CH2CH2) 3-0Hl-10 mM) in ethanol, contacted with a gold substrate aligned and removed. The substrate is washed for a few seconds with a solution containing the thiol HS- (CH2) 10-CH3 (1-10 M in ethanol). The resulting surface is then rinsed with ethanol and a nitrogen flow is dried down. The treatment of the surface with a solution containing acryloyl chloride and triethyl chloride in? 4 dioxane causes the functional i zac ion of the hydroxyl-terminated domains with plate groups. A set of capillaries containing mixtures of lactide, bis-acplamide, N-acr i lsi lsucc i ida, azo-b? S-ci anovalérico acid, and nucleic acid probes fune i on with 11 Animo groups then come in contact with the aligned surface, aligning the capillaries with the domains terminated with acplato to place prepaid solutions containing specific probes in each domain. The capillaries in the set of capillaries contain spectral probes for a sequencing of nucleic acids of interest. The exposure of the small drops of prepolymers configured to ultraviolet light causes the formation of gels crosslinked in the substrate, each having a binding domain on the surface. The assay is carried out by treating the substrate with a mixture of samples that may contain sequences capable of binding to one or span of the binding domains presented on the gel surfaces in a regulated solution containing tppropylamina and sequences labeled with the ECL MARKER 1 that can compete with the analysts of interest to be bound on the surface. The linker domains (4200, 4203, and 4202) (in drops of pol lacp lick (4203) in a gold electrode (4232) are then placed in the vicinity of a working electrode IT0 (4204) as shown in FIG. Figure 42. The 3u: emitted from each of the link domains is quantified using a CCD camera (4205) and compared to the link domains for internal standards included in the sample solution 6.36 MULTIPLE SANDING TESTS OF HYDRATION OF ECL IN POLYACRIL MIDA SURFACES SUPPORTED IN AN ELECTRODE A matrix of exposed and exposed silicon substance of 1-2 microns to be thickened is prepared in accordance with well-known procedures to give pattern of circular depressions arranged in a A 10: 1 blend of SYLGAPD silicone elastomer 184 and the corresponding SYLGARD 184 curing agent is left in the matrix and cured.The packed SYLGARD is carefully removed from the silicon matrix. The stamp The resulting lastomeric is "inked" by exposure to a solution containing the hydroxylated thiol HS- (CH2) 11- (0CH2CH2) 3-0H (1-30 mM) in ethanol, is contacted with an aligned gold substrate and it is stirred. The substrate is washed for several seconds with a solution containing the thiol HS- (CH2) 10-CH3 (1-10 mM in ethanol). The resulting surface is then rinsed with ethanol and dried under a stream of nitrogen. Surface treatment »has a solution containing acylloyl chloride and triethyl sheet in diaxane causes the fune ionalization of the hydroxyl terminated domains with a-lane groups. A set of capillaries that contains? 06 mixtures of acnlamide, til s-acri lamide, N-acp 101 lsucc iniida, aza-bis-cyanovalépco, and nucleic acid probes functionalized with groups to ino then enter in contact with the aligned surface, aligning the capillaries with domains terminated with acplato to place prepolymer solutions containing specific probes in each domain. The capillaries in the set of capillaries contain specific probes for a nucleic acid sequence of interest. The e: position of the small prepolymer droplets configured to ultraviolet light causes the formation of crosslinked gels on the substrate, each having a surface binding domain. The assay is carried out by treating the substrate with a sample mixture which may contain sequences capable of being linked to one or more of the binding domains presented on the gel surfaces in a regulated solution which has a tnpropyl laminate. and sequences marked with ECL MARKER 1, which can link the apali or in non-complementary sequences on the probes fixed on the surface. The binding domains (4200, 4201, and 4202) (in polyacid lick drops (4203) at a gold electrode (4232) are then placed near a working electrode IT0 (4204) as shown in the figure 42. The light emitted from each of the domains is quantified using a CCD camera (4205) and compared to the binding domains for internal standards included in the sample solution 6.37 TOTAL TYPES OF DIFFERENT TYPES IN A SURFACE OF POLYACRILAMIDE SUPPORTED ON AN ELECTRODE A matrix of photoendu rec ib 1 e exposed and developed substance of 1-2 microns thick is prepared in accordance with well-known procedures to provide a pattern of circular depressions arranged in a set. 10: 1 mixture of SYLGARD silicopa 184 elastomer and the corresponding SYLGARD 184 curing agent is emptied into the matrix and cured, the polished SYLGARD is carefully removed from the silicon matrix. The result is "inked" by exposure to a solution containing the hydroxyl-terminated thiol HS- (CH2) 11- (0CH2CH2) 3-0H (1-10 M) in ethanol, it is contacted with an aligned gold substrate and it is stirred. The substrate is washed for several seconds with a solution containing the thiol HS- (CH2) 10-CH3 (1-10 mM in ethanal). The resulting surface is then rinsed with ethanol and dried under a stream of nitrogen. The treatment of the surface with a solution containing acnloil chloride and tneti laminate in dioxane causes the activation of the hydroxyl terminated domains with acrylate groups. A set of capillaries containing mixtures of acnlamide, bis-aoryl ida, N-acr i loi lsucci nimida, a aza-biscii anova lenco, and any of the binding reagents described in examples 6.31-6.36 enter after in contact with the aligned surface, aligning the capillaries with the finished domains with acplate to place prepol solutions containing specific probes in each domain. Each capillary in the capillary set contains specific binding domains for analytes of interest. The e: position of the small drops of prepolymers configured to ultraviolet light causes the formation of crosslinked gels in the substrate, each having a binding domain on the surface. The assay is carried out by treating the substrate with a mixture of samples that may contain analytes capable of binding to binding sites of binding domains presented on the gel surfaces in a regroded solution containing tppropi laminate and or well analogous dizziness with ECL MARKER of analytes competing with analysts for the binding on the binding domains and / or secondary binding reagents marked with ECL MARKER 1 on the analysts of interest. The binding domains (42 <> "> 0, 4201, and 4202) (in drops of pal lacp lick (4203) ep a gold electrode (4232) are then placed c & of a working electrode IT0 (4204) as shown in Figure 42. The light emitted from each of the binding domains is quantized using a CCD camera (4205) and will be compiled with 2 < "> 9 link domains for internal standards included in the sample solution. 6.38. ECL HIGHLY REVERSIBLE Gold electrodes pal icpstal ípos (purchased in Bia-Analy ical Services, 2mm2) were cleaned by manual polishing sequentially with an alumina paste of 0.5 μm and 0.03 μm, followed by chemical attack in 1: 3 H202 / H2S04 and cyc elc roqui co in H2S04 diluted between -0.2 V and 1.7 V versus Ag / AgCl. The cleaned electrodes were distilled overnight in a dilute solution of oethylthiol (CSSH) dissolved in ethanol. The protein adsorption was carried out by coating electrodes modified with C8SH with 20 μl of bovine serum albumin (BSA) labeled chron dialyser 1 in a saline solution of phosphate buffer (PBS, 0.15 M NaCl / 0.3 M NaPi, pH 7.2) and washing the surface extensively with the same regulator after a 10 minute incubation. An ECL was performed in a three-electrode cell with an Ag / AgCl reference electrode, a C3ble platinum counter electrode and an EG-potentiometer. > G 283. The intensity of the light was measured with a photometer from Pacific Intruments and a Hamamatsu photometer photometer placed at the bottom of the electrochemical cell. The electrode that adsorbed protein was immersed in a solution of 0.1 M TPA and 0.2 M phosphate, pH 7.2. A highly reversible ECL response (of substantially similar intensity in the forward and backward scans) was observed when the electrode potential was cycled between 0.0 V and 1.2 V, as shown in Figure 44A, which indicates the reversible nature of the ECL process and the stability of the thiol and protein layers in the electrode. Cyclical ethnic experiments were performed on the same instruments as for ECL, without the use of PMT and photometer. In the experiment, an electrode covered with CSSH (not protein) was placed in a 3 M solution of potassium ferricyanide (in PBS) and the electrode was scanned from • + 0.5 V 1.2 V back, and followed by another cycle between + 0.5 V and -0.3 V. It is indicative that the monolayer is still intact at 3.2 V, since there was only a capacitive current in the voltammogram between +0.5 V and -0.3 V and no faradaic current of ferpcyanide (Figure 44B). 