CA2031246A1 - Two-dimensionally crystallized macromolecular films - Google Patents
Two-dimensionally crystallized macromolecular filmsInfo
- Publication number
- CA2031246A1 CA2031246A1 CA002031246A CA2031246A CA2031246A1 CA 2031246 A1 CA2031246 A1 CA 2031246A1 CA 002031246 A CA002031246 A CA 002031246A CA 2031246 A CA2031246 A CA 2031246A CA 2031246 A1 CA2031246 A1 CA 2031246A1
- Authority
- CA
- Canada
- Prior art keywords
- film
- films
- streptavidin
- macromolecular
- lipid
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Abandoned
Links
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical group N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 claims abstract description 34
- 229960002685 biotin Drugs 0.000 claims abstract description 17
- 235000020958 biotin Nutrition 0.000 claims abstract description 17
- 239000011616 biotin Substances 0.000 claims abstract description 17
- 150000002632 lipids Chemical class 0.000 claims abstract description 16
- 108010090804 Streptavidin Proteins 0.000 claims description 19
- 229920002521 macromolecule Polymers 0.000 claims description 8
- 235000018102 proteins Nutrition 0.000 description 14
- 108090000623 proteins and genes Proteins 0.000 description 14
- 102000004169 proteins and genes Human genes 0.000 description 14
- 239000003446 ligand Substances 0.000 description 8
- 230000027455 binding Effects 0.000 description 4
- 238000000034 method Methods 0.000 description 4
- 230000015572 biosynthetic process Effects 0.000 description 2
- 108091006004 biotinylated proteins Proteins 0.000 description 2
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 2
- 235000018417 cysteine Nutrition 0.000 description 2
- 238000000799 fluorescence microscopy Methods 0.000 description 2
- 238000007689 inspection Methods 0.000 description 2
- 238000011835 investigation Methods 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- LFMMUTRDOOGCOX-YLUOMYIDSA-N 5-[(3as,4s,6ar)-2-oxo-1,3,3a,4,6,6a-hexahydrothieno[3,4-d]imidazol-4-yl]-n,n-dioctadecylpentanamide Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)N(CCCCCCCCCCCCCCCCCC)CCCCCCCCCCCCCCCCCC)SC[C@@H]21 LFMMUTRDOOGCOX-YLUOMYIDSA-N 0.000 description 1
- KLTZIDAFCWAECV-PHGKCTHYSA-N 5-[(3as,4s,6ar)-2-oxo-1,3,3a,4,6,6a-hexahydrothieno[3,4-d]imidazol-4-yl]-n-[1-(dioctadecylamino)propyl]pentanamide Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)NC(CC)N(CCCCCCCCCCCCCCCCCC)CCCCCCCCCCCCCCCCCC)SC[C@@H]21 KLTZIDAFCWAECV-PHGKCTHYSA-N 0.000 description 1
- 108090001008 Avidin Proteins 0.000 description 1
- 229920002307 Dextran Polymers 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 101100536883 Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513) thi5 gene Proteins 0.000 description 1
- 108010039918 Polylysine Proteins 0.000 description 1
- 239000004372 Polyvinyl alcohol Substances 0.000 description 1
- 241000183024 Populus tremula Species 0.000 description 1
- 101100240664 Schizosaccharomyces pombe (strain 972 / ATCC 24843) nmt1 gene Proteins 0.000 description 1
- 240000004543 Vicia ervilia Species 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 239000000427 antigen Substances 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 239000013078 crystal Substances 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 230000000694 effects Effects 0.000 description 1
- 238000006911 enzymatic reaction Methods 0.000 description 1
- 125000001495 ethyl group Chemical group [H]C([H])([H])C([H])([H])* 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 238000012544 monitoring process Methods 0.000 description 1
- 229920000656 polylysine Polymers 0.000 description 1
- 229920000193 polymethacrylate Polymers 0.000 description 1
- 229920002451 polyvinyl alcohol Polymers 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 230000009870 specific binding Effects 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 230000007704 transition Effects 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
- 229920003169 water-soluble polymer Polymers 0.000 description 1
Classifications
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B82—NANOTECHNOLOGY
- B82Y—SPECIFIC USES OR APPLICATIONS OF NANOSTRUCTURES; MEASUREMENT OR ANALYSIS OF NANOSTRUCTURES; MANUFACTURE OR TREATMENT OF NANOSTRUCTURES
- B82Y30/00—Nanotechnology for materials or surface science, e.g. nanocomposites
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B82—NANOTECHNOLOGY
- B82Y—SPECIFIC USES OR APPLICATIONS OF NANOSTRUCTURES; MEASUREMENT OR ANALYSIS OF NANOSTRUCTURES; MANUFACTURE OR TREATMENT OF NANOSTRUCTURES
- B82Y5/00—Nanobiotechnology or nanomedicine, e.g. protein engineering or drug delivery
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N11/00—Carrier-bound or immobilised enzymes; Carrier-bound or immobilised microbial cells; Preparation thereof
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N11/00—Carrier-bound or immobilised enzymes; Carrier-bound or immobilised microbial cells; Preparation thereof
- C12N11/02—Enzymes or microbial cells immobilised on or in an organic carrier
- C12N11/06—Enzymes or microbial cells immobilised on or in an organic carrier attached to the carrier via a bridging agent
-
- 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
-
- 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
- G01N33/54353—Immunoassay; Biospecific binding assay; Materials therefor with an insoluble carrier for immobilising immunochemicals with ligand attached to the carrier via a chemical coupling agent
Abstract
Abstract of the Disclosure: Two-dimensionally crystall-ized macromolecular films are built up with the aid of a lipid monofilm carrying biotin units.
