CA1209907A - Method of affinity purification employing monoclonal antibodies - Google Patents
Method of affinity purification employing monoclonal antibodiesInfo
- Publication number
- CA1209907A CA1209907A CA000425555A CA425555A CA1209907A CA 1209907 A CA1209907 A CA 1209907A CA 000425555 A CA000425555 A CA 000425555A CA 425555 A CA425555 A CA 425555A CA 1209907 A CA1209907 A CA 1209907A
- Authority
- CA
- Canada
- Prior art keywords
- environment
- antigen
- antibody
- monoclonal antibody
- process according
- 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.)
- Expired
Links
- 238000000034 method Methods 0.000 title claims abstract description 38
- 238000001261 affinity purification Methods 0.000 title abstract description 6
- 239000000427 antigen Substances 0.000 claims abstract description 126
- 102000036639 antigens Human genes 0.000 claims abstract description 126
- 108091007433 antigens Proteins 0.000 claims abstract description 126
- 230000027455 binding Effects 0.000 claims abstract description 25
- 238000009739 binding Methods 0.000 claims abstract description 25
- 230000000984 immunochemical effect Effects 0.000 claims abstract description 14
- 239000007788 liquid Substances 0.000 claims description 21
- 239000007787 solid Substances 0.000 claims description 20
- 230000003196 chaotropic effect Effects 0.000 claims description 11
- 239000003795 chemical substances by application Substances 0.000 claims description 11
- 210000002966 serum Anatomy 0.000 claims description 11
- 238000000746 purification Methods 0.000 claims description 9
- ZRALSGWEFCBTJO-UHFFFAOYSA-N Guanidine Chemical compound NC(N)=N ZRALSGWEFCBTJO-UHFFFAOYSA-N 0.000 claims description 8
- 229920002684 Sepharose Polymers 0.000 claims description 8
- 239000012535 impurity Substances 0.000 claims description 7
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 claims description 6
- 239000004202 carbamide Substances 0.000 claims description 6
- CHJJGSNFBQVOTG-UHFFFAOYSA-N N-methyl-guanidine Natural products CNC(N)=N CHJJGSNFBQVOTG-UHFFFAOYSA-N 0.000 claims description 4
- 239000004793 Polystyrene Substances 0.000 claims description 4
- SWSQBOPZIKWTGO-UHFFFAOYSA-N dimethylaminoamidine Natural products CN(C)C(N)=N SWSQBOPZIKWTGO-UHFFFAOYSA-N 0.000 claims description 4
- 229920002223 polystyrene Polymers 0.000 claims description 4
- ZNNZYHKDIALBAK-UHFFFAOYSA-M potassium thiocyanate Chemical compound [K+].[S-]C#N ZNNZYHKDIALBAK-UHFFFAOYSA-M 0.000 claims description 4
- 239000000020 Nitrocellulose Substances 0.000 claims description 3
- 239000004677 Nylon Substances 0.000 claims description 3
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 claims description 3
- 229920002678 cellulose Polymers 0.000 claims description 3
- 239000001913 cellulose Substances 0.000 claims description 3
- 239000011521 glass Substances 0.000 claims description 3
- 229920001220 nitrocellulos Polymers 0.000 claims description 3
- 229920001778 nylon Polymers 0.000 claims description 3
- 229920002401 polyacrylamide Polymers 0.000 claims description 3
- 239000000741 silica gel Substances 0.000 claims description 3
- 229910002027 silica gel Inorganic materials 0.000 claims description 3
- 230000004071 biological effect Effects 0.000 claims description 2
- 230000009977 dual effect Effects 0.000 claims description 2
- 230000003100 immobilizing effect Effects 0.000 claims 3
- IOLCXVTUBQKXJR-UHFFFAOYSA-M potassium bromide Chemical compound [K+].[Br-] IOLCXVTUBQKXJR-UHFFFAOYSA-M 0.000 claims 3
- 229920003229 poly(methyl methacrylate) Polymers 0.000 claims 2
- 239000004926 polymethyl methacrylate Substances 0.000 claims 2
- 238000003375 selectivity assay Methods 0.000 claims 2
- 230000002411 adverse Effects 0.000 abstract description 2
- 239000003599 detergent Substances 0.000 description 13
- 210000004408 hybridoma Anatomy 0.000 description 12
- 102100035703 Prostatic acid phosphatase Human genes 0.000 description 11
- 108010043671 prostatic acid phosphatase Proteins 0.000 description 11
