JP2638680B2 - 精製イムノグロブリン - Google Patents
精製イムノグロブリンInfo
- Publication number
- JP2638680B2 JP2638680B2 JP3516509A JP51650991A JP2638680B2 JP 2638680 B2 JP2638680 B2 JP 2638680B2 JP 3516509 A JP3516509 A JP 3516509A JP 51650991 A JP51650991 A JP 51650991A JP 2638680 B2 JP2638680 B2 JP 2638680B2
- Authority
- JP
- Japan
- Prior art keywords
- antibody
- column
- purified
- protein
- purified antibody
- 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 - Lifetime
Links
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Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/06—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies from serum
- C07K16/065—Purification, fragmentation
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/395—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum
-
- 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
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
- C07K16/2893—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against CD52
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/24—Immunoglobulins specific features characterized by taxonomic origin containing regions, domains or residues from different species, e.g. chimeric, humanized or veneered
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/70—Fusion polypeptide containing domain for protein-protein interaction
- C07K2319/74—Fusion polypeptide containing domain for protein-protein interaction containing a fusion for binding to a cell surface receptor
- C07K2319/75—Fusion polypeptide containing domain for protein-protein interaction containing a fusion for binding to a cell surface receptor containing a fusion for activation of a cell surface receptor, e.g. thrombopoeitin, NPY and other peptide hormones
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Immunology (AREA)
- Medicinal Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Mycology (AREA)
- Veterinary Medicine (AREA)
- Microbiology (AREA)
- Animal Behavior & Ethology (AREA)
- Epidemiology (AREA)
- Pharmacology & Pharmacy (AREA)
- Public Health (AREA)
- Engineering & Computer Science (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Steroid Compounds (AREA)
- Saccharide Compounds (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GB9022547.5 | 1990-10-17 | ||
| GB909022547A GB9022547D0 (en) | 1990-10-17 | 1990-10-17 | Purified immunoglobulin |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPH05504579A JPH05504579A (ja) | 1993-07-15 |
| JP2638680B2 true JP2638680B2 (ja) | 1997-08-06 |
Family
ID=10683866
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP3516509A Expired - Lifetime JP2638680B2 (ja) | 1990-10-17 | 1991-10-17 | 精製イムノグロブリン |
Country Status (29)
Cited By (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2020203718A1 (ja) | 2019-03-29 | 2020-10-08 | 旭化成メディカル株式会社 | タンパク質の精製方法 |
| WO2020209267A1 (ja) | 2019-04-08 | 2020-10-15 | 旭化成メディカル株式会社 | タンパク質含有溶液精製用ポリアミド媒体及びその製造方法 |
| US10858391B2 (en) | 2015-07-31 | 2020-12-08 | Chugai Seiyaku Kabushiki Kaisha | Method for purifying composition comprising antibodies with anionic polymer |
| US11359194B2 (en) | 2008-04-11 | 2022-06-14 | Chugai Seiyaku Kabushiki Kaisha | Antigen-binding molecule capable of binding two or more antigen molecules repeatedly |
| US11454633B2 (en) | 2014-12-19 | 2022-09-27 | Chugai Seiyaku Kabushiki Kaisha | Anti-myostatin antibodies, polypeptides containing variant Fc regions, and methods of use |
| US11780912B2 (en) | 2016-08-05 | 2023-10-10 | Chugai Seiyaku Kabushiki Kaisha | Composition for prophylaxis or treatment of IL-8 related diseases |
| US12252532B2 (en) | 2015-12-25 | 2025-03-18 | Chugai Seiyaku Kabushiki Kaisha | Anti-myostatin antibodies and methods of use |
| US12473375B2 (en) | 2006-03-31 | 2025-11-18 | Chugai Seiyaku Kabushiki Kaisha | Methods for controlling blood pharmacokinetics of antibodies |
| US12516115B2 (en) | 2016-08-05 | 2026-01-06 | Chugai Seiyaku Kabushiki Kaisha | Composition for prophylaxis or treatment of IL-8 related diseases |
