AU607393B2 - Shaped articles, which are provided with coatings, for the binding of substances having a bioaffinity, a process for their preparation, and their use - Google Patents
Shaped articles, which are provided with coatings, for the binding of substances having a bioaffinity, a process for their preparation, and their use Download PDFInfo
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- AU607393B2 AU607393B2 AU59837/86A AU5983786A AU607393B2 AU 607393 B2 AU607393 B2 AU 607393B2 AU 59837/86 A AU59837/86 A AU 59837/86A AU 5983786 A AU5983786 A AU 5983786A AU 607393 B2 AU607393 B2 AU 607393B2
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/68—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving nucleic acids
- C12Q1/6813—Hybridisation assays
- C12Q1/6834—Enzymatic or biochemical coupling of nucleic acids to a solid phase
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- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
- G01N33/543—Immunoassay; Biospecific binding assay; Materials therefor with an insoluble carrier for immobilising immunochemicals
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Abstract
Shaped articles with polymeric coatings, which bind to their surface biological substances with bioaffinity binding properties, are described. Shaped articles provided with coatings and, bound thereto, biological materials can be used, for example, as diagnostic agent in enzyme immunoassays or assays which make use of nucleic acid hybridisation.
Description
COMMONWEALTH OF AUSTRALIA '7 7 Form PATENTS ACT 1952-69 COMPLETE SPECIFICATION
(ORIGINAL)
Class Int. Class Application Number: Lodged: C9 ~'31 Complete Specification Lodged: 'his document contains the an1-ndnents made under I _ction 49 ind is correct Fqr ~prin ting.
0 0 0 0 0 0 0 0 o'P Reated Art: 00 0 0 0 Accepted: Published: 0'aone Gf Applicant: 0 of Address of Applicant 0 ,Artual Inlventor: 0 06 Address for Service BEHRINGWERKE AKTIENGESELLSCHAFT D-3550 Marburg 1, Federal Republic of Germnany RET NHARD FRANZE, HANS GEORG BESCHLE EDWD. WATERS SONS, 50 QUEEN STREET, MELBOURNE, AUSTRALIA, 3000.
Complete Specification for the invention entitled: SHAPED ARTICLES, WHICH ARE PROVIDED WITH COATINGS, FOR THE BINDING OF SIT3STANCES HAVING A BIOAFFINITY, A PROCESS FOR THEIR PREPARATION, AND THEIR USE The following statement is a full description of this iriwention, including the best method of performing it known to :-US i BEHRINGWERKE AKTIENGESELLSCHAFT 85/B 015 Ma 533 Dr. Ha/Sd.
Shaped articLes, which are provided with coatings, for the binding of substances having a bioaffinity, a process for their preparation, and their use The invention relates to shaped articles having polymeric coatings, the coating having the property of binding biological substances which have bioaffinity binding properties, and to a process for their preparation. These shaped articles which are provided with coatings can be used as "carriers" for the binding of Sone partner of a pair undergoing bioaffinity binding.
i Components for biological assay methods are frequently bound to a solid carrier in order, for exampLe, to i 10 remove excess reactants more easily. Carrier-bound rej actants are used, for exampLe, in radioimmunoassays and enzyme immunoassays. To improve the adhesion of biological material to plastic surfaces these surfaces are irradiated. Furthermore, the binding of assay comj 15 ponents to carriers has been improved by treatment with ibifunctional hemical reagents such as glutaraldehyde.
S2 It has also been proposed to reduce the range of variation of immunoLogical assay methods by use of plastic carriers for the coating with immunoLogically active SlmateriaL, which carriers contain less then 1 percent by weight of auxiliaries and additives (European Patent i A 0 126 392).
25 Use has been made, for methods which involve nucleic acid hybridization, of membranes for the binding of single-stranded nucleic acids. Membranes of this .ype are normally composed of nitroceLlulose. It is also known to promote the binding of nucleic acids to plastic surfaces by treatment of the surfaces with protamine.