- 239000000872 buffer Substances 0.000 description 9
- 230000035945 sensitivity Effects 0.000 description 8
- 230000007613 environmental effect Effects 0.000 description 7
- 230000004927 fusion Effects 0.000 description 6
- 238000011534 incubation Methods 0.000 description 6
- 239000002609 medium Substances 0.000 description 6
- 239000000243 solution Substances 0.000 description 6
- 206010035226 Plasma cell myeloma Diseases 0.000 description 5
- 238000010828 elution Methods 0.000 description 5
- 201000000050 myeloid neoplasm Diseases 0.000 description 5
- 230000002829 reductive effect Effects 0.000 description 5
- 239000006228 supernatant Substances 0.000 description 5
- 238000005406 washing Methods 0.000 description 5
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 4
- 241000699666 Mus <mouse, genus> Species 0.000 description 4
- 238000001042 affinity chromatography Methods 0.000 description 4
- 239000011324 bead Substances 0.000 description 4
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- 238000003795 desorption Methods 0.000 description 4
- 239000000047 product Substances 0.000 description 4
- 239000007790 solid phase Substances 0.000 description 4
- 210000004989 spleen cell Anatomy 0.000 description 4
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 3
- 230000000694 effects Effects 0.000 description 3
- 206010003445 Ascites Diseases 0.000 description 2
- 241000606161 Chlamydia Species 0.000 description 2
- 108090000790 Enzymes Proteins 0.000 description 2
- 102000004190 Enzymes Human genes 0.000 description 2
- 241001465754 Metazoa Species 0.000 description 2
- 241000699670 Mus sp. Species 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- PPBRXRYQALVLMV-UHFFFAOYSA-N Styrene Chemical compound C=CC1=CC=CC=C1 PPBRXRYQALVLMV-UHFFFAOYSA-N 0.000 description 2
- 239000012062 aqueous buffer Substances 0.000 description 2
- 238000003556 assay Methods 0.000 description 2
- 210000003719 b-lymphocyte Anatomy 0.000 description 2
- 238000004587 chromatography analysis Methods 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 238000005194 fractionation Methods 0.000 description 2
- NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 239000000203 mixture Substances 0.000 description 2
- 230000000717 retained effect Effects 0.000 description 2
- 230000002441 reversible effect Effects 0.000 description 2
- 238000012216 screening Methods 0.000 description 2
- 210000000582 semen Anatomy 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- GEYOCULIXLDCMW-UHFFFAOYSA-N 1,2-phenylenediamine Chemical compound NC1=CC=CC=C1N GEYOCULIXLDCMW-UHFFFAOYSA-N 0.000 description 1
- CIWBSHSKHKDKBQ-JLAZNSOCSA-N Ascorbic acid Chemical compound OC[C@H](O)[C@H]1OC(=O)C(O)=C1O CIWBSHSKHKDKBQ-JLAZNSOCSA-N 0.000 description 1
- BSYNRYMUTXBXSQ-UHFFFAOYSA-N Aspirin Chemical compound CC(=O)OC1=CC=CC=C1C(O)=O BSYNRYMUTXBXSQ-UHFFFAOYSA-N 0.000 description 1
- BTBUEUYNUDRHOZ-UHFFFAOYSA-N Borate Chemical compound [O-]B([O-])[O-] BTBUEUYNUDRHOZ-UHFFFAOYSA-N 0.000 description 1
- 241000498849 Chlamydiales Species 0.000 description 1
- KRKNYBCHXYNGOX-UHFFFAOYSA-K Citrate Chemical compound [O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O KRKNYBCHXYNGOX-UHFFFAOYSA-K 0.000 description 1
- 108010014172 Factor V Proteins 0.000 description 1
- 108010054218 Factor VIII Proteins 0.000 description 1
- 102000001690 Factor VIII Human genes 0.000 description 1
- 102000018997 Growth Hormone Human genes 0.000 description 1
- 108010051696 Growth Hormone Proteins 0.000 description 1
- 102000002265 Human Growth Hormone Human genes 0.000 description 1
- 108010000521 Human Growth Hormone Proteins 0.000 description 1
- 239000000854 Human Growth Hormone Substances 0.000 description 1
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
- 102000004877 Insulin Human genes 0.000 description 1
- 108090001061 Insulin Proteins 0.000 description 1
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 1