Description
2031~
O.Z. 0050/41278 Two-dimensionally crystallized macromolecular fllms The present invention relates to two-dimension-ally crystallized macromolecular films which have been produced with the assistance of a lipid monofilm carrying 5biotin units.
The formation of crystalline films of natural macromolecules, espe~ially of proteins, i8 of particular interest. Such films allow investigations of the struc-ture of these substances, the possibility of analysis of 10structural relations between ~he molecules and, in some cases, ~he development of novsl applications. However, it is precisely the interesting protein~ which do not naturally form crystals suitable for analysisO Hence there has been no lack of attempts to generate crystal-15lized protein ilms. Thus, Uzigiris ~ Kornberg (Nature 301 (1983) 125-129) have reported a method for forming two-dimensional protein films on lipid films. This method allows specific binding of proteins to natural or syn-thetic lipid ligands present in the planar lipid film.
20However, despite the preparation of a num~ar of crystal-lized protein films, the disadvantage was that a specific lipid ligand, and thus a protein-antigen con~ugate, must be available for each protein. In this connection the formation of specific protein films, those of strep-25tavidin, u~ing this technique was also proposed. For this purpose, the lipid intended for ~he lipid film was provided wi.th a biotin ligand so that, because of the particularly high affinity of biotin for streptavidin~
the streptavidin molecule~ are able to attach themselves 30to the biotin ligands in the lipid film and form a two-dimensionally crystallized streptavidin film in the water/air transition zone. Direct inspection of such films is pos-~ible using fluorescence microscopy, and the crystalline nature can be determined by electron micro-35scopy (Blankenburg et al., Biochemistry 28 (1989) 8214).
It is an object of the present in~ention to prepare crystallized macromolecular films which have not .: . ~ -' ' ' ' :
, :.................... - : , 203~2~
, - 2 - o.Z~ 0050/41278 been obtainable to date in a 3traightforward manner.
We have found that thi~ obiect i~ achieved by two-dimensionally cry3tallized macromolecular film~ which are compo~ed of a first lipid monofilm carrying biotin units and of a second film which i9 composed of strepta-vidin and attache~ itself to the biotin units and cry~tallizes, and of a film which is composed of a biotinylated macromolecula and is built up over the free active centers of the streptavidin film.
~hu~, these crystallized macromolecular films are composed of biotinylated macromolecules which are bound to the streptavidin film. In another embodiment of the films according to the invention the binding is achieved indirectly via a low molecular weight or pol~meric biotin ligand molecule. The crystalli~ation of the second macromolecular film is induced both by the receptor affinity binding and by the ordering of the streptavidin film which i~ already present.
In a particular embodiment of the films according to the invention the macromolecule~ are composed of proteins.
The first lipid monofilm carrying the biotin units characterizing the crystallized macromolecular films according to the invention is generally composed of the known amino functional lipids.
Examples o~ compounds which have proven particu-larly advantageous ~or the purposes of the present invention are N-biotinyl-S-~1,2-bis(octadecyloxycarbon-yl)ekhyl)cysteine, N-biotinyl-S-(l-carboxy-2-~N,N-diocta-decylaminocarbonyl)ethyl)cysteine, N-biotinoyl-S-1-phos-phatidyl-3-glycero-~n-dimyristoyl, N,N-dioctadecyl-N'-biotinylpropanediamine and N, N-dioctadecyl-biotinamide.