Each of these methods solves only specific problems in i-- -WWOf w tw 2 particular biological determination methods which make use of carrier-bound components.
Thus, the task is still to find methods by which the adhesion of biological material to carrier surfaces can be improved.
It has now been found, surprisingly, that treatment of surfaces of shaped articles, for example of microassay plates, with a solution of cellulose nitrate improves the binding properties of these shaped articles for nucleic acids or proteins, or even for micro-organisms such as viruses. This treatment has made it possible for the very first time to bind nucleic acids to polystyrene, which is frequently used for the production of microassay plates.
Hence the invention relates to a shaped article having a polymeric coating, the combination being impermeable to aqueous solutions, which comprises the coating being composed of or containing a polymer which has the property of binding, from aqueous solutions, a biological substance which is a partner in bioaffinity binding.
The shaped articles can be composed of glass, ceramics or plastics. They can be, for example, small flat plates, plates with concave depressions to receive solutions, such as microassay plates, or tubes, beads or cuvettes.
A suitable coating is composed of a polymer which, on the one hand, has the property of adhering to the material of the shaped article and, on the other hand, binds biological materials from aqueous solutions in such a manner that they remain available as reactants in bioaffinity binding systems. The combination of a shaped article and a coating is impermeable to aqueous solutions.
r r 1
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3 The coating can be composed of one poLymer or of a mixture of several polymers. It can contain additives which promote, on the one hand, the adhesion of the coating to the shaped article and, on the other hand, the binding of the components having biozffinity.
Examples of suitable polymers are derivatized celluloses, such as cellulose nitrates, and of these especially collodion wools, as well as acetylcellulose, synthetic polymers such as polyamides, preferably copolyamides soluble in alcohols, polyacrylic acid, and of these the partially esterified or' amidated derivatives, as well as partially esterified or partially 0 o acetalizeo polyvinyl alcohols. The preferred polymers 1.5. are those which do not change, or change only slightly,, 0 0 S o 15 the optical properties of the shaped article, for oo example the transparency or the reflection.
S000 0o 0 0 0 00 0o a. The polymers are applied either in solution or in dispersion, or even as a powder, for example in spraying or dipping processes, to the shaped article, When tubes or 0" microassay plates are used as shaoed article the 0 00 0o°o polymer-containing solution or dispersion is preferably introduced into the tubes or the depressions and then .0 0 either poured out or Left therein and, in the latter case, the solvent or dispersing medium is removed by 00: evaporation. The type of drying depends on the evapor- So ating properties of the particular solvent or dispersing med um used.
Preferably, the coating is composed of or contains cellulose nitrate. Of course, it is aLso possibLe for the entire shaped article to be made of cellulose nitrate.
A caLlulose nitrate for this purpose can be applied in the form of a solution, for example by dipping or by spraying tl;e shaped article. However, it is also possible to apply the cellulose nitrate in the form of a -4 j h 1 4 dispersion.
An example of a suitable soLvent in the case of cel- SLulose nitrate is ethanol, but other soLvents can also be used. It is essential that the shaped article is not changed by the solvent in such a manner that its utilizability in the assay is adversely affected.
It is also possible to apply the coating in the form of a film or, for example, by powder coating.
If a solution of cellulose nitrate is used, for example in ethanol, the concentration is preferably between 1 pg/ml and 20 mg/ml, preferably 2 Pg/ml to 2 mg/mi cellulose nitrate.
The biological materials having bioaffinity binding properties can be proteins or glycoproteins which have the function of antigens, of antibodies, in this context both polyclonal and monoclonal, and of lectins. It is also possible for lipoproteins, glycolipids, oligosacj charides and polysaccharides having immunological or not having immunological binding properties to be bound to Sthe polymeric Layer. Single-stranded deoxyribonucleic acid (DNA) or single-stranded ribonucleic acid (RNA) as well as their oligonucleotides are likewise bound to the coating, owing to which the surfaces coated in this manner can be used for hybridization techniques.