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- CERQOIWHTDAKMF-UHFFFAOYSA-M Methacrylate Chemical compound CC(=C)C([O-])=O CERQOIWHTDAKMF-UHFFFAOYSA-M 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- 239000002202 Polyethylene glycol Substances 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 1
- 240000006365 Vitis vinifera Species 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 239000008351 acetate buffer Substances 0.000 description 1
- 150000001413 amino acids Chemical class 0.000 description 1
- 230000000890 antigenic effect Effects 0.000 description 1
- 125000000637 arginyl group Chemical group N[C@@H](CCCNC(N)=N)C(=O)* 0.000 description 1
- 238000004380 ashing Methods 0.000 description 1
- 238000003149 assay kit Methods 0.000 description 1
- 244000309466 calf Species 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 239000011248 coating agent Substances 0.000 description 1
- 238000000576 coating method Methods 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 229940009976 deoxycholate Drugs 0.000 description 1
- KXGVEGMKQFWNSR-LLQZFEROSA-N deoxycholic acid Chemical compound C([C@H]1CC2)[C@H](O)CC[C@]1(C)[C@@H]1[C@@H]2[C@@H]2CC[C@H]([C@@H](CCC(O)=O)C)[C@@]2(C)[C@@H](O)C1 KXGVEGMKQFWNSR-LLQZFEROSA-N 0.000 description 1
- 230000005595 deprotonation Effects 0.000 description 1
- 238000010537 deprotonation reaction Methods 0.000 description 1
- 230000001627 detrimental effect Effects 0.000 description 1
- 230000003292 diminished effect Effects 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 229960000301 factor viii Drugs 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- 239000000122 growth hormone Substances 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 125000000487 histidyl group Chemical group [H]N([H])C(C(=O)O*)C([H])([H])C1=C([H])N([H])C([H])=N1 0.000 description 1
- 239000005556 hormone Substances 0.000 description 1
- 229940088597 hormone Drugs 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 230000028993 immune response Effects 0.000 description 1
- 230000002163 immunogen Effects 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 229940125396 insulin Drugs 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- 230000002427 irreversible effect Effects 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- HOVAGTYPODGVJG-VEIUFWFVSA-N methyl alpha-D-mannoside Chemical compound CO[C@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]1O HOVAGTYPODGVJG-VEIUFWFVSA-N 0.000 description 1
- 230000001483 mobilizing effect Effects 0.000 description 1
- UYDLBVPAAFVANX-UHFFFAOYSA-N octylphenoxy polyethoxyethanol Chemical compound CC(C)(C)CC(C)(C)C1=CC=C(OCCOCCOCCOCCO)C=C1 UYDLBVPAAFVANX-UHFFFAOYSA-N 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 229920001223 polyethylene glycol Polymers 0.000 description 1
- 239000011148 porous material Substances 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 230000001737 promoting effect Effects 0.000 description 1
- 102000004169 proteins and genes Human genes 0.000 description 1
- 108090000623 proteins and genes Proteins 0.000 description 1
- 230000005855 radiation Effects 0.000 description 1
- 238000003127 radioimmunoassay Methods 0.000 description 1
- 230000004044 response Effects 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 229960001866 silicon dioxide Drugs 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 235000017281 sodium acetate Nutrition 0.000 description 1
- 239000001632 sodium acetate Substances 0.000 description 1
- 239000007974 sodium acetate buffer Substances 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- SUKJFIGYRHOWBL-UHFFFAOYSA-N sodium hypochlorite Chemical compound [Na+].Cl[O-] SUKJFIGYRHOWBL-UHFFFAOYSA-N 0.000 description 1
- 230000003381 solubilizing effect Effects 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 230000009870 specific binding Effects 0.000 description 1
- 239000003104 tissue culture media Substances 0.000 description 1
Classifications
-
- 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