A streptavidin film i~ then attached to this biotinylated lipid film via the specific receptor~.
Streptavidin is a protein which ha~ four identical subunits, each of which i~ able to bind a biotin mole-cule. The non-covalent binding between streptavidin and ...... .
.. , ~ .
. , . .: , . ..
... : . :.
,. . ~ . -. . .
. , : - , , :
:::
:;: , -, , 2~3~2~3~
, - 3 - O.Z. 0050/41278 biotin is known to be one of the strongest; the X~ valus is about 1015 mol-l. Thi~ at~achment of the streptavidin to the biotin units of the lipid film result~ in an ordered, two-dimensional film a~ i9 depicted by way of example in Fiyure 1 with (A) = lipid, (B) = biotin and (C) = strep-tavidin. Very large two-dimensional streptavidin regions covering from 50 to 200 ~m are produced in this way. They can be detected by means of fluorescence microscopy.
The attachmen~ of a biotinylated, water-soluble macromolecule, in particular a biotinylated protein, to the free attachment sites of the biotin surfaca is now possible with the depicted surface of the two-dimension-ally crystallized strep~avidin film. The water-soluble macromolecules can be biotinylated poly(meth)acrylate, polylysine, polyvinyl alcohol or dextran. They ~erve to anchor another ligand molecule to the already crystall-ized surface. Proteins, such as biotinylated monoclonal antibodies or enzymes, are able to bind directly to the streptavidin film and be built up in a surprisingly straightforward manner to give crystalli~ed films.
Figures 2 and 3 show the films according to the inven-tion, where X generally represents a macromolecule and the ~quares 0 are intended to represent the protein.
The two-dimensionally crystallized macromolecular film~ built up in this way can be obtained by binding a water-soluble biotin ligand adapter molecule to the streptavidin film and thus maklng new recognition struc-tures available to another protein. It is also possible to bind a water-soluble polymer with biotin and ligand ~tructure~ to the streptavidin film, in exactly the same way as a biotinylated protein can be coupled to the ~treptavidin film. Details of the experimental procedure are to be found, inter alia, in Blankenburg et al., Biochemi~try 28 (1989) 8214.
Detection of the film~ obtained in thi3 way i~
carried out in a straightforwaxd manner by direct inspec-tion under the fluorescence microscope. The crystallinity ' '`':
.
~03~2~
O.Z. 0050/41278 Two-dimensionally crystallized macromolecular fllms The present invention relates to two-dimension-ally crystallized macromolecular films which have been produced with the assistance of a lipid monofilm carrying 5biotin units.
The formation of crystalline films of natural macromolecules, espe~ially of proteins, i8 of particular interest. Such films allow investigations of the struc-ture of these substances, the possibility of analysis of 10structural relations between ~he molecules and, in some cases, ~he development of novsl applications. However, it is precisely the interesting protein~ which do not naturally form crystals suitable for analysisO Hence there has been no lack of attempts to generate crystal-15lized protein ilms. Thus, Uzigiris ~ Kornberg (Nature 301 (1983) 125-129) have reported a method for forming two-dimensional protein films on lipid films. This method allows specific binding of proteins to natural or syn-thetic lipid ligands present in the planar lipid film.
20However, despite the preparation of a num~ar of crystal-lized protein films, the disadvantage was that a specific lipid ligand, and thus a protein-antigen con~ugate, must be available for each protein. In this connection the formation of specific protein films, those of strep-25tavidin, u~ing this technique was also proposed. For this purpose, the lipid intended for ~he lipid film was provided wi.th a biotin ligand so that, because of the particularly high affinity of biotin for streptavidin~
the streptavidin molecule~ are able to attach themselves 30to the biotin ligands in the lipid film and form a two-dimensionally crystallized streptavidin film in the water/air transition zone. Direct inspection of such films is pos-~ible using fluorescence microscopy, and the crystalline nature can be determined by electron micro-35scopy (Blankenburg et al., Biochemistry 28 (1989) 8214).
It is an object of the present in~ention to prepare crystallized macromolecular films which have not .: . ~ -' ' ' ' :
, :.................... - : , 203~2~
, - 2 - o.Z~ 0050/41278 been obtainable to date in a 3traightforward manner.