The biological materials envisaged to be suitable for binding to the coating are aqueous solutions and buffer isolutions in which the former are dissolved or dispersed; dispersed when they take the form of glycolipids, lipoproteins, viruses, cells and constituents of cells of eukaryotic or prokaryotic structure. The solutions can contain additives which ensure the uniform binding of the biological materials.
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5 PreLiminary tests are carried out to determine the concentration of the particular bioLogicaL material which is to be bound to the coating, a-d the solution, or else its buffer components, its ionic strength and ics pH, and the conditions, such as the temperature and duration of the contacting of the liquid which contains the biological material which is to be bound and of the shaped article which is provided with the coating, in general in order to achieve uniform and high Loading with as near as possible irreversible binding of the particular biological material to the surface. The concentrations of the biological materials are, for example, between 5 mg/ml and 5 ng/ml or even less. The bufi oo fers which are used are, for example, phosphate, tris/ 00 00 SHCI and carbonate buffers in concentrations from 10 to S o0"o 15 100 mM and in the pH range 7 to 10, preferably 8.0 to oo o 9.6. The time can be varied between 30 minutes and o 20 h, and the temperature between 4 0 C and 80 0 C. One of 00 the possible procedures for these preliminary tests is described by Cantarero et al. (1980), Anal. Biochem.
S 0 20 105, 375-382, for the binding of proteins to polystyrene.
0 9 O The shaped articles provided with coatings can be used o o for the production of a means for analysis.
0 0 0 The invention is illustrated in detail by the Examples oo000 which follow, but without Limiting the subject-matter of the invention by his.
the invention by this.
Examples 1. Coating of microassay plates with cellulose nitrate as the polymer Polystyrene mi4roassay plates (A/S Nunc, 4000 Roskilde, Denmark, Cat. No. 262170, with 96 wells with round bases, hygienic quality standard) were used. Solutions of cellulose nitrate (NCA 400 and p: 00 0 0 0 0 0
DL)
6 NCA 500 supplied by WoLff WaLsrode AG, 30J0 WaLsrode, Federal Republic of Germany) in absolute ethanol were prepared in the foLLowing concentrations: 2 mg/ml and 50 pg/mL NCA 400, and 100 pg/mL NCA 500. ALL the weLLs of several microassay pLates were filled with, in each case, 100 pL of a solution of the said concentrations and, as controL, o,,Ly with the solvent ethanol. The solvent was then evaporated off by passing over a stream of air.
2. Use of microassay plates coated with a coating of ceLLulose nitrate for an enzyme immunoassay (ELISA) for the detection of antibodies against mumps.
2.1. Binding of mumps antigens to the coated and uncoated microassay plates Mumps virus cultured in vero cells, and vero cells which had not been infected with mumps virus, were processed by the method of Nicolai-SchoLten et at.
(1980), Med. Microbiol. Immunol. 168, 81-90, to give preparations which below are called mumps antigen and (negative) control antigen.
In all 192 wells of 2 microassay plates coated with 100 pg/mL cellulose nitrate NCA 500 in ethanoL 'J 2 microassay plates treated only with ethanol (see Example 1) in each case 2 x 48 50 pl aliquots of the solutions of mumps antigen and of control antigen were introduced, according to Popow-Kraupp et at. (1982), J. Med. Virol. 10, 119-129 and according to Sakata et al. (1984), J. Clir. Microbiol.
19, 21-25, in such a manner that the wells charged with the two solutions alternated consecutively.
Incubation was carried out at 40C for 15 to 20 h.
The solutions were then removed by suction, and the wells were washed.
Soo 20 00 0 0 0 t -7- 2.2. Detection of mumps antibodies The assay was carried out essentially as described by NicoLai-Scholten et al. A positive control serum was diluted 1:1000 with a solution of 1% bov- I 5 ine serum, 4% polyoxyethylene-(20)-sorbitan mono- Laurate (Tween 20) in 130 mM NaCI, 20 mM sodium phosphate, pH 7.2 (PBS). 100 pl of this were placed in aLL 96 wells of each microassay plate.