Families Citing this family (48)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB9022545D0 (en) | 1990-10-17 | 1990-11-28 | Wellcome Found | Culture medium |
| IL103418A (en) * | 1991-10-15 | 1997-11-20 | Wellcome Found | Therapeutic agent for the t-cell mediated inflammation of the joints and its production |
| GB9125768D0 (en) * | 1991-12-04 | 1992-02-05 | Hale Geoffrey | Therapeutic method |
| GB9300501D0 (en) * | 1993-01-09 | 1993-03-03 | Wellcome Found | Purification of immunoglobulin |
| NZ315357A (en) † | 1995-08-01 | 1999-08-30 | Pasteur Merieux Serums Vacc | Method for industrially producing a japanese encephalitis vaccine, and resulting vaccine |
| US6090382A (en) * | 1996-02-09 | 2000-07-18 | Basf Aktiengesellschaft | Human antibodies that bind human TNFα |
| WO1997029131A1 (en) * | 1996-02-09 | 1997-08-14 | Basf Aktiengesellschaft | HUMAN ANTIBODIES THAT BIND HUMAN TNF$g(a) |
| GB9603256D0 (en) * | 1996-02-16 | 1996-04-17 | Wellcome Found | Antibodies |
| US20030023043A1 (en) * | 2000-03-02 | 2003-01-30 | Kazuhisa Uchida | Method of separating and purifying protein |
| EP2336149A1 (en) | 2001-03-09 | 2011-06-22 | Chugai Seiyaku Kabushiki Kaisha | Protein purification method |
| JP4288153B2 (ja) * | 2001-06-05 | 2009-07-01 | ジェネティクス インスティテュート，エルエルシー | 非常に陰イオン性であるタンパク質を精製する方法 |
| GB0220894D0 (en) * | 2002-09-09 | 2002-10-16 | Millipore Uk Ltd | Method of separation |
| EP1561756B1 (en) | 2002-09-11 | 2015-12-23 | Chugai Seiyaku Kabushiki Kaisha | Method of purifying protein |
| EP2314604A3 (en) | 2002-10-15 | 2011-05-25 | Intercell AG | Nucleic acids coding for adhesion factors of group B streptococcus, adhesion factors of group B streptococcus and further uses thereof |
| GB0304576D0 (en) * | 2003-02-28 | 2003-04-02 | Lonza Biologics Plc | Protein a chromatography |
| BRPI0417993A (pt) * | 2003-12-22 | 2007-04-27 | Genzyme Corp | anticorpo anti-cd52 para tratamento da diabetes |
| CN104610422A (zh) * | 2005-03-11 | 2015-05-13 | 惠氏公司 | 弱分配层析的方法 |
| RU2510400C9 (ru) | 2007-09-26 | 2014-07-20 | Чугаи Сейяку Кабусики Кайся | Способ модификации изоэлектрической точки антитела с помощью аминокислотных замен в cdr |
| AU2010248935B2 (en) | 2009-05-13 | 2016-12-15 | Genzyme Corporation | Methods and compositions for treating lupus |
| SG176060A1 (en) | 2009-05-13 | 2011-12-29 | Genzyme Corp | Anti-human cd52 immunoglobulins |
| WO2011090719A2 (en) * | 2009-12-29 | 2011-07-28 | Dr. Reddy's Laboratories Ltd. | Protein purification by ion exchange |
| US20130096284A1 (en) | 2010-06-21 | 2013-04-18 | Kyowa Hakko Kirin Co., Ltd. | Method for purifying protein using amino acid |
| RU2467783C2 (ru) * | 2010-07-30 | 2012-11-27 | Закрытое акционерное общество "БиоХимМак СТ" | Способ хроматографического выделения иммуноглобулина |
| WO2012073992A1 (ja) | 2010-11-30 | 2012-06-07 | 中外製薬株式会社 | 複数分子の抗原に繰り返し結合する抗原結合分子 |
| US9062106B2 (en) | 2011-04-27 | 2015-06-23 | Abbvie Inc. | Methods for controlling the galactosylation profile of recombinantly-expressed proteins |
| GB201109238D0 (en) * | 2011-06-01 | 2011-07-13 | Antitope Ltd | Antibodies |
| US9067990B2 (en) | 2013-03-14 | 2015-06-30 | Abbvie, Inc. | Protein purification using displacement chromatography |
| WO2013158273A1 (en) | 2012-04-20 | 2013-10-24 | Abbvie Inc. | Methods to modulate c-terminal lysine variant distribution |
| US9334319B2 (en) | 2012-04-20 | 2016-05-10 | Abbvie Inc. | Low acidic species compositions |
| WO2013176754A1 (en) | 2012-05-24 | 2013-11-28 | Abbvie Inc. | Novel purification of antibodies using hydrophobic interaction chromatography |
| US9650411B2 (en) | 2012-08-07 | 2017-05-16 | Kyowa Hakko Kirin Co., Ltd. | Method of purifying protein |
| WO2014035475A1 (en) | 2012-09-02 | 2014-03-06 | Abbvie Inc. | Methods to control protein heterogeneity |
| US9512214B2 (en) | 2012-09-02 | 2016-12-06 | Abbvie, Inc. | Methods to control protein heterogeneity |
| CA2905010A1 (en) | 2013-03-12 | 2014-09-18 | Abbvie Inc. | Human antibodies that bind human tnf-alpha and methods of preparing the same |