6.39. ECL CASE REVEPSIBLE Electrode modifications and protein adsorption of > in the same way as 1 debed above. In the ECL experiments, the potential was explored between 0.0 V and 1.5 V, and the intensity of the corresponding light was recorded. As illustrated in Figure 45A, a significant loss of ECL was observed between forward and backward scans of the same cycle, as well as between 111 different cycles. Vol thiol cyclic tamograms / Au in ferricyanide after oxidation at 1.5 V showed a significant amount of faradaira current, indicating a partial desorption of the tial onalayer at 1.5 V (Figure 45B 6.40.) IRREVERSIBLE ECL In these experiments , modifications of electrode and protein adsorption were carried out in the same way as in Example 6.38. For medium 3, the electrification potential was explored up to 2.0 V and back to 0.0 V. An intense light was observed in the forward scan (more light than the one »was observed in reversible conditions in Example 6.38), but fell to the bottom in the reverse scan, as shown in Figure 46. Vol cyclic tam-grams of the modified electrode in ferpc Anuran after oxidation at 2.0 V indicated that the majority of the thiol monolayer was desorbed (Figure 46B) 6.41 AN ECL PUNISHED IMMUNOASSAY USING AN IMMOBILIZED PRIMARY ANTIBODY ON AN ELECTRO CONFIGURED GOLD DO In this example, an antibody against prostate specific antigen (PSA) is immobilized on a gold electrode configured for use in a PSA immunoassay. A matrix of photoendur- able substance exposed and developed from one to two microns thick is pire- red in accordance with! Well-known procedures for providing a coating of photocurable substance on a silicon support non? n square patch of 3 mm - > t mm where the sust.pcia fataenduree íble is removed. A 10: 1 mixture of silicone elastomer SYLGAPD 184 and the corresponding curing agent is poured over the matrix and cured. The SYLGARD pal imerized is carefully removed from the silicon matrix. The resulting elastomeric "stamping" is "inked" by its exposure to a solution containing the hydroxyl-terminated thiol HS- (CH2) 11- (QCH2CH?) 3-0H and the finished thiol cron the non-lotnacetic acid (NTA) ) (CH2) 11 (OCH2CH2) 30C (0) NH (CH2) 4CHCl2 H) N (CH2C02H2) in ethanol. The "inked" stamp comes into contact with a gold substrate and is removed to form a 1 mm x 1 mm SAM. The substrate is washed for several seconds with a solution containing only the hydroxyl-terminated thiol in ethanol, to avoid nonspecific binding of proteins over regions outside the stamped characteristic, the resulting surface is then rinsed with ethanol and dried. a stream of nitrogen. The treatment of the surface with a solution of N? C12 followed by treatment with a solution containing a fusion pratein presents the binding sites of an anti-PSA mouse monoclonal and the peptides < H? S) 6, leads to the immobilization of the fusion protein on the surface in such a manner! controlled This process offers a reproducible and predetermined amount of protein immobilized on the surface. The orientation of the protein on the surface is controlled by the location of the sequence (H?) 6 in the primary structure of the fusion protein. The absolute amount of immobilized pratein is controlled by the ratio between the thiol terminated with NEA and the thiol terminated with hydro i in the patterned SAM and chirping & The surface area of the property is piada. A calibration curve for PSA is determined by the preparation of solutions containing known concentrations of serum PSA (in concentrations ranging from 1 fM to 1 uM.) Numerous surfaces prepared in accordance with the above described are treated with the Calibration standards of PSA and then with a solution containing a secondary antibody against PSA (labeled with a MARKER 1 derivative) at an optimized concentration.The calibration curve is determined by immersing the surfaces in a solution containing 0.1 M TPA and 0.2 Phosphate. M (pH 7.2), and by measuring the peak intensity of the light emitted when the electric potential at the gold surface is cycled between 0.0 and 2.0 V at a scanning speed of 0.5 V / sec. The ion of unknown PSA concentrations in the serum in a sample is carried out by the same procedure except that the PSA concentration is calculated from the peak ECL signal by reference to the calibration curve. 7. INCORPORATION DF REFERENCES. The present invention is not limited in its scope to the specific embodiments described herein. Various modifications of the invention in addition to those described herein will be apparent to one skilled in the art from the foregoing description and the accompanying drawings. Such modifications eae > n within the scope of the claims. Many publications are mentioned in the present, their presentations are incorporated by reference in their entirety.

Claims (10)

1. CLAIMS 1. An adequate time for its detection in the detection of an anachronism by means of an electrochemi-collision that comprises an electrode and a counter-electrode, said electrode or counter-electrode has immobilized on a surface of the same tub a predetermined amount of a reagent capable of binding a speci fi c elec- trocally identi fi ed or a liaison partner of a species marked the ractol ici e u ni e.
2. 2. An apparatus for use in the detection of an analyte by means of electrostatic radiation or an electrode, comprising an electrode and a counter electrode, said electrode or counter electrode has immobilized on a surface thereof a predetermined amount of a reagent. able to link directly or indirectly to a marked species e1ect roqu ímicol? initiate 3. An apparatus for use in the detection of an analyte by electroquimi calumini scenc? To which comprises an electrode, said electrode has immobilized on a surface thereof a predetermined amount of a reagent capable of-? link a component of an assay of the t roquimi calumi linkage. 4. An apparatus according to claim 3 wherein said ctrode is the work elect. 5. An apparatus according to claim 3 wherein said electrode is the counter electrode. 6. An apparatus according to claim 3 wherein the immobilized reagent and the electrode complex allow substantially the transfer of electrons between said electrode and a marker the ecrt roqiu my colsminister ". 7. An apparatus according to claim 3 wherein said electrode consists of a porous material. 8. An apparatus for the detection of an analyte by the ectroquimicolumi nor scencia that compirende a porous electrode and a counter electrode. 9. An apparatus for its use in the detection of an analyte by means of electrochemistry! It is not a concept that comprises a locking electrode and a counter-electrode, said working electrode has immobilized on a surface thereof and in electrochemical contact with itself, a predetermined amount of a reagent capable of binding a component of a essay of elecrtroq? imi columini scencia de enlace. 10. An apparatus for its use in the detection of an apalite by means of electrochemistry! umi niscenci, comprising a working electrode and a counter electrode, said counter-electrode has immobilized on a surface thereof and in electrochemical contact therewith, a predetermined amount of a reagent capable of binding a component of a test of the ec troqu i ico! umi ni scene the link. twenty-one" 11. An apparatus for use in the detection of an analyte by electracj? Is it a collision, which comprises an electrode, an electrostatic cop and a piarosa matrix in contact? the ec trochemical with said electrode, said porous matrix contains on a surface of the same a predetermined quantity of a reagent capable of binding a candidate of a test of electroluminum here. 12. An apparatus for its use in the detection of an analyte by the ectrctquimicolu i mscen ». When an electrode comprises a plurality of discrete binding domains, said binding domains can link a component of a test of the chemical base. 13. An apparatus for use in the detection of an analyte by the ect roqui my col umiscenc la, which comprises a working electrode and a plurality of discrete binding domains each containing a predetermined amount of a reagent capable of binding - a component of an electrochemical link luminiscenci assay. 14. An apparatus according to claim 33 further comprising a counter electrode. 15. A compliance apparatus according to claim 13, further comprising a counter-ion, a spiosi 1 vo of »sample delivery and a light detection device. 16. An apparatus for s? use in the detection of an analyte by elec roquimicolumini scenc la, comprising (a) an electrode, (b) a plurality of discrete binding domains each containing a predetermined amount of a rapa reagent; of »linking a component of an electrochemical microlumi link binding assay, (c) a counter electrode, (d> a device for supplying samples to said link domains, (e) device for triggering the electrochemie col? i niseenc ia, and (f) device for detecting the ectroquimiealumi niscenc la 17. An apparatus for use in the detection of an analyte by electrochemicoluminiscence, comprising (a) an electrode, (b) a support that has immobilized therein a plurality of discrete binding domains each containing a predetermined amount of a reagent capable of binding a component of an elect roquimicolumi assay to the link, (< r) a corithra-tite, (ci) a device for provide samples to said link domains, < e) device to trigger the ct roquimicolumi niscencia, and (f) dispositi o piara to detect the elekquí! or initiation 18. An apparatus according to claim 17, wherein said plurality of domains are in electrochemical contact with said electrode. 19. A suitable unit according to claim 17, wherein said electrode is porous. 20. An apparatus according to claim 19, wherein said electrode is made of a carbon material. 21. An apparatus according to claim 17, wherein said electrode is formed of fibrils. 22. An apparatus in accordance with rei indication 37, wherein said electrochemi-luminescence detection device detects the elect roq? Imicsl? My mseenc one or spans of said discrete link domains. 23. A apiarate according to claim 17, wherein said support is a porous matrix. 24. An apparatus according to claim 37, wherein said support is a porous matrix and said electrode is porous. 25. An apparatus according to claim 17, wherein said support is a porous matrix, said matrix being positioned between said electrode and counter electrode. 26. An aparate, ptara its use in the detection of an analyte .0 by elect roquimicolumi ru serene ia, comprising (a) an electrode, (b) a plurality of discrete binding domains, each containing a predetermined amount of a reagent capable of binding a component of an eleetroqui micoluminiscane binding assay, ( c) a counter-electrode, (d) a device for supplying samples to said link domains, (e) a device for triggering the root cause, and (f) a plurality of devices for detecting the electrocolumini cenc la 27. A aptarate according to claim 26, wherein said plurality of devices for the detection of the electrsquimicaluminiscepcia is used to form an image of one or several of said link domains. 28. An apparatus according to claim 27, wherein at least one of said plurality of detection devices detects the electrochemical collision from a link domain, 29. An apparatus according to claim 27, wherein said The plurality of devices for the detection of electrochemistry is a set CCD or a set of diodes. 30. An apparatus for use in the detection of an analyte by means of the ect r-oquimicolumi or scenc 1a, comprising an electrode having immobilized on a surface thereof a plurality of cyclical binding domains challenges, said link domains can link a component of an essay of elec here icolu link iniscence. 33. A device for use in the detection of an apalite by electo roquim icol umi ni > -encía, comprising an electrode that »has immobilized on the surface thereof a plurality of discrete binding domains, each containing a predetermined amount of a reagent capable of binding a complementation of a bond electrochemi-luminescence assay. 