Incubation was carried out at 370C under air satur- S 10 ated with moisture for 1 h, followed by washing three times with 300 uL each time of a roLution of 1% Tween 20 in PBS. This was foLlowed by incubaition, i.e. at 37°C for 1 h, with 50pl per well of the solution, described by Nicolai-Scholten, of the conjugate of anti-human IgG with alkaline phosphatase Subsequently three washings with 300 pL of the solution of 1% Tween 20 in PBS each time was carried out. The enzymatic activity of the AP j conjugate bound in the wells was determined by incubation with 100 pL per well of a solution of g/L p-nitrophenyl phosphate in 10% diethanolamine in water, adjusted to pH 9.8 with HCL, at to 250C for 45 minutes. The reaction was stopped Sby addition of 50 PL per well of a solution of 2 N i 25 NaOH. The extinctions at 405 nm of the colored i solutions were measured using a Titertek appara- I tus, MuLtiskan MC, a photometer supplied by Flow Laboratories Inc., McLean, Va. 22102, USA.
I 30 2.3. Result The result is shown in Table 1. The extinctions of the wills in the plates treated with cellulose nitrate and Loaded with mumps antigen are about three times those of the plates treated only with the solvent ethanol. The wells treated with the (nlegative) control antigen show a Low extinction, both 8 when pLates treated with ceLLuLose nitrate were used and when plates treated only with the solvent were used, the extinction being between 0.01 anu 0.02 in the former case and between 0 and 0.01 in the second case. This extinction, which may be termed the background, has to be regarded as very Low for the plates treated with ceLLulose nitrate, a sign of low non-specific binding of the controL serum and of the AP-IgG conjugate. The three-fold higher extinction for th, coated plates shouLd be emphasized, which denotes an increase in the sensitivity by the same order of magnitude.
j 1/ ~d1
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IRa~ ~srr~era~suna~sRs~ aati, o o Table 1 Microassay plate coated with cellulose nitrate in pg per wrLL Mean extinction at 405 nm, and standard deviation, of wells treated with mumps antigen control antigen plate 1 plate 2 plate 1 plate 2 n 48 n 48 n 48 n 48 Difference in extinction from wells mumps antigen-control antigen plate 1 plate 2 0.410 0.350 0.020 0.010 0.390 0.340 0.041 0.030 0.040 0.031 0 0.150 0.120 0.010 0 0.140 0.120 0.017 0.015 0.017 0.015 4 _i~ *^-^ai^sswxi-wi.y 10 3. Use of microassay plates coated with coatings of celLulose nitrate for DNA hybridization 3.1. Binding of singLe-stranded DNA to the coated microassay plate The wells of the microassay plates used had been treated, as described in Example 1, with solutions of 2 mg/mL and 50 pg/ml cellulose nitrate NCA 400 in each case, and for control onLy with the solvent ethanol.
100 Pl of dilutions of 500, 250, 50, 5 and 0 ng/mL DNA of the plasmid pBW3, in a buffer of 10 mM tris/ HCL, 1 mM EDTA, pH 8.0, which had been decomposed into single strands by heating at 1000C for 10 min foLLowed by cooling at 0 0 C for 5 min, were introduced into the wells of the coated plates and into the weLLs of the plates treated only with ethanol as controls. The plates loaded with the solutions were maintained at 80 0 C for 8 h (baked), during which tney evaporated to dryness.
o C$ 0 15 o c 0 h
A
3.2. Prehybridization 1, u C S. The stock solutions used for the preparation of the buffers detailed below were 50-fold concentrated Denhardt's solution (Denhardt, 1966, Biochem.
Biophys. Res. Comm. 23, 641-652): 10 g of Ficoll 400 (a sucrose polymer suppLied by Pharmacia, MW 400,000), 10 g of polyvinylpyrroLidone, MW 360,000, g of bovine serum albumin dissolved in 1 liter of distilled water, and 20-fold concentrated citrate-buffered saline solution (SSC, abbreviation for standard sodium citrate), that is to say 3.0 M NaCI, 300 mM trisodium citrate.