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/16—Hydrolases (3) acting on ester bonds (3.1)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/46—Hybrid immunoglobulins
- C07K16/468—Immunoglobulins having two or more different antigen binding sites, e.g. multifunctional antibodies
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Immunology (AREA)
- Genetics & Genomics (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biophysics (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- Biomedical Technology (AREA)
- Biotechnology (AREA)
- Microbiology (AREA)
- General Engineering & Computer Science (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US36778182A | 1982-04-12 | 1982-04-12 | |
| US367,781 | 1982-04-12 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA1209907A true CA1209907A (en) | 1986-08-19 |
Family
ID=23448565
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA000425555A Expired CA1209907A (en) | 1982-04-12 | 1983-04-11 | Method of affinity purification employing monoclonal antibodies |
Country Status (11)
| Country | Link |
|---|---|
| EP (1) | EP0105359A4 (it) |
| AT (1) | AT393386B (it) |
| AU (1) | AU622099B2 (it) |
| CA (1) | CA1209907A (it) |
| CH (1) | CH672028A5 (it) |
| DK (1) | DK192191D0 (it) |
| ES (3) | ES8404858A1 (it) |
| FI (1) | FI88403C (it) |
| GB (1) | GB2128630B (it) |
| IT (1) | IT1219779B (it) |
| WO (1) | WO1983003678A1 (it) |
Families Citing this family (30)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB8328918D0 (en) * | 1983-10-28 | 1983-11-30 | Unilever Plc | Alkaline phosphatase |
| GB8331071D0 (en) * | 1983-11-22 | 1983-12-29 | Karayiannis P | Assay for dna/rna |
| US4666865A (en) * | 1984-01-13 | 1987-05-19 | Centocor, Inc. | Immunoassay for biologically active human interferon-gamma employing unique monoclonal antibodies |
| US4789631A (en) * | 1984-02-17 | 1988-12-06 | Synbiotics Corporation | Immunoassay for anti-dirofilaria immitis antibody |
| GB8426468D0 (en) * | 1984-10-19 | 1984-11-28 | Technology Licence Co Ltd | Monoclonal antibodies |
| AU5259786A (en) * | 1985-01-30 | 1986-08-07 | United States Of America, The | Monoclonal antibodies against chlamydial genes specific lipopolysaccharide |
| US4818687A (en) * | 1985-02-28 | 1989-04-04 | Massachusetts Institute Of Technology | Affinity column and process for detection of low molecular weight toxic substances |
| US4859611A (en) * | 1985-02-28 | 1989-08-22 | Massachusetts Institute Of Technology | Affinity column and process for detection of low molecular weight toxic substances |
| IL75828A (en) * | 1985-07-17 | 1991-06-10 | Univ Ramot | Immobilization by biologically active proteins |
| NZ218336A (en) * | 1985-12-09 | 1991-08-27 | Kirin Amgen Inc | Monoclonal antibodies to human pluripotent granulocyte colony stimulating factor (hpg-csf) |
| US5175255A (en) * | 1987-03-23 | 1992-12-29 | Amgen Inc. | Methods for purification of platelet-derived growth factor |
| US5190859A (en) * | 1987-02-26 | 1993-03-02 | Dana-Farber Cancer Institute, Inc. | Purification of LFA-3 |
| SE468653B (sv) * | 1987-03-06 | 1993-02-22 | Perstorp Biolytica | Adsorbent foer isokratisk affinitetskromatografi |
| JPS6463599A (en) * | 1987-05-01 | 1989-03-09 | Xoma Corp | Purification of immunoglobulin by selective anti-idiotype bond |
| WO1989000695A1 (en) * | 1987-07-14 | 1989-01-26 | The Victoria University Of Manchester | Method for the diagnosis of infections with detection of lipopolysaccharide antigens |
| CA1323567C (en) * | 1987-10-05 | 1993-10-26 | Gene R. Nathans | Method for purification of antibodies |
| US5582862A (en) * | 1988-04-04 | 1996-12-10 | General Hospital Corporation | Antibodies that bind to α2-antiplasmin crosslinked to fibrin which do not inhibit plasma α2-antiplasmin |
| US5372812A (en) * | 1988-04-04 | 1994-12-13 | The General Hospital Corporation | Composition and method for acceleration of clot lysis |