32. A pair of devices? use in li to detection of an anatous by the ectroquimi columi mseencía, which comprises an electrode that has immobilized on a surface thereof a plurality of discrete link dominica, said link domains contain a marker the ec t raq? i icolum my be. 33. A apiarate for use in the detection of an analyte by the luminance rachine, which comprises an elec- trode that has immobilized a surface thereof a plurality of discrete link domains, said link domains can generate a plurality of electrochemical signals umi niscencí; and a counter-roll. 34. An apparatus for use in the detection of an analyte by means of elec troquimicolumi or scenerÃa, which comprises a support having immobilized there a plurality of discrete domains, each containing a predetermined amount of a reagent capable of binding a component of an assay of link electrocoluminiscence. 35. An apparatus for its use in the detection of an analyte by elec roqu i icolumi ni scenc i, comprising an electrode and a support having immobilized on a surface thereof a plurality of discrete binding domains, each containing a predetermined amount of a reagent capi to bind a component of an electrochemlycolumini bond assay, said electrode and said linker domains are in electrochemical contact. 36. An apparatus according to claim 35, wherein the elect is the blocking electorate. 37. An apparatus according to claim 35, wherein the electrode is the counter electrode. 38. An aptarate for its use in the detection of an anayte by electrochemical! uminiscence, which comprises: (a) a cell the chemical cycle, (b) a first surface containing an electrode, (c) a second surface that has immobilized there a plurality of binding domains, each containing? n binding reagent capable of binding a component of an electrochemical test! umi link mseepcia, said first surface and said second surface are spatially aligned to allow the transfer of electrons between said electrode and an electraquimical marker directly or indirectly linked over a binding reagent. 39. An apparatus for its u in the detection of a naïvet by elec uq? imicolumi ni cenc i, which comprises an electrochemical cell and an electrode having immobilized there a plurality of binding domains, each containing a capping linkage reagent to bind a component of an electrically inactive assay of in! ace 40. A method for carrying out a plurality of electrochemical tests, including the steps of: (a) p >contacting a plurality of discrete binding domains with a sample containing one or several analyte of interest or assay conditions; (b) use elec t rocal i niscenc a in one or more of said domains; and íc) detect the electrochemical! umi niscence in a plurality of said link domains. 41. A method for carrying out a plurality of electrochemical assays for a pillity of different analytes of interest, comprising the piasees of: (a) contacting a plurality of domains of discrete linkages with a sample containing a plurality of analytes of interest under test conditions; (b) using elect roqu imi col umi or using the said plurality of discrete link domains; and (c) detect simulously the PC i roqu i icolumi ni s > each of said discrete link domains. 42. An article comprising a plurality of discrete binding domains in a support, said binding domains having a relative spatial organization in relation to each other, and having different binding specificities for linking a plurality of different analytes of interest in an assay of The c roqui! umi ni cenc la. 43. An article comprising a plurality of discrete link domains on a support, each of said dominics having a relative spatial organization in relation to each other and each having a different fidelity of linkage different to an analogous one. In an interest in an electro-icolumi assay or a scenario, each domain contains a different binding component linked to an analyte of different interest. 44. An article comprising a plurality of discrete binding domains in a support, said domains having a relative spatial organization in relation to each other and each having a different binding specificity for an anchor of interest in an eq test. I, roqu imicolumi ni cenc. i a, c d domain is linked directly or indirectly with a different interest field and a layer: - e! eu troqu ímicol? mimscencía. 45. An article comprising a plurality of discrete binding domains in a sopearte comprising a thorny material, each of said domains having a relative spatial organization in relation to each other and falling one has a different binding specificity for an analogous one. In an interest in an elec- trochemical assay in the domain, each domain contains a different link component linked to an analyte of different interest. 46. An article according to claim 45, wherein said porous material comprises fibrils. 47. An article according to claim 45 wherein said porous material comprises carbon. 48. An article comprising a plurality of discrete binding domains in a support comprising a functional fibril 12 d, said domains having a relative spatial organization in relation to each other and each having a different binding specificity for an analyte of interest in an electrochemicoluminiscenei assay, each domain is directly or indirectly linked to an analyte of different interest and to a portion capable of ecotroquicum1um or scency. 49. An article comprising a plurality of binding domains in a support comprising tub or vain polymer matrices, said domains having a relative spatial organization in relation to each other and each having a different binding specificity for an analyte of interest in an essay on »the ec roqui mi col? mini scepcia, each domain is linked directly or indirectly to an analyte of interest and to a capar portion of e3 ect roqu imicolu i ni se ene i. 50. A cassette for its use in the detection of naïvetite in a sample by electrochemiluminescence, which comprises: (a) a plurality of domains of »discrete binding» a support; and (b) one or several electrode and control electrodes. 51. A cassette for using the detector of an analyte in a sample by means of electrochemical collisions, comprising: (a) a plurality of discrete link domains in a support; (b) one or more pairs of electrodes and with 3 ect odes spatially aligned with said discrete link domains; and < c > a device for supplying samples in said plurality of discrete link domains. 52. A cassette according to claim 49, wherein said plurality of discrete binding domains form at least one cap-surface of linking a component of a binding electrochemical and binding assay. 53. A cassette according to claim as claimed in claim 50, wherein said plurality of binding domains includes binding domains having different binding specificities to provide the simultaneous binding of a plurality of different analytes of interest present in a sample. 54. A cassette may detect or measure the electrolume clearance, comprising: (a) a first support having a plurality of discrete link domains in it; < b > a plurality of electrode and counter-electrode pairs, each of said plurality of discrete link domains is aligned with one of said plurality of electrode and counter electrode pairs that is close to said, said connection keys di.cr * = » The v pairs of electrode v cont raelect rodo form a plurality of cells to detect or carry out measurements of electrochemistry niscenc l, said pairs of the ectrode against the ectrode are steerable by a source of electrical energy in form of a »wave of voltage; 8 effective to trigger the ec t roquimicoluminiscen? and (c) device for supplying samples in said plurality of discrete link domains. 55. A cassette according to claim as claimed in claim 53, wherein said plurality of link domains includes domains of in! Acre having different binding specificities to provide the simultaneous binding of a plurality of different analytes of interest present in a sample. 56. A cassette p? At-3 detect or measure an analyte of interest in a sample, comprising: (a) a prime support having a plurality of discrete link domains on a surface thereof, at least one of said domains »discrete link is of different binding specifity» of the other link domains, each of said plurality of discrete link domains is hydrophobic and surrounded by hydraphobic regions; ib) a second support having a plurality of hydrophobic domains comprising suitable reaction media to carry out a chemical assay there; and e) the device pair-to contact said plurality of discrete binding domains and said plurality of reaction means in such a way that tina shows to analyze that it is present in each domain of link is found in t-> p contact ccan a means and reaction. 57. A cassette according to claim 50 wherein said discrete link domains further comprise an internal control. 58. A method for preparing a plurality of discrete binding domains on a support containing binding reagents capable of binding the analysts of interest, comprising the steps of (a) forming a single-sided on-the-shelf assay on a support said monolayer includes a linker group A on the monolayer surface not adjacent to the support, said first linker group A can specifically bind to a linker group B; and (b) contacting said first binding group A with a binding reagent capable of binding to an analyte of interest, said binding reagent being bound to said linking group B, such that said binding reagent is linked with said monolayer by a union A: B to form a binding surface, said linking surface is organized in the form of a plurality of discrete binding domains. 59. A process according to claim 57 wherein a plurality of different binding reagents is linked to the plurality of discrete link domains and wherein said step of contacting is carried out by means of or the supply of a plurality of fluid samples, each fluid sample includes a different binding reagent, on said monolayer from tub plurality of end guides. 60. A method for detecting or measuring an analyte in an electrowinning-up-link assay, comprising the steps of; (a) contacting a plurality of discrete binding domains immobilized on a surface of one or several supports with a sample containing a plurality of analytes and a component of said assay linking to a tag of the instrument. micol umi niscene ia; (b) the application of an effective voltage waveform to trigger the electromagnetic activity or scenc. a in one or several domains in the presence of a suitable reaction medium to carry out a test of e1ec t roqu ínurolumi niscenc ia; and < «~) The detection or measurement of the electo-chemical! umi or scenc i a parti of said plurality of children. 