For the prehybridization to occupy non-specific I- 11 -i binding sites, 100 PL portions of the following Isolution were introduced into aLL the weLLs and i incubated at 420C for 4 h: 0.01% yeast RNA, 0.1% j sodium dodecyL suLfate (SDS), 1% glycine, concentrated Denhardt's solution, 5-fold concentrated SSC, 50% formamide in 50 mM sodium phosphate buffer, pH 3.3. Hybridization The probe DNA used was DNA from the plasmid pBW3 which had been biotinylated by "nick" translation and prepared as described by Rigby et al. (1977), J. Mol. Biol. 113, 237-251, and diluted to a concentration of 250 ng/ml with a solution of 0.01% yeast RNA, 0.1% SnS, 10% dextran sulfate, Denhardt's solution of normal concentration, 5-fold concentrated SSC, 45% formamide in 20 mM sodium phosphate buffer, pH 7.0. The probe solution ready for use was obtained by heating it at 1000C for 10 min and I, :n cooling it to 0 0
C.
100 Pl of DNA probe solution were introduced into each well. Incubation took place at 42°C for 15 h for the hybridization.
3.4. Detection The probe solution was removed by suction. This was followed by several washing steps with tho following solutions in the sequence of amounts iridicated, and the incubation temperatures and incjub tion times indicated: 3 times with 300 pL of 0.1% SDS in 'centrated SSC at 20 to 25 0 C for 3 3 times with 300 pl of 0.1% oncentrated SSC at 20 to 25 0 C for twice with 300 pl of 0.1% SDS in Id SSC at
I
-nr r- i;l FCssrp~ F i 12 500C for 15 min each time, and 3 times with 150 pL of 0.1% SDS in 2-fold SSC at to 25 0 C for 1 min each time.
Subsequently, treatment with 300 uL per well of the solutions designated buffer A and buffer B below was carried out once with each in order to avoid non-specific binding of protein to the solid phase.
Buffer A: Buffer B: 0.05% 4-octylphenoxypolyethoxyethanol (Triton x 100), 0.1 M tris/HCL, 0.1 M NaCL, 2 mi MgCL2, pH 7.5, at 20 to 25 0
C
for 1 min; 3% bovine serum albumin in buffer A, at 420C for 20 min.
This was followed by an incubation, that is to say a heat-treatment, at 800C for 10 min without buffer.
Fo- the detection first 300 Pl of buffer B were introduced into the wells once more, and the liquid was left there at 20 to 250C for 20 min and then removed by suction, 100 ul per well of a solution of 2 ug/ml streptavidin (Bethesda Research Laboratories, Gaithersburg, Ma.
20877, USA) in buffer A were incubated at 20 to 25 0
C
for 1 h. Then washing was carried out three times with 300 pl of buffer A for 2 min each time. This was followed by incubation of 100 pl per well of DNA detection system in a concentration of 1 pg/mr in buffe A at 20 to 250C for 1 h. DNA detection system (Bethesda Res. Lab.) is a polymer containing biotinylated alkaline phosphatase prepared as described by Leary et al. (1983), Proc. Nat. Acad.
Sci. 80, 4045-4049. Subsequently washing was carried out with 300 ul of the following two buffer solutions, in each case three times at 20-25 0 C for
A
i- i .I 13 2 min, to remove unbound DNA detection system: Buffer A and 0.1 M tris/HCL, 0.1 M NaCI, 50 mM MgCI 2 pH Incubation was carried out with 100 iJ per weLL of a solution of 1.5 mg/ml p-nitrophenyl phosphate in 10% diethanoLamine in water, adjusted to pH 9.8 with HCL, as substrate for the alkaline phosphatase, at 37 0 C for 45 min, and then the enzymatic hydrolysis was stopped by addition of Pl per well of 2 N sodium hydroxide solution. The extinctions at 405 nm of the colored solutions in the wells were Likewise measured with a Titertek( Multiskan MC apparatus.