We have found that thi~ obiect i~ achieved by two-dimensionally cry3tallized macromolecular film~ which are compo~ed of a first lipid monofilm carrying biotin units and of a second film which i9 composed of strepta-vidin and attache~ itself to the biotin units and cry~tallizes, and of a film which is composed of a biotinylated macromolecula and is built up over the free active centers of the streptavidin film.
~hu~, these crystallized macromolecular films are composed of biotinylated macromolecules which are bound to the streptavidin film. In another embodiment of the films according to the invention the binding is achieved indirectly via a low molecular weight or pol~meric biotin ligand molecule. The crystalli~ation of the second macromolecular film is induced both by the receptor affinity binding and by the ordering of the streptavidin film which i~ already present.
In a particular embodiment of the films according to the invention the macromolecule~ are composed of proteins.
The first lipid monofilm carrying the biotin units characterizing the crystallized macromolecular films according to the invention is generally composed of the known amino functional lipids.
Examples o~ compounds which have proven particu-larly advantageous ~or the purposes of the present invention are N-biotinyl-S-~1,2-bis(octadecyloxycarbon-yl)ekhyl)cysteine, N-biotinyl-S-(l-carboxy-2-~N,N-diocta-decylaminocarbonyl)ethyl)cysteine, N-biotinoyl-S-1-phos-phatidyl-3-glycero-~n-dimyristoyl, N,N-dioctadecyl-N'-biotinylpropanediamine and N, N-dioctadecyl-biotinamide.
A streptavidin film i~ then attached to this biotinylated lipid film via the specific receptor~.
Streptavidin is a protein which ha~ four identical subunits, each of which i~ able to bind a biotin mole-cule. The non-covalent binding between streptavidin and ...... .
.. , ~ .
. , . .: , . ..
... : . :.
,. . ~ . -. . .
. , : - , , :
:::
:;: , -, , 2~3~2~3~
, - 3 - O.Z. 0050/41278 biotin is known to be one of the strongest; the X~ valus is about 1015 mol-l. Thi~ at~achment of the streptavidin to the biotin units of the lipid film result~ in an ordered, two-dimensional film a~ i9 depicted by way of example in Fiyure 1 with (A) = lipid, (B) = biotin and (C) = strep-tavidin. Very large two-dimensional streptavidin regions covering from 50 to 200 ~m are produced in this way. They can be detected by means of fluorescence microscopy.
The attachmen~ of a biotinylated, water-soluble macromolecule, in particular a biotinylated protein, to the free attachment sites of the biotin surfaca is now possible with the depicted surface of the two-dimension-ally crystallized strep~avidin film. The water-soluble macromolecules can be biotinylated poly(meth)acrylate, polylysine, polyvinyl alcohol or dextran. They ~erve to anchor another ligand molecule to the already crystall-ized surface. Proteins, such as biotinylated monoclonal antibodies or enzymes, are able to bind directly to the streptavidin film and be built up in a surprisingly straightforward manner to give crystalli~ed films.
Figures 2 and 3 show the films according to the inven-tion, where X generally represents a macromolecule and the ~quares 0 are intended to represent the protein.
The two-dimensionally crystallized macromolecular film~ built up in this way can be obtained by binding a water-soluble biotin ligand adapter molecule to the streptavidin film and thus maklng new recognition struc-tures available to another protein. It is also possible to bind a water-soluble polymer with biotin and ligand ~tructure~ to the streptavidin film, in exactly the same way as a biotinylated protein can be coupled to the ~treptavidin film. Details of the experimental procedure are to be found, inter alia, in Blankenburg et al., Biochemi~try 28 (1989) 8214.
Detection of the film~ obtained in thi3 way i~
carried out in a straightforwaxd manner by direct inspec-tion under the fluorescence microscope. The crystallinity ' '`':
.
~03~2~
- 4 - O.Z. 0050/41278 of the re~ulting films can be checked by electron micro~-copy after tran~fer by the Langmuir-Schafer technique.
The crystallized macromolecular film~ according to the invention permit rapid and straightforward pre-paration of samples for investigation of the structure ofthesa macromolecules which are not otherwise obtainable in cry~tallized form. These films are also suitable for monitoring enzymatic reactions when the protein type is coupled with retention of its en7.ymatic activity to the streptavidin film.
'~ -~ . :
:., . . : , ; ~
.~ , .
:
: .
.:- :
The crystallized macromolecular film~ according to the invention permit rapid and straightforward pre-paration of samples for investigation of the structure ofthesa macromolecules which are not otherwise obtainable in cry~tallized form. These films are also suitable for monitoring enzymatic reactions when the protein type is coupled with retention of its en7.ymatic activity to the streptavidin film.