| US8921526B2 (en) | 2013-03-14 | 2014-12-30 | Abbvie, Inc. | Mutated anti-TNFα antibodies and methods of their use |
| US9499614B2 (en) | 2013-03-14 | 2016-11-22 | Abbvie Inc. | Methods for modulating protein glycosylation profiles of recombinant protein therapeutics using monosaccharides and oligosaccharides |
| US9017687B1 (en) | 2013-10-18 | 2015-04-28 | Abbvie, Inc. | Low acidic species compositions and methods for producing and using the same using displacement chromatography |
| AU2013203043B2 (en) * | 2013-03-15 | 2016-10-06 | Takeda Pharmaceutical Company Limited | Methods to produce a human plasma-derived igg preparation enriched in brain disease-related natural iggs |
| AR095199A1 (es) | 2013-03-15 | 2015-09-30 | Genzyme Corp | Anticuerpos anti-cd52 |
| EP3052640A2 (en) | 2013-10-04 | 2016-08-10 | AbbVie Inc. | Use of metal ions for modulation of protein glycosylation profiles of recombinant proteins |
| US9181337B2 (en) | 2013-10-18 | 2015-11-10 | Abbvie, Inc. | Modulated lysine variant species compositions and methods for producing and using the same |
| US9085618B2 (en) | 2013-10-18 | 2015-07-21 | Abbvie, Inc. | Low acidic species compositions and methods for producing and using the same |
| US8946395B1 (en) | 2013-10-18 | 2015-02-03 | Abbvie Inc. | Purification of proteins using hydrophobic interaction chromatography |
| WO2015073884A2 (en) | 2013-11-15 | 2015-05-21 | Abbvie, Inc. | Glycoengineered binding protein compositions |
| BR112016014824A2 (pt) | 2013-12-27 | 2017-09-19 | Chugai Pharmaceutical Co Ltd | Método para purificar anticorpo que tem ponto isoelétrico baixo |
| CA3031028C (en) | 2016-07-25 | 2024-02-13 | Lu Wang | Affinity chromatography wash buffer |
| TW202104244A (zh) | 2019-04-10 | 2021-02-01 | 日商中外製藥股份有限公司 | Fc區域改變抗體的純化方法 |
| JPWO2022260091A1 (cg-RX-API-DMAC7.html) | 2021-06-10 | 2022-12-15 |
Family Cites Families (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5118796A (en) * | 1987-12-09 | 1992-06-02 | Centocor, Incorporated | Efficient large-scale purification of immunoglobulins and derivatives |
| DE68909441T2 (de) * | 1988-02-12 | 1994-02-10 | British Tech Group | Modifizierte Antikörper. |
-
1990
- 1990-10-17 GB GB909022547A patent/GB9022547D0/en active Pending
-
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- 1991-10-16 FR FR9112738A patent/FR2668164A1/fr active Granted
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- 1991-10-16 ZA ZA926191A patent/ZA926191B/xx unknown
- 1991-10-17 AT AT91917891T patent/ATE162552T1/de not_active IP Right Cessation
- 1991-10-17 AT AT0900791A patent/ATA900791A/de not_active Application Discontinuation
- 1991-10-17 ES ES91917891T patent/ES2112865T5/es not_active Expired - Lifetime
- 1991-10-17 EP EP91917891A patent/EP0504363B2/en not_active Expired - Lifetime
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- 1991-10-17 ES ES09250029A patent/ES2081742B1/es not_active Expired - Lifetime
- 1991-10-17 CA CA002069481A patent/CA2069481C/en not_active Expired - Lifetime
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-
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- 1992-02-28 GB GB9209529A patent/GB2253397A/en not_active Withdrawn
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- 1992-05-27 LU LU88122A patent/LU88122A1/xx unknown
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-
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- 1994-08-11 AU AU70242/94A patent/AU7024294A/en not_active Abandoned
- 1994-10-07 US US08/319,598 patent/US5644036A/en not_active Expired - Lifetime
-
1997
- 1997-04-28 BR BR1100358-8A patent/BR1100358A/pt active IP Right Grant
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-
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- 1998-04-10 GR GR980400777T patent/GR3026588T3/el unknown
Non-Patent Citations (2)
| Title |
|---|
| Ｊｏｕｒｎａｌ ｏｆ Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，Ｖｏｌ．９，Ｎｏ．２（１９８９），ＰＰ．８３−１０６ |
| Ｔｈｅ Ｌａｎｃｅｔ，１７Ｄｅｃ．１９８８，ＰＰ．１３９４−１３９９ |
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