| EP0937146A2 (en) * | 1996-09-20 | 1999-08-25 | The General Hospital Corporation | Composition and method for enhancing fibrinolysis using antibodies to alpha-2-antiplasmin |
| EP3521311A1 (en) * | 2008-04-11 | 2019-08-07 | Chugai Seiyaku Kabushiki Kaisha | Antigen-binding molecule capable of binding to two or more antigen molecules repeatedly |
| RU2642318C2 (ru) | 2010-11-30 | 2018-01-24 | Чугаи Сейяку Кабусики Кайся | Антигенсвязывающая молекула, способная многократно связываться с множеством антигенных молекул |
| CN112812184A (zh) | 2011-02-25 | 2021-05-18 | 中外制药株式会社 | FcγRIIb特异性Fc抗体 |
| WO2013047748A1 (ja) | 2011-09-30 | 2013-04-04 | 中外製薬株式会社 | 複数の生理活性を有する抗原の消失を促進する抗原結合分子 |
| EP3517550A1 (en) | 2011-11-30 | 2019-07-31 | Chugai Seiyaku Kabushiki Kaisha | Drug containing carrier into cell for forming immune complex |
| SG11201700841QA (en) | 2014-12-19 | 2017-03-30 | Chugai Pharmaceutical Co Ltd | Anti-myostatin antibodies, polypeptides containing variant fc regions, and methods of use |
| LT3233921T (lt) | 2014-12-19 | 2021-12-10 | Chugai Seiyaku Kabushiki Kaisha | Anti-c5 antikūnai ir panaudojimo būdai |
| US11359009B2 (en) | 2015-12-25 | 2022-06-14 | Chugai Seiyaku Kabushiki Kaisha | Anti-myostatin antibodies and methods of use |
| TWI693940B (zh) | 2016-08-05 | 2020-05-21 | 日商中外製藥股份有限公司 | Ｉｌ-８相關疾病之治療用或預防用組成物 |
| US11608374B2 (en) | 2017-01-30 | 2023-03-21 | Chugai Seiyaku Kabushiki Kaisha | Anti-sclerostin antibodies and methods of use |
| CN110724204B (zh) * | 2019-11-18 | 2021-10-22 | 广东菲鹏制药股份有限公司 | Fc融合蛋白的纯化方法 |
Family Cites Families (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4172124A (en) * | 1978-04-28 | 1979-10-23 | The Wistar Institute | Method of producing tumor antibodies |
| EP0059598B1 (en) * | 1981-02-26 | 1985-07-17 | Unilever Plc | A process and apparatus for the recovery of immunoglobulines |
| US4474893A (en) * | 1981-07-01 | 1984-10-02 | The University of Texas System Cancer Center | Recombinant monoclonal antibodies |
| US4361509A (en) * | 1981-12-14 | 1982-11-30 | Scripps Clinic And Research Foundation | Ultrapurification of factor VIII using monoclonal antibodies |
-
1983
- 1983-04-11 ES ES521371A patent/ES8404858A1/es not_active Expired
- 1983-04-11 CA CA000425555A patent/CA1209907A/en not_active Expired
- 1983-04-12 AT AT9019/83A patent/AT393386B/de not_active IP Right Cessation
- 1983-04-12 CH CH6699/83A patent/CH672028A5/de not_active IP Right Cessation
- 1983-04-12 GB GB08332644A patent/GB2128630B/en not_active Expired
- 1983-04-12 WO PCT/US1983/000524 patent/WO1983003678A1/en not_active Application Discontinuation
- 1983-04-12 IT IT20550/83A patent/IT1219779B/it active
- 1983-04-12 EP EP19830901671 patent/EP0105359A4/en not_active Withdrawn
- 1983-12-09 FI FI834530A patent/FI88403C/fi not_active IP Right Cessation
- 1983-12-13 ES ES528000A patent/ES8506902A1/es not_active Expired
- 1983-12-13 ES ES528001A patent/ES8706964A1/es not_active Expired
-
1987
- 1987-05-06 AU AU72569/87A patent/AU622099B2/en not_active Ceased
-
1991
- 1991-11-26 DK DK911921A patent/DK192191D0/da not_active Application Discontinuation
Also Published As
| Publication number | Publication date |
|---|---|
| ES8706964A1 (es) | 1987-07-01 |
| EP0105359A1 (en) | 1984-04-18 |
| IT1219779B (it) | 1990-05-24 |
| DK192191A (da) | 1991-11-26 |
| CH672028A5 (it) | 1989-10-13 |
| WO1983003678A1 (en) | 1983-10-27 |
| DK192191D0 (da) | 1991-11-26 |
| EP0105359A4 (en) | 1984-08-20 |
| ES528000A0 (es) | 1985-08-01 |
| AU7256987A (en) | 1987-09-03 |
| FI88403C (fi) | 1993-05-10 |
| ATA901983A (de) | 1991-03-15 |
| ES521371A0 (es) | 1984-05-16 |
| AU622099B2 (en) | 1992-04-02 |
| IT8320550A0 (it) | 1983-04-12 |
| GB8332644D0 (en) | 1984-01-11 |
| GB2128630B (en) | 1986-08-28 |
| FI834530A (fi) | 1983-12-09 |
| FI88403B (fi) | 1993-01-29 |
| GB2128630A (en) | 1984-05-02 |
| FI834530A0 (fi) | 1983-12-09 |
| ES8404858A1 (es) | 1984-05-16 |
| ES8506902A1 (es) | 1985-08-01 |
| ES528001A0 (es) | 1987-07-01 |
| AT393386B (de) | 1991-10-10 |
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