63. A set of elements for use in e3 performance of a plurality of essays of the ect roc olume um irascence for a plurality of analysts of interest, comprising: (a) an article that comprehends a plurality of » discrete link domains are a support, said link domains have a relative spatial organization in relation to each other and have different binding specificities for a plurality of different analytes of interest in a test rie elect roqu imicolu iniscenc la; and (b) a container containing a reagent necessary to carry out said tests. 62. A set of axis elements according to the indication 60 which also includes an apparatus for carrying > - Open those trials. 63. A set of elements for use in the completion of a plurality of electrochemical assays for a plurality of analysts of interest, which comprise a container that contains specific binding components for a plurality of analysts. different for its use in a plurality of trials of electroquimicolumi nisceneía. 64. A set of elements in accordance with the rei indicated in claim 62 further containing one or more containers containing non-binding campion-receptors for a plurality of tests of the three-dimensional and one-phase scenarios. 65, IWx set of elements according to claim 62 which further contains an article comprising a plurality of discrete link domains on a support, said e-mail domains have a relative spaepal organization in relation to each other and have a specificity of different linkages for a plurality of different analytes of interest in an essay of the ec roqu ii columi ni cenc í. 66. A cassette comprising: (a) a plurality of discrete link domains in a support, forming at least one link surface; (b) a plurality of pairs of electrodes and contracts! ct rodos, where said discrete link domains are spatially aligned with a plurality of pairs of electrons and contracts! ecdos and (c) a device for supplying samples in said plurality of discrete link domains. 67. A cassette comprising: (a) a plurality of discrete link domains in a support, forming at least one link surface; Y (b) a plurality of pairs of ele > zt rods and counter electrodes, wherein said discrete binding domains are spatially aligned with said plurality of electrode and counter-electrode pairs and can approach said pity of electrode and counter electrode pairs, where said binding domains are hydrophobic or hydrophobic in relation to the surface of the support. 68. A cassette q comprising: (a) a plurality of discrete link domains in a first support, forming at least one link surface; (b) a plurality of pairs of electrodes and counter electrodes, wherein said discrete link domains are spatially aligned with said plurality of electrode and counter electrode pairs, the plurality of electrodes being located on said interface, each electrode adjacent to a link domain, and the encrypted terminals are in a second sop >; and (c) a device for supplying samples to said plurality of discrete linking domains. 69. The cassette according to claim 6 > 8 wherein said binding domains are hydrophobic or hydrophobic in relation to the surface of the support. 70. A cassette in accordance with rei indication 66, where said support contains from 2 to 500 link domains, 71, A cassette according to claim 66, wherein said plurality of binding domains comprises binding domains that have different binding specificities to provide the simultaneous binding of several different anion rings of interest present in a sample. 72. A cassette for detecting to measure the electrochemistry lu iniscenci, comprising: (a) a first scant having a plurality of discrete link domains there; (b) a plurality of electrode and counter-electrode pairs, said plurality of discrete link domains is aligned with said plurality of pairs of electrodes and ceantra-electrodes and in the vicinity of said plurality of pairs of elect These discrete and discrete linking domains of the electrodes and counter-electrodes form a plurality of beliefs to detect or carry out measurements of the electrolu- turity or scenarios, said parameters. of electrodes cont rae! Echoes can be directed by a source of electrical energy in the form of an effective voltage waveform to trigger the e f i c i i i i i i i i c i i c i i i i i i i i i i i i i i c i c i i i i i i c i i i i i i i i i i i c i i i i i i i i i i i i i i i i i i i i i i i i i i i i i c (c) a device for supplying samples on said plurality of discrete link domains. 73. The cassette in accordance with the rei indication 72 also comprises a second holder capable of collocating adjacent to said first support to provide a device that has samples therebetween, wherein said plurality of electrode pairs and contract! ect reluctant to rely on the same afterwards. 74. The cassette according to claim 72 wherein said plurality of pairs of electrodes and counter electrodes is fixed on said first support. 75. The compliance cassette according to claim 72, further comprising: a second capric support to be positioned adjacent to said first implant to provide a device containing samples therebetween, wherein a plurality of electrodes is positioned in said first abutment. The support and a plurality of counter electrodes are positioned on said second support, in such a way that said plurality of electrodes and counter-electrodes are positioned close to each other. 76. The cassette according to claim 72 wherein said plurality of discrete link domains contains from 5 to 1 00 link domains. 77. The cassette according to claim 72 wherein said plurality of discrete link domain comprises at least one link domain that contains link reagents that are identical to each other and that differ in speci? Cation. The fidelity of the binding reagents contained within other link domains, to provide the link of multiple analytes of different interest. 78. The cassette according to claim 72, wherein said plurality of discrete binding domains comprises at least one binding domain which has binding reagents that differ in terms of binding strength. 79. The cassette in accordance with claim 78, that '~ > ~ r t- further comprises a reflecting sill adjacent to said first support or to said second support. 80. The cassette according to claim 78 provides said first support and said second support, the plurality of discrete link domains and the plurality of electrodes and counter electrodes are substantially transparent. 81. The cassette according to claim 72 wherein said pairs of electrodes and read cores are within a size range of 0.001 to 10 mm in diameter or width. 82. The conformity cassette erort claim 8. where said link domains are within a range of sizes> 0.01 to 10 mm in diameter or width, 83, the cassette according to claim 72, wherein said pairs of electrodes and counter electrodes can receive power from ? at least one source of electrical energy separately. 84. The cassette according to claim 72, wherein said binding domains are hydroflils and e ~, t5n surrounded by a surface hiofof óbca. 85. The cassette according to claim 72, wherein said domains of enl.ee are hydrophobic and are surrounded by a super fi cial surface. 06. The compliance cassette c. Claim 72, wherein said bonding surfaces comprise a self-assembled monolayer, conf igg. 87. The cassette according to claim 86, wherein said self-assembled monolayer configured comprises 5 l candioles. 88. The compliance cassette according to claim 87, wherein said binding domains can be bound to selected analytes within the group consisting of proteins, nucleic acids, carbohydrate moieties, antibodies, or antigens, cells, organic compounds, and organic compounds nomics. 89. The compliance cassette cron 13 claim 70, where di dios binding domains contain functional reagents in selected trials within the group consisting of clinical chemical assays, q? Imial? Miniscenc 1 assays, immunoassays and assays with probes from ác nucleic ideas. 90. The compliance cassette with the rei indication 73, which further comprises a removable electrode protection barrier interposed between said second support and said discrete link domains, said electrode protection bar can be removed before trigger that e lec t n1seenc roqu1m1co1u 1 1a. 93, the cassette according to claim 72 can, in addition to 5-compr therefore an electrically conductive material on 38 a plurality of electrodes of said pairs of electrodes or adjacent to a plurality of electrodes of said pairs of elements, positioned to move an electric potential away from the electrode surface in a test means, 92. A p To measure the electrochemical quality of my sample, which comprises; (a) a plurality of cells for containing at least one sample, said plurality of cells being formed from a plurality of pairs of electrodes and counter electrodes and a first support comprising a plurality of link domains, said plurality of discrete bonding domains is aligned with the plurality of pairs of electrodes and counter-electrodes and close to said plurality of electrode pairs and against the ectrodes, said pairs of electrodes and counter electrodes can receive epergery separately, said cells are suitable for carrying carried out measurements of e 1 t e t roqu im itro 1 < tm i n i se ene i a, < b) a voltage control device adapted to apply a controlled oxygen waveform to said plurality of electrode and control electrodes, said voltage waveframe being effective to trigger electrochemical inactivation in said plurality of electrodes; cells; and (c) a photon detecting device for detecting the electrochemical immunology of said sample. 93. A set of elements suitable for measuring the electrochemical! uminiscencí to, or comprises one or more lenses rec tp (a) a plurality of discrete domains link in a support, forming at least one surface of "link; and ib) a plurality of pairs of electrodes and counter electrodes spac ally aligned with said plurality of discrete link domains and which can approach said plurality of discrete link domains. 94. The set of elements according to rei indication 93, further comprising at least one second support capable of power- positioned adjacent said support surface to provide a link that dispeasitivo "contains samples. 