Result and assessment of the result Table 2 shows the result. Wells which had been coated as described in 3.1. with 2 mg/ml and with pg/mL cellulose nitrate NCA 400, and then had been treated with single-stranded DNA of the plasmid pBW3 having a concentration of 5 to 500 ng/ml by baking, generate, after the hybridization and binding of the DNA detection system to the probe, color signals which increase with increasing DNA concentration. The color signal of the background, that is to say that in the wells which had not been treated with DNA, is lower and, moreover, is approximately as weak as that in the wells which had not been coated with cellulose nitrate but had been treated with DNA of the said concentrations (controls).
The result shows that no DNA is detectable without coating with the co&ting.
iii f 1 k i
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Table 2 Microassay plate: coating of cellulose nitrate in pg/well Extinctions at 405 nm after DNA-hybridization and detection using AP detection system for DNA after previous treatment (baking) with single-stranded DNA of the plasmid pBW3 with the amounts ng per well 200 2.31 1.61 0.62 0.25 0.10 1.92 1.40 0.69 0.25 0.10 0 0.15 0.15 0.19 0.15 0.15 t
Claims (9)
1. Plates with concave depressions and tubes made of plastic, being coated with a polymer, the combination of the two being impermeable to aqueous solutions, said polymer being capable of binding a biological material from aqueous solutions, said biological material being a member of a specific binding pair, said polymer being derivatized cellulose, or a synthetic polymer comprising the group of polyamides or esterified or amidated polyacrylic acids characterized in that the coating solution is applied into the depressions or tubes and the remainder of the solution is removed, either by discharging or evaporating the solution.
2. A plate as claimed in claim 1, wherein the coating contains cellulose nitrate.
3. The use of a plate as claimed in claim 1 as a component of a diagnostic kit.
4. A process for the production of a means of analysis where said means of analysis is impermeable to aqueous solutions and said means of analysis is composed of a plastic plate and a polymer coating together with components of bioaffinity binding partners bound to the surface of the coating, the process comprising the plate first being provided with a coating of polymer of derivatized cellulose or a synthetic polymer comprising the group of polyamides or esterified or amidated polyacrylic acids in such a manner that a composite which is impermeable to aqueous solutions is produced, and wherein this composite is treated with an aqueous solution or aqueous dispersion of one or more components of bioaffinity binding partners so that this component or these components are bound to the surface of the coating. V i t Cb <ALLL C-) 1<~ c Liu I purpose can De applied in the form of a solution, for example by dipping or by spraying te shaped article.
However, it is also pos- sible to apply the cellulose nitrate in the form of a I i r- r L i I '-4 16 The process as claimed in claim 4, wherein the component of bioaffinity binding partners is or are a virus or a constituent of a virus as well as constituents of cells having eukaryotic or prokaryotic structure, a single-stranded DNA or RNA or their oligonucleotides, a protein or peptide, a glycoprotein, blycolipid, glycan or lipoprotein.
6. The process as claimed in claim 4, wherein the plate is a microassay plate. (0
7. The process as claimed in claim 4, wherein use is made, for the production of the coating, of a solution, a dispersion or a powder containing a synthetic polymer, natural polymer or a natural polymer which has been modified by a chemical reaction or derivatized.