'~ -~ . :
:., . . : , ; ~
.~ , .
:
: .
.:- :
Claims
We claim:
A two-dimensionally crystallized macromolecular film which is composed of a first lipid monofilm carrying biotin units and of a second film which is composed of streptavidin and attaches itself to the biotin units and crystallizes, and of a film which is composed of a biotinylated macromolecule and is built up over the free active centers of the streptavidin film.
A two-dimensionally crystallized macromolecular film which is composed of a first lipid monofilm carrying biotin units and of a second film which is composed of streptavidin and attaches itself to the biotin units and crystallizes, and of a film which is composed of a biotinylated macromolecule and is built up over the free active centers of the streptavidin film.
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DE19893939973 DE3939973A1 (en) | 1989-12-02 | 1989-12-02 | TWO-DIMENSIONAL CRYSTALLIZED MACROMOLECULAR LAYERS |
| DEP3939973.7 | 1989-12-02 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA2031246A1 true CA2031246A1 (en) | 1991-06-03 |
Family
ID=6394725
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA002031246A Abandoned CA2031246A1 (en) | 1989-12-02 | 1990-11-30 | Two-dimensionally crystallized macromolecular films |
Country Status (4)
| Country | Link |
|---|---|
| EP (1) | EP0431400A1 (en) |
| JP (1) | JPH03246300A (en) |
| CA (1) | CA2031246A1 (en) |
| DE (1) | DE3939973A1 (en) |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6872522B1 (en) | 1996-06-25 | 2005-03-29 | Michael Mecklenburg | Broad specificity affinity arrays: a qualitative approach to complex sample discrimination |
Families Citing this family (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE19724787A1 (en) * | 1997-06-06 | 1998-12-10 | Biotez Berlin Buch Gmbh Bioche | Streptavidin / avidin coated surfaces |
| EP2189791A3 (en) | 1998-02-04 | 2011-03-09 | Life Technologies Corporation | Microarrays and uses therefor |
| DE19808226C1 (en) * | 1998-02-27 | 2000-03-02 | Bruker Analytik Gmbh | Investigating hydrophilic macromolecules in an aqueous solution by attaching them to a lipid film on a solid carrier |
| US6576478B1 (en) | 1998-07-14 | 2003-06-10 | Zyomyx, Inc. | Microdevices for high-throughput screening of biomolecules |
| US6682942B1 (en) | 1998-07-14 | 2004-01-27 | Zyomyx, Inc. | Microdevices for screening biomolecules |
| US6897073B2 (en) | 1998-07-14 | 2005-05-24 | Zyomyx, Inc. | Non-specific binding resistant protein arrays and methods for making the same |
| US6406921B1 (en) | 1998-07-14 | 2002-06-18 | Zyomyx, Incorporated | Protein arrays for high-throughput screening |
| WO2002043856A2 (en) * | 2000-10-24 | 2002-06-06 | Fatemeh Mojtabai | Ordered two-and three-dimensional structures of amphiphilic molecules |
Family Cites Families (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4282287A (en) * | 1980-01-24 | 1981-08-04 | Giese Roger W | Biochemical avidin-biotin multiple-layer system |
| US4489133A (en) * | 1982-11-16 | 1984-12-18 | The Board Of Trustees Of The Leland Stanford Jr. University | Two-dimensional crystallization technique |
-
1989
- 1989-12-02 DE DE19893939973 patent/DE3939973A1/en not_active Withdrawn
-
1990
- 1990-11-22 EP EP90122257A patent/EP0431400A1/en not_active Withdrawn
- 1990-11-28 JP JP32339390A patent/JPH03246300A/en active Pending
- 1990-11-30 CA CA002031246A patent/CA2031246A1/en not_active Abandoned
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6872522B1 (en) | 1996-06-25 | 2005-03-29 | Michael Mecklenburg | Broad specificity affinity arrays: a qualitative approach to complex sample discrimination |
| US7662560B2 (en) | 1996-06-25 | 2010-02-16 | Michael Mecklenburg | Broad specificity affinity arrays: a qualitative approach to complex sample discrimination |
Also Published As
| Publication number | Publication date |
|---|---|
| JPH03246300A (en) | 1991-11-01 |
| DE3939973A1 (en) | 1991-06-06 |
| EP0431400A1 (en) | 1991-06-12 |
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