95. The set of compliance elements according to claim 94, wherein said second support carries said plurality of pairs of the ect surrounds and counter electrodes capable of being aligned with said plurality of discrete link dominica and approaching said plurality of domain names. enl ce di cre eas. 96, The set of compliance elements > .on claim 93, further comprising reacti os suitable for performing an assay of elec traquimicol uimniscene Ia a predetermined amount of an analyte of interest p? i f i 40 97. A cassette for detecting or measuring an ana litho of interest in a sample, q? E comprises (a) a first support having a plurality of discrete domains of1 link on the surface thereof to form at least one bonding surface, at least some of said discrete link domains have different binding strengths and other link domains, each of said plurality of discrete link domains is hiphofilic and is surrounded by chopping regions. rofobic, and (b) a second support having a plurality of hybrid domains comprising suitable reaction means for carrying out a chemical assay there to form a test surface, said plurality of discrete binding domains and said plti lity of said reaction means may come into contact in such a way that a sample to be analyzed that is present in each binding domain is in contact with a reaction medium for detecting or measuring a third of a mth-s . 98. The cassette according to claim 72, further comprising a temperature control device. 99. A cassette to carry out a reaction of interest, comprising: I (a) a first support having a plurality of discrete domains on the surface of the support, each of said domains is hydrophilic and is found by a hydrophobic region on said surface "first support"; and 5 ib) a second support having a plurality of discrete domains on the surface of the second scaffold, each of said domains (i) is hydrophobic and is surrounded by a hydrophobic region on said second support surface, (11) It comprises a suitable reaction medium to carry out a rea? g? can be of interest, and iii) is located spatially aligned with the domains in said first support surface of such a tile that said second support is located to contact each of said domains in said second support surface ccan a domain aligned on said first support surface. 100. The cassette according to claim 66 wherein said discrete link domains further comprise an internal control. 101. The apparatus according to claim 92 in < "J wherein said plurality of discrete link domains includes at least identical link domains 102. A link surface which is the product of the following process: (a) the formation of a self-contained monolayer e" n? In this case, said monolayer comprises a first binding group A on the surface of the monolayer not adjacent to the support, said first binding group A can specifically bind on a second group of link B, said layer is applied at least to a domain in said support, and 5 (b) contacting said first linkage group A will create a linkage reagent, said linkage reagent can be linked to an analyte of interest, which link reagent is linked to c) said linking group B, such that said binding reagent is linked to said monolayer by means of an A: B bond, forming a binding surface, said link surface being organized in the form of a plurality of domains of discrete link qu e contain said reagents in the link capable of binding to an analyte of interest. 103. An apparatus comprising the attachment surface of claim 102. 104. The cassette according to claim 106 wherein said support comprises an elastoreic material. 305. A process for the preparation of a plurality of < "J discrete link domains in a support, which compose" the steps of: (a) forming a monocoque to an assembly on a support, said monolayer comprises a first linkage group A on the surface of the monolayer not adjacent to the support, said first link group A can be linked speci fi ciently with 24" a second link group B, said monolayer is applied to at least one domain in said support; and ib) contacting said first binding group A with a binding reagent, said binding reagent can »bind to an analyte of interest, said binding reagent is linked to said linking group B, in such a way that said tie reagent is bonded to said manolayer by means of-? A link A: B to form a binding surface r, said binding surface is organized as a plurality of discrete binding domains containing said binding reagents capable of binding to each other an analyte of interest. 306 ,. The process according to claim 10 wherein in step (a) said monalayer is produced in the form of a pattern on said support by a sele > rrc? onaclo within the group q? e consists of chemical mieroataque, deposit with micros 11 ete and microstamped. 107. The process according to claim 105 wherein said binding reagent is selected from the group consisting of proteins and fragments derived from the genesis, and nucleic acids and fragments and derivatives thereof. 108. The process according to claim 105, wherein said binding reagent is selected from the group consisting of antibodies and binding fragments thereof, antigens and epigens, cells and cellular components, enzymes, enzyme substrates, lectins, protein A, protein, organic compounds, organometallic compounds and carbohydrate compounds. 109. The process according to claim 105, wherein said binding reagent comprises a plurality of different binding reagents, and said contacting step is carried out by supplying a plurality of fluid st, each sample of fluid comprises a different binding reagent, on said cartridge to pair a plurality of fluid guides, such that discrete binding techniques on the binding surface in said mopolayer have different binding reagents attached there. 110. A method to detect or measure the ectrochemicol? im scence, which comprises (a) the contacting of a plurality of discrete bonding domains located on a surface of one or several supports with a sample that connects molecules together-i a matrix e? 3 ec oqu i >; .olum? n? scen e; (ti) apply an effective voltage canon array to trigger the electrocolumnum in each of a plurality of pairs of electrodes and counter electrodes spaced aligned with said plurality of do i ni > discrete link lines and in the vicinity of said plurality of discrete link domains, and (c) detect or measure said electrochemical imaging. 111. The method according to claim 1, wherein said plurality of discrete binding domains is within a range of 5 to 100 binding domains. 112. The compliance method > rron of claim 110, wherein said plurality of iscrete linker domains comprises at least one binding domain containing identical linking reagents therebetween and which »differ in specificity of reactive link reactants contained within other binding domains , can provide the link of multiple analysts of different interest. 113. The method according to claim 110, wherein said support comprises a reflecting surface. 114. The method according to claim 1, wherein said support, the bonding surface and the pairs of electrodes and counter electrodes are substantially the same. 135. The method according to claim 310, wherein said link domains are within a range of sizes ele? 0.003 to 10 mm in diameter or width. 116. The method of conformance with the indication 110, wherein said electrode and counter electrode pads can receive energy separately from at least one source of electrical energy. 117. The method of compliance according to the indication 130, wherein said binding domains are hydrophilic and are surrounded by a hydrophobic surface. 118. The method according to claim 330, wherein said binding domains are hydrophobic and are surrounded by a hydrophilic surface. 119. The method of conformance with claim 110, wherein said link domains are self-assembled, configured monolayers, 120. The method of conformance refers to the claim 119, where said link domains can be linked separately with "n". selected analyte within the rupee which consists of proteins, nucleic acids, carbohydrate moieties, antibodies, antigens, cells and cellular components, organic compounds, and organogenic compounds. 121. The method of conformance with rei indication 110, wherein said method comprises further contacting said link domains with a suitable reaction medicament to perform a selected assay within the rump consisting of clinical chemical assays. , immunoassays as well as tests of nucleic acid probes. 322. The method according to claim 110, 24: where said "various" or "multiple" support is a plurality of supports placed in a stack and at least a part of said drowsiness is substantially transposable to the light generated by the ect rachimicol inini scency, each of said plurality tieportes is ptosipona adjacent to another of said supports. 123. A method for measuring or measuring the ecrtroquimieolumim scenc i a in a sample, comprising (a) contacting one or vanes of a plurality of discrete link domains, said plurality of link domains being located on a surface of one or several supports, with a sample comprising molecules linked to one another. electrolysis marker, where a plurality of pairs of electrodes and counter electrodes are spatially aligned with said plurality of discrete binding domains, wherein said plurality of pairs of electrodes and counter electrodes is present on a second support surface, (b) said second support surface near said link surface such that each of said pairs of electrodes and counter electrodes is close to a different bonding domain ", (er) applying an effective voltage waveform to trigger the ectrochemical col umipisceneía in each of said plurality of pairs of electrodes and ccantraelectrode, and (d) detect or measure said elect roquimieol ? miniscene. 124. The method according to claim 130 wherein during step (a) a plurality of pairs of electrodes and counter electrodes is protected from the sample by a removable electrode protection barrier, and said method further comprises removal. of said barrier before applying d? >; ~ There is a volta wave shape. 125. A method for detecting or measuring ana lytes of interest in a sample comprising the droplet ctalocation of a sample containing an analyte to be detected in a plurality of discrete binding domains on a support surface. , said plurality of discrete linker deaminies comprises at least one linker domain containing linker reagents that are identical to each other and q? e differ in specificity of link reagents contained within other linker domains, each said discrete binding domains are characterized to be either hydrophobic or hydrophilic, provided that the said support surface region surrounding said binding domain is (i) hydraphically if said binding domain is hydrophilic, and (ii) hydraphilic if said binding domain is hydrophobic, to allow said analyte or said analytes of interest in the sample to be linked. p) with said link domains, and (b) bringing said drops into said first support with a surface of a second support having a plurality of discrete hydrophilic domain comprising suitable reaction means for carrying out a chemical test there, and ( c) determine the presence of said analysts of interest linked to said eplace domain. 