8. The process as claimed in claim 4, wherein, for the production of the coating, a solution or a dispersion of 0 0* cellulose nitrate is applied, and the solvent or the dispersing medium is removed by drying. 0 4 O 4 044 8t 044
9. The process as claimed in claim 4, wherein the binding of components of bioaffinity binding partners from aqueous solutions or dispersions containing a virus or a constituent of a virus as well as constituents of cells having eukaryotic or prokaryotic structure, a single-stranded DNA, RNA or an oligonucleotide thereof, a protein or peptide or a glycoprotein, glycolipid, glycan or lipoprotein to the shaped articles provided with the coatings is carried out by incubation of the solutions or of the dispersions with the latter. DATED this 20th day of November, 1990 BEHRINGWERKE AKTIENGESELLSCHAFT WATERMARK Patent Trademark Attorneys 290 Burwood Road Hawthorn Victoria 3122 AUSTRALIA DBM/JMW:EK(14:4)
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
DE19853524451 DE3524451A1 (en) | 1985-07-09 | 1985-07-09 | Article for use in immunoassay coated with polymer |
DE3524451 | 1985-07-09 |
Publications (2)
Publication Number | Publication Date |
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AU5983786A AU5983786A (en) | 1987-01-15 |
AU607393B2 true AU607393B2 (en) | 1991-03-07 |
Family
ID=6275295
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
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AU59837/86A Ceased AU607393B2 (en) | 1985-07-09 | 1986-07-08 | Shaped articles, which are provided with coatings, for the binding of substances having a bioaffinity, a process for their preparation, and their use |
Country Status (13)
Country | Link |
---|---|
EP (1) | EP0211229B2 (en) |
JP (1) | JP2619861B2 (en) |
AT (1) | ATE70916T1 (en) |
AU (1) | AU607393B2 (en) |
CA (1) | CA1282322C (en) |
DE (2) | DE3524451A1 (en) |
DK (1) | DK324686A (en) |
ES (1) | ES2000648A6 (en) |
FI (1) | FI88339C (en) |
GR (1) | GR861755B (en) |
MX (1) | MX168106B (en) |
NO (1) | NO862751L (en) |
PT (1) | PT82940B (en) |
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AU649397B2 (en) * | 1988-10-11 | 1994-05-26 | Coulter Corporation | Immunoreactant carriers having a novel biocompatible intermediate coating and process of making same |
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JPS62173058U (en) * | 1986-04-21 | 1987-11-04 | ||
US5206136A (en) * | 1986-11-19 | 1993-04-27 | Genetic Systems Corporation | Rapid membrane affinity concentration assays |
CA1304682C (en) * | 1986-11-19 | 1992-07-07 | Nobuo Monji | Membrane affinity concentration immunoassay |
US5759774A (en) * | 1988-05-18 | 1998-06-02 | Cobe Laboratories, Inc. | Method of detecting circulating antibody types using dried or lyophilized cells |
US5747244A (en) * | 1991-12-23 | 1998-05-05 | Chiron Corporation | Nucleic acid probes immobilized on polystyrene surfaces |
DE4302012C1 (en) * | 1993-01-26 | 1994-07-21 | Serosearch Gmbh Entwicklung Un | Immunological test |
DE19744135C1 (en) * | 1997-09-29 | 1999-03-25 | Schering Ag | Medical implants coated with epothilone |
JP2001083162A (en) * | 1999-09-17 | 2001-03-30 | Fuji Photo Film Co Ltd | Filmy biopolymer absorbent and absorbing kit |
DE10311981A1 (en) * | 2003-03-12 | 2004-09-23 | Oligene Gmbh | Device for application, extraction and storage of biological material, includes immobilizing substrate for e.g. diagnosis, therapy or application |
EP1462804A1 (en) * | 2003-03-25 | 2004-09-29 | Stichting Sanquin Bloedvoorziening | Method for the detection of a pathogenic form of a prion protein |