126. A method for detecting or measuring analytes of interest in a sample, comprising (a) placing drops of a sample containing an analyte to be detected or measured in a plurality of discrete link domains on a support surface, said plurality of discrete binding domains comprises at the meneas a binding domain q? e contains binding reagents which are identical to each other and which differ in specificity from reactive binding readings contained within other binding domains, one of said discrete binding domains are characterized as either hydrophobic or hydrophilic, provided that the region of said support surface surrounding each of said binding domains is i) hilofobic if said enl ce domain is hydrophilic, and (ii) hydrophilic if said binding domain is hydraphobic, in order to allow said analyte to said analytes of interest in the sample link in) with said binding domains, v ' (b) placing drops of a reaction medium in said sample drops; c) determine the presence of said analytes of interest linked to said domain link. 127. A method for detecting or measuring electrochemiloluminisception in a sample comprising the following steps in the established order: ia) contacting a sample with a support surface, said surface containing a plurality of discrete link domains, said domains The linkers are spaced aligned with a plurality of pairs of electrodes and counter electrodes and can approach said plurality of pairs of electrodes and counter electrodes; (b) approaching said link domains with said plurality of electrode and cranked electrode pairs; (e) apply an effective voltage waveform to trigger the ecol i i col i i serene; d) detect or measure e leetreaq? im icol umi ni scenc la. 128. A method for detecting or measuring elec t roqu i mi columi or scenc i a in a sample that runs: (a) contacting a sample with a surface of a support, said surface contains a plurality of discrete link domains; (b) explore a pair of electrodes and counter electrodes on the surface of said support in the vicinity of said Ü51 Link domains, while applying an effective voltage waveform, will trigger the ecchyme collision; and (c) detect or measure the elec trochim icumumi or scenc l. 129. The process according to claim 109 wherein each of said domains is pre-prepared such that it is spatially aligned with a plurality of electrode pairs > counter electrodes and near said plurality of electrode pairs and with rae! ec rodos. 130. A method for detecting or measuring an analyte of interest in a sample, which comprises: (a) contacting a sample with a surface of a soup, said surface contains »> In a plurality of discrete link domains, said link domains are spiked with a plurality of electrode and chronoelectric pairs and can approach said plurality of electrode and counter electrode pairs, said link domains (i) having a eleetroquimicoluminiscente marker, and < p) can be linked to an interest field, and where such contact is made in • -einei i < .. such that the link of any dispute in the sample with said link domains may occur; (b) approaching said link domains to said plurality of e-lec t and counter electrode pairs; (c) apply an effective voltage waveform to trigger the elec- tricultural voltage.; (d) detect or remove the electrochemical collision, where a decrease of the electrophoresis in relation to the elec- trochemicals is observed when the contacting process is not carried out; It takes the goat in the absence of any interest in the sample, indicates the presence or quantity of said sample in the sample. 3 ^. A method for detecting or measuring an analyte of interest in a sample, comprising: (a) contacting a sample with a surface of a sopearte, said surface containing a plurality of discrete binding domains, said link domains being they find themselves aligned with a plurality of pairs of electrodes and contraelects surrounded and can approach said plurality of pairs of electrodes and counter electrodes, said linking domains can bind an analyte of interest, wherein the contact is re-contacted. liza and conditions such that the linkage of any anal i te in the sample on said binding domains, and where said sample contains molecules that are placed in a sample create a marker the ec t roqu i mi columis niscente; (b) bringing said link domains to said plurality of electrode pairs and contracting lecdo; íc) apply an effective voltage waveform for ¿71. to unleash the ect roqu) my col? my ni scenc ía; and (d) detecting the electrode and the columninization, where an increase in electrochemistry or concentration compared to background levels indicates that the amount of analyte in the sample is 3 ppm. 132. A method for detecting or measuring an analyte of interest in a sample, comprising: (a) contacting a sample with a surface of a support, said surface containing a plurality of discrete link domains, said domains of link are spaced 3 aligned with a plurality of pairs of electrodes and with rae! In this way, and can be applied to said plurality of pairs of electrodes and counter-electrodes, said binding domains can bind an analyte of interest, wherein said contacting takes place under conditions such that the eplace of any analyte in the sample with said link domains; ib) contacting said link domains with a link partner of the analyte of interest, wherein said enl a ce partner is attached to an electronic arcadcar? ímicoluminiscen e; Ic? bringing said link domains to said plurality of electrode and counter electrode targets; id) apply an effective voltage waveform to trigger the ec troqui íe olu i niscepci; and íe > ) detect or I go the eler t roq? i my colu ini cenc a, where an increase in mycoluminescence electrcaqu ion compared to background levels indicates the presence or quantity of the analyte in the sample. 133, The method of conformance according to claim 133, wherein steps ía) and (b) are carried out directly. 134. The method according to claim 131, wherein step (a) is carried out before step (b); and the gap of the binding domains to remove the unbound analyte is carried out after step (a) and before step ib). 135. A method for detecting or measuring an analyte of interest in a sample, comprising: (a) contacting a first sample with a surface of a support, said surface containing a plurality of discrete link domains, said domains eie link are aligned with a plurality of electrode and counter-electrode pairs and can approach said plurality of electromechanical sites and > Ontraelectronics, in dcande said sample contains an analyte of interest linked to a marker the ec + toqu i i col um ru scen te, where said contacting is carried out under conditions such that said analyte in the sample can be linked with said link domains; (b) contacting a second sample with said binding domains, under conditions such that the binding of any analyte in said second sample to said binding domains may occur, wherein an electrochemical marker is present; umi teacher is not linked to any ana lito in said second sample; i c) bringing said link domains to said plurality of electrode and chronoelectric pairs; (d) apply an even effective voltage waveform. unleash the el ec roq? imicolu i niscenc í; and íe) detect or measure the elect roqu í icoluis n, where a decrease in the electromechanical uminiscence compared to the electraq? imicolumin scencr observed when step (b) is omitted or when no hr; and ana lito in the second sample, indicates the presence or quantity of the analyte in the sample. 136. The method according to claim 331 wherein the sample is derived from a mammal, and wherein said method is used to determine or confirm the identity of the mammal. 337. The method according to claim 333 wherein the sample contains cells from a mammal, and said method is used to quantify the number of cells in said sample. 138. The method for carrying out a "interest" reaction, comprising: ía) applying a sample to each of a plurality of discrete domains on the surface of a first support, each of domains domains is hi drof ilic, and is surrounded by a hydrophobic region on said first support surface; and (b) limiting a second support having a plurality of discrete domains on the surface of the second support, each of said domains i) is hydrolyzed and surrounded by a hydrophobic region. in said second support surface, i) comprises a reaction medium suitable for carrying out a reaction of interest, and iii) is especially aligned with the domains on said first support surface, to contact each one of said domains in said surface of second .. support with a domain aligned on said first support surface, such that said sample is in contact with said reaction medium. 139. The method according to claim 109 wherein said plurality of fluid samples are concurrently supplied in said monolayer. 140. The method according to claim 33 < "> wherein said support comprises a material the eternal handle 341. The method according to claim 139 wherein said self-contained, monolayer monolayer configured comprises alkntiole-j. 142. A method for detecting and measuring an analyte of interest q? ee omp rende: (a) contacting one or several discrete link domains of a plurality of discrete link domains, said plurality of link domains being found at x> a surface of one or so-so carriers , wherein said contacting is performed with a sample comprising molecules linked to an ectrocyte and columnar marker, where said sample is not in contact with electrodes or counter electrodes during said contact step; (b) aerercar an electrode to one or more binding domains to said plurality of binding domains, (c) applying an effective voltage waveform to trigger the ect roquimicol? miniserepe in one or several domains of linking said plurality of link domains; and (d) detecting or measuring the eleet roqu i ieolumi niscenc? a 143. A method for detecting or measuring an analyte of interest, which comprises: (a) contacting one or more discrete link domains, of u? - The plurality of link domains, said plurality of link domains (i) being located on a surface of »tino or several supports, and iii) it is! The space is aligned with a plurality of electrons and with a s-electrode and close to said plurality of pairs of electrodes and contracts reads, wherein said contacting is carried out with a sample comprising molecules linked together to readear e1eet roqu imirolttmi n iscente; (b) bringing one electrode and counter electrode closer to one or more dominics of said plurality of link domains; (c) applying a form of effective voltage cannula to trigger electrochemist-minisection in one or several link domains of said plurality of linkages; and (d > detecting electrochemical measurement.) 144. A cassette comprising: (a) an electrode that contains on its surface a predetermined amount of a material that comprises binding reactors organized in? In a discrete link domain or in several discrete link domains, said link reactivations can be specifically linked to a molecule carrying an electrochem micolumi piscent tag or a "link partner" of a molecule carrying an electrochemical tag. Is the electrons between the said electrode and a chemical electro-marker capable of transmitting electrons? i niscente in said molecule with .59 The electronic marker is connected to said binding reagent or to said binding partner when said partner is linked to said binding reagent or (11) allows said electrode to generate photons from said electronic tag. niscente; and ib) a counter electrode. 145. A cassette comprising an electrode containing on its surface a predetermined amount of a material comprising binding reagents organized in one or several discrete binding domains, said binding reagents are marked in an electo- logical or iniscent manner, and said material allows the transfer of electrons between said electrode and said electrochemical marker! umi niscente. 146. The confectionery cassette with claim 143 wherein said elect spray is porous. 147. The cassette according to claim 144 wherein said electrode is porous. 148. A cassette comprising: (a) a support having one or several discrete eplace domains containing linkage reagents; (b) an ionically porous porous matrix, said binding domain is bonded to said porous matrix; (c) an electrode in electrochemical contact with said binding domain; and (d) a con rae! ec trodo 149. A cassette conforming to claim 147 where the rea? _ I vo ~ > de enlate- »are mar-erados para Electrochemical! umi ni he & ?Inc . 150. A cassette that completes: a) a linkage domain that connects with reagents; and (b)? n porous support, said binding domain is linked to said porous support, said porous support is an electrode in electrochemical contact with dirho binding domain. 151. The cassette cié '-'- informid > _on the rei indication 149 that r omp in e also? n contrae »! ee rodo. 152. The cassette according to claim 150 wherein said binding reagents are covalently linked to said electrode. 153. A cassette comprising; (a) a first support having a first surface containing an electrode; and ib) a second sopearte having a second surface that contains a link domain, said first surface and said second surface are spatially aligned to each other. oncac to elec t oqu icu. 354. A set of elements comprising: (a) a first support having a first surface than with a first one; (b) a second scaffold that grounds a second surface containing a domain and bond, said binding domain contains a predetermined amount of binding reagents, said first surface and said second surface are spatially aligned, it is reliable to establish a con ta te ec t roquími co; and (c.) fr-asco that »contains a species marked for electroquimicciluini ru scenc. a. 155, A cassette that »understands! (a)? n prime support u has a first surface that contains an elec- trode; and ib) a second sopor-t having a second surface containing one or more discrete binding domains, said first surface and said second surface being aligned spatially to allow the transfer of electrons between an electrochemical marker ! ? i associated with the link domain and the electrode. 156. The cassette in accordance with the rei indication 154, wherein the second surface is a porous material, and said cassette further comprises a counter electrode. 357. A cassette that you understand ía) an ele ", fcrodo that has a first surface; íh) a c on rae! Echoed to f * has a second superfi * le; c) a porous material between said first surface and said second surface, said porous material contains reagents that can bind a molecule seated for eleca rcaquimic olumum or eneya, said porous material and said first surface they are spatially aligned to allow the transfer of electrons between a marker and the columnar ect in a molecule attached to one or more of said binding reagents and said first surface. 350. An eg cassette comprises: (a) a porous electrode; ib) a contrsel ec t oclo; ee) a support having a plurality of discrete link domains there, said link domains being spiked 1-to-one allowing the transfer of electrons between a species targeted for the rachimi! uminiscenc i, bonded on the binding domain and said porous electrode. 159. A case that you understand (a) a porous electrode; and (b) a counter electrode; said porous electrode contains in s? surface a material that includes reagents of bonding, dichea material allows the transfer of electrons between said ele- ment and? n ma elect roqu inticolum i scented actor united to one or several of said reagents of link ?. 160. A cassette that you understand (a) a support that has a plurality of discrete link domains there: (tt)? n a pair compartment to transpirate fluid to said link domains and outside of said link domains; and c) a spatially aligned electrode and counter-electrode to generate a signal ee. t roq? i my col? miniscente from a marker the ect oq? iico? my ru scente attached to this plurality of domain- »enl ce. 161. A cassette comprising: (a) an electrode containing on its surface a plurality of discrete link domains; and ib) a contract! ec 1 rodo. 1 2, A cassette comprising: (a) a plurality of discrete link domains in a sop e; (b) an electrode; and (c> a counter electrode, said electrode can generate a plurality of electrochemical signals from a plurality of electro-luminescent markers linked to said plurality of challenging link domains. rei indication 163 in deande »said plurality of minios cié link contains a marker the fctroqui initial my mseente, and where the cassette also contains? p disposi ti see to provide samples in said plurality of dominicas cié discrete link. cassette of the rei indication 163 which further comprises a positive signal for supplying samples op to said plurality of discrete binding domains 365. The cassette of the relay 160 where said electrode can generate a signal elecrally and electrically from a marker the urruni cente ectech associated with at least one of those link domains 166. A cassette that assimilates: (a) a support that has ne a plural icrlad of domains in 1 are discrete there; and ib) one or several pairs of electrodes and counter-electrodes. 167. The cassette of claim 165 cj? E further comprises a device for supplying samples in said plurality of discrete link domains. 16B. A set of elements that comprises: (a)? N electrode that contains »in s? surface discrete link domains organized in a configuration; (b)? complying to transport fluid haepa said link domains outside said link domains; í > _) a counter-study; and (d) a vial containing molecule dizzy for ele. troqu i mi r.olu initiate. 169. A ca sette that comprises! ia) a plurality of discrete binding domains bonded to an electrode, said electrode being close to an ionically porous porous m tnr; and ib) a contr e! ec sprinkled 170. A cassette comprising: (a plurality of discrete binding domains, said linking domains are linked to an ionically porous porous matrix; ib) an electrode close to said ionically permeable matrix: and (c) a counter electrode. 173. A cassette comprising: (a) a plurality of binding domains, said linking domains are linked to a loosely permeable porous matrix; and (b) an electrode in electrochemical contact with a field of said link domains. 172. The cassette of the vindication 170 which also comprises a counter-roll. 173. A cassette comprising: (a)? A plurality of discrete link domains, said plurality of link domains are in: - ados with? N so porous porous; and b) an electrode in electrochemical contact with a plurality of said link domains. 374. A cassette comprising: (a) an electrochemical cell comprising an electrode, a c > int raelec rodo and an ionic solution in contact with said ^ 6 electrode; and < b) a support ejue has a plur-ality of domains of > discrete link there, said plurality of link domains are in electrochemical contact create cucho electreado. 175. The cassette of claims 343, 144, or ca 160 wherein the electrode comprises carbon fibrils. 176. A method for detecting or measuring the electrochemistry and collimation, which comprises (i) contacting the binding reagents in the cassette of claim 143 with a sample that contains molecules linked to an elect i my col umi pi scente; ib) Apply an effective voltage waveform to trigger the elec roq? Ieolumi does not even appear in said ecothrope and contracts! ec t rodo; and (c) detect or measure said elect roqu imicolu t or scenc a. 177. A method can be used to define or measure the design and implementation of the scenarios, which includes: (a) contacting the linkage reagents in the cassette of the re-in ation. shows that it comprises molecules > - »nlaza» ias to a marker e 1 ec t roqu imii o 3 um i n i s ». < b) apply an effective voltage waveform to trigger the elec troch i micolumi niscenc i a on said electrode and continue to read t roclo; and íc) to detect or to go to said ele "c t roquimicolumi rusc ene la. 378. The method of conformity > J ccan the rei indication 175 where »said electorate is porous. 179. A method for detecting the measurement of the ect roc my my piscenc ia, which understand (a) contacting the binding reagents in the cassette of claim 144 with a sample comprising mol 'ul -? They are linked to an electronic scoreboard. ib) apply an effective voltage waveform to trigger the electron taq? imicolumi niscenc ía in said the node ect and cont.r.el ect rodo; and (c) detecting or measuring said electromagnetic spectrum. 