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GB2007362A (en) * | 1977-11-04 | 1979-05-16 | Int Diagnostic Tech | Method of preparing a device for use in immunoassay |
GB2125963A (en) * | 1982-06-18 | 1984-03-14 | Mochida Pharm Co Ltd | Carriers for immunochemical measurement and measuring reagents utilizing said carriers |
EP0163799A1 (en) * | 1984-05-04 | 1985-12-11 | Dora Köhler | Antigen or antibody supported carrier |
Family Cites Families (4)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
FR2430013A1 (en) * | 1978-06-27 | 1980-01-25 | Sebia Sa | PHYSICO-BIOCHEMICAL SYSTEM FOR THE DETECTION OF SUBSTANCES, WITH ANTIGENIC ACTIVITY |
DE3346795A1 (en) * | 1983-12-23 | 1985-07-04 | E. Prof. Dr. 3550 Marburg Geyer | Enzyme immunoassay and corresponding diagnostic aid |
FR2569478B1 (en) * | 1984-08-23 | 1987-01-09 | Guerin Bernard | IMMUNOLOGICAL ANALYSIS STRIP AND METHOD FOR THE PRODUCTION THEREOF |
DD236400A1 (en) * | 1985-04-22 | 1986-06-04 | Univ Ernst Moritz Arndt | PROCESS FOR COATING FIXED PHASES FOR THE IMMUNOASSAY |
-
1985
- 1985-07-09 DE DE19853524451 patent/DE3524451A1/en not_active Withdrawn
-
1986
- 1986-07-01 AT AT86108907T patent/ATE70916T1/en not_active IP Right Cessation
- 1986-07-01 DE DE8686108907T patent/DE3683101D1/en not_active Expired - Fee Related
- 1986-07-01 EP EP86108907A patent/EP0211229B2/en not_active Expired - Lifetime
- 1986-07-07 GR GR861755A patent/GR861755B/en unknown
- 1986-07-07 ES ES8600167A patent/ES2000648A6/en not_active Expired
- 1986-07-07 FI FI862869A patent/FI88339C/en not_active IP Right Cessation
- 1986-07-08 CA CA000513273A patent/CA1282322C/en not_active Expired - Lifetime
- 1986-07-08 DK DK324686A patent/DK324686A/en not_active Application Discontinuation
- 1986-07-08 NO NO862751A patent/NO862751L/en unknown
- 1986-07-08 JP JP61158890A patent/JP2619861B2/en not_active Expired - Fee Related
- 1986-07-08 MX MX003054A patent/MX168106B/en unknown
- 1986-07-08 AU AU59837/86A patent/AU607393B2/en not_active Ceased
- 1986-07-08 PT PT82940A patent/PT82940B/en not_active IP Right Cessation
Patent Citations (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
GB2007362A (en) * | 1977-11-04 | 1979-05-16 | Int Diagnostic Tech | Method of preparing a device for use in immunoassay |
GB2125963A (en) * | 1982-06-18 | 1984-03-14 | Mochida Pharm Co Ltd | Carriers for immunochemical measurement and measuring reagents utilizing said carriers |
EP0163799A1 (en) * | 1984-05-04 | 1985-12-11 | Dora Köhler | Antigen or antibody supported carrier |
Cited By (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
AU649397B2 (en) * | 1988-10-11 | 1994-05-26 | Coulter Corporation | Immunoreactant carriers having a novel biocompatible intermediate coating and process of making same |
Also Published As
Publication number | Publication date |
---|---|
JP2619861B2 (en) | 1997-06-11 |
ES2000648A6 (en) | 1988-03-16 |
FI862869A (en) | 1987-01-10 |
GR861755B (en) | 1986-10-31 |
AU5983786A (en) | 1987-01-15 |
NO862751D0 (en) | 1986-07-08 |
DE3524451A1 (en) | 1987-03-12 |
FI88339B (en) | 1993-01-15 |
JPS6225264A (en) | 1987-02-03 |
EP0211229B2 (en) | 1994-12-14 |
FI88339C (en) | 1993-04-26 |
CA1282322C (en) | 1991-04-02 |
DK324686A (en) | 1987-01-10 |
EP0211229A3 (en) | 1987-12-16 |
EP0211229B1 (en) | 1991-12-27 |
PT82940A (en) | 1986-08-01 |
NO862751L (en) | 1987-01-12 |
DK324686D0 (en) | 1986-07-08 |
MX168106B (en) | 1993-05-04 |
ATE70916T1 (en) | 1992-01-15 |
FI862869A0 (en) | 1986-07-07 |
PT82940B (en) | 1989-01-30 |
EP0211229A2 (en) | 1987-02-25 |
DE3683101D1 (en) | 1992-02-06 |
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MK14 | Patent ceased section 143(a) (annual fees not paid) or expired |