380. A method for detecting or measuring electrochemistry, which comprises: (a) contacting the binding reagents in the cassette of claim 350 with a sample comprising molecules eny to them? n scoreboard e1 ec t roqui ico1um i ni scente; ib) apply un-? form »: the effective voltage wave p =. to unleash the elec tro tro i tn? > .o3? my or scericia in said electrode and with rae! ecology and (c) detecting said electrochemical inactivation. 381. A method to detect or measure the ectraq? Imicoluau niscericia, which you understand (a) put in contact a link domain that contains a first surface ctan a sample that contains molecules linked to a marker electro roq? imicol? miniscente, said first surface is aligned with a second surface containing an electrode, > acha first surface and said surface area are spatially aligned to establish an n ontac t > : > electrochemical ib) apply a way of walking effective voltage to trigger the ec t roqu? m? cabbage? I stepped on the electrode and continued! eccrated and (cr) detect or measure said ect raqui icol umi niscency. 382. The method, > ra »; l»:? of conformity with the 180 »Ri > The first surface is a porous material. 183. A method for detecting or measuring the ectrochemistry, which includes (a) contacting the binding reagents in the cassette of the re-vindication of a sample that includes linked to a marker iee roqui í coi? mini s »-_ ent > r-; (b) show a form of 'wave > le v »r > lta e effective to trigger 1 -i the ec t roqu imi creates! umi ni scenc ía en icha first • u t-f? »R. ie »and said second supe fici and go) detect or tell me the -c I roqu i mi col umiru .CPGICÍ a. 184. A method for detecting or removing the elec- tronic and cen- tury that you want to connect the domains to the link on the cassette? of 13 rei indicac i n 157 with a sample that is e > : attip > rende ol '-' the links to a marker e > r roq? i i columi ni s > "erti, e> (b) apply an effective voltage waveform to trigger the ec troqu i nu col umi or scenc ia in ci? r_hos electrodes and with rae lee t roda; and ícr) de tac t - or by means of said technical election, 185. A method of detecting or measuring the cost of the research, which includes: (a) putting reagents into contact with link in the cassette of the re vindication 158 with a sample that includes molecules attached to a tracer element; (b) apply? -form »ie effective voltage wave to trigger the elec- triculture on the said electrode surface and surface > laugh "contract! ec trodo; and c) detecting or measuring said electrochemical columipi scenc la. 186). A method to detect or measure the e 1 e t roqu i i ero 1 nm i p i s »rren > laugh, that c omp r »- ^» n > ie: ía) contact the domains »r.! e link in the cassette of the claim in 159 with a sample comprising riiol c? those linked to an a rca» Jor e I ct roqu im icol »mi I did not even know how to apply an effective voltage waveform to trigger the electric shock? i nor scence in said surface of the electrode and surface of the ralectrode; and (c) detect ca me »ci ird? eh3 the ec t roeju i mi columi ni s rene ía 187. A method to" determine or I go 3 to elec t, roqu iciccilumi niscencia, q? e you understand (a) put in contact the binding domains in the cassette of claim 160 shows that it comprises molecules linked to a marker and 1 ec t roquim e 1 um in i ssess; (b) apply an effective voltage waveform f charm to trigger the electromagnetic electron microscope in said electrode and counter electrode, and (c) to detect or measure said electo rachi icoluitiscence 188. A method for detecting rt to measure the electroluminescence, which comprises: in contact the binding domains in the cassette of claim 361 with a sample comprising molecules linked to a positive electrotoxic marker; ib) applying an effective crate voltaic shape to trigger the electrochromic I niscenc la in said e 1 ecod and with ra 1 ec t rodo; and íc) detect ca meti i r said the ec t, r > rjq? i icolumi ni ert > - 1 a. 389. A method for detecting or editing the ectro- chy column is that you can (a) contact a plurality of discrete binding domains on a ccan? Na support that shows molecules linked to a marker the ecotroqu ummiumiscent by supplying a sample containing these molecules > :? n sayings > ri »ra > n? nicas de enlace, said sample modulate modular signals the ec roq? i icol? i no scente, where said modulation can be correlated with a concentration of analyte of interest in the sample; (b) applying a form of effective voltage arc to trigger the eccentric one or one on an electrode and reads it from a positive electrochemical marker to a molecule attached to the meno-j to one of said binding domains; (c) measure- said elec troquí imicolumi ni scenc ía; and id) determines) said concentration > An interesting guideline, 190. A method for detecting or measuring the elec- tricity and the circumstances, which you can understand (a) put the reagents in contact with in the cassette of claim 143 with a sample which comprises a first molecule and a second molecule linked to an identical electrochemical marker? im seente, in which the second molecule is a specific binding partner of the first mole. ^ ib) will be able to generate an effective voltage waveform to trigger the elec- trochemical transmission in said electrode and counter electrode.; and (c) detect * »ra measuring said electro-rruniscency. 191. Urt method for detecting or measuring the ec roq imi col umi ru scen cia, which understand (a) contacting the binding domains »in the cassette of claim 165 cut a sample comprising molecules linked to a marker ec roqu ím i colu i mserente; (b) applying an effective waveform to trigger the magnetic field in at least one of said pairs of electrodes and counter electrodes; and r (c) detect or measure d? ch-? the ec troquimicolum ni scenc la, 192. A method can not detect or get rid of the electrochem-nmini scence, which you understand) to put the link domains in contact "in the cassette of the Claim 168 shows that it comprises molecules linked to a marker or a microdermatitis; ib) apply an effective voltage waveform to trigger the ecchromic! umi ni scenc ía e »n said electrode and counter electrode; and Ic) to detect * or I am going to say said electrochemical information. 19"ü A method p - r detect or I go the the 3c t roqi.p micol? My ru scenc ia, which comprises: ía) contact the domains and link in that of claim 169 with a sample q ? e comprises molecules linked to a marker and I e »zt roqu imi col um ini scent; (b) apply a form of »wave > tle effective voltage pair deser? e > -Je »n r the electo roquimicol? My niscepc a in said the ect, rodo and with r ele rodo; and (r) detecting or going to said electro-icol? miru serene. 394. A method for detecting or measuring the e1 e »r t roqu ic u um iscen c ation, which-? cromp rende: ía) contact the link domains in the cassette > claim 171 with a sample comprising molecules linked to a marker e1 e »c t roqu i mie o3 miscente; ib) applying an effective voltage waveform in order to trigger the voltage in said electrode and counter electrode; and ic) detect ca medi said the ec t reactj? imieol? im scenc la, 195. A method for detecting or measuring the electrochemistry inception, which you understand (a) the contacting with rie 1 > . ?? > riom? n? > The link in the cassette of claim 173 contains a sample of molecules that are linked to a tag by the ectroq i mice. umi nir.cer? te; ib) apl? -.- > r- a waveform > ie see! What is the effective way to disengage the c raqu i mi col? i niscene i H in said electrode and counter electrode; and (c) detecting or measuring said elec quote col umiscence, 196. The method according to claim 175,: 74 188, or 389, wherein the electrode comprises c-fibrils. 197. A method to carry out a plurality of ectrcaq tests? i micolumiruscenc l, which gives the pa of: < a) contacting a plurality of discrete polymer matrices, each polymer matrix comprising one or several linking domains with a? -? sample containing one >;? vain to n 11 coughs of interest; ib) provoke in one or more > Were such domains of interest a reaction of "1 ee oq? I'm my friend! my nisrenci; (c) Detect the e 3 traqui icol? nuru scenc l. 1 »? 8. A method of copying with what is stated in rei indication 197, where the electroquimicoluminiscence is detected by photographic film. 199. A method for carrying out a plurality of tests of the ec roqu imicolumini scenc la, comprising the steps of: ia) contacting a plurality of domains > A link that includes acids or leric acids with a sample containing a variety of analysts of interest; i b) or r »> '-? > "Ai in u do not vary from > ri i ch a p 1 strip 1 i da d of »J» .am i ru os? na reaction d > - er troch i micol u ipi scenc? a; (e) detecting the Iroquois and my colinescence in a plurality of said domains > laugh link 200. A method in accordance with what is stated in claim 399 wherein said plurality of link domains contain the oligonucleotides linked to elec t rachemic mains. umi ni -soe ri es, 201. A method in accordance with that set forth in claim 399, wherein said plurality of link domains contain oly or opic acids bound to markers the luminic ecchimic and ti no or vain > Such analogous signals, when linked to said acids or proteins, cause the modulation of the signal or the electromechanical signal to the one or more binding domains. 202. A method pa ra. to carry out a plurality of tests and elect rcaqu iu such umi ni scenc ia, which comprises the detection of a plurality of apalitos present in a sample of multiple components in a concent, rae i ón inferior to apreas imadamente 1/3 OOO comprising l > step (s) of) contacting a plurality of discrete binding domains «ron? na shows that it contains one or more analytes of interest; ib) eliciting in one and several of said plurality of domains causes an electrochemie reaction olumini seepc i; and í) detect the the ec roq? imi o! umi ni scenc l in a fj 1 u a 1 i dae! of this-, "io irio de enlace ,, 20" - ",, A system to carry out a plurality of tests of the ectroqui ir.ol uminiscen rr? a, eg comprises: (a ) a plurality of specific binding domains for a plurality of different analytes; ib) a volume waveform generator; and (»:) un > 1 i spasi 1 vo e detection of photons. 2 < "J4 A system for carrying out a plurality of tests of elect roq? Imi columi niscepcia, which comprises: (a)? N the e? Ecod; (b)? N contra? Eld; (c) a ptl ural 1 of specific binding domains for a plurality of different analytes; id) a device for triggering the e x t roqu 1 m 1>: .o1um 1 nor scenc 13 and íe?) A device for detecting e1 ec t roqu 1 m 1 co1 um 1 ni scenc 1 a.