AU658926B2 - Purified immunoglobulin - Google Patents
Purified immunoglobulin Download PDFInfo
- Publication number
- AU658926B2 AU658926B2 AU25321/92A AU2532192A AU658926B2 AU 658926 B2 AU658926 B2 AU 658926B2 AU 25321/92 A AU25321/92 A AU 25321/92A AU 2532192 A AU2532192 A AU 2532192A AU 658926 B2 AU658926 B2 AU 658926B2
- Authority
- AU
- Australia
- Prior art keywords
- antibody
- column
- purified preparation
- protein
- purified
- 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
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Classifications
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- 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 (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GB909022547A GB9022547D0 (en) | 1990-10-17 | 1990-10-17 | Purified immunoglobulin |
Related Parent Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| AU87294/91A Addition AU649078C (en) | 1990-10-17 | 1991-10-17 | Purified CDW52-specific antibodies |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| AU2532192A AU2532192A (en) | 1993-02-11 |
| AU658926B2 true AU658926B2 (en) | 1995-05-04 |
Family
ID=10683866
Family Applications (3)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| AU25321/92A Expired AU658926B2 (en) | 1990-10-17 | 1992-09-23 | Purified immunoglobulin |
| AU70242/94A Abandoned AU7024294A (en) | 1990-10-17 | 1994-08-11 | Purified immunoglobulins |
| AU45218/97A Expired AU716402B2 (en) | 1990-10-17 | 1997-11-13 | Purified immunoglobulins |
Family Applications After (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| AU70242/94A Abandoned AU7024294A (en) | 1990-10-17 | 1994-08-11 | Purified immunoglobulins |
| AU45218/97A Expired AU716402B2 (en) | 1990-10-17 | 1997-11-13 | Purified immunoglobulins |
Country Status (29)
| Country | Link |
|---|---|
| US (1) | US5644036A (enExample) |
| EP (1) | EP0504363B2 (enExample) |
| JP (1) | JP2638680B2 (enExample) |
| KR (2) | KR960015399B1 (enExample) |
| AT (2) | ATA900791A (enExample) |
| AU (3) | AU658926B2 (enExample) |
| BE (1) | BE1004226A5 (enExample) |
| BR (1) | BR1100358A (enExample) |
| CA (1) | CA2069481C (enExample) |
| CH (2) | CH681455A5 (enExample) |
| DE (1) | DE69128774T3 (enExample) |
| DK (1) | DK0504363T4 (enExample) |
| ES (2) | ES2081742B1 (enExample) |
| FI (2) | FI110003B (enExample) |
| FR (2) | FR2668164A1 (enExample) |
| GB (2) | GB9022547D0 (enExample) |
| GR (3) | GR910100425A (enExample) |
| HU (1) | HUT64601A (enExample) |
| IE (1) | IE913560A1 (enExample) |
| IL (3) | IL102726A (enExample) |
| IT (1) | IT1250064B (enExample) |
| LU (1) | LU88122A1 (enExample) |
| MX (1) | MX9203794A (enExample) |
| MY (2) | MY119030A (enExample) |
| NZ (2) | NZ240247A (enExample) |
| PT (2) | PT99248B (enExample) |
| TW (1) | TW283710B (enExample) |
| WO (1) | WO1992007084A1 (enExample) |
| ZA (2) | ZA918259B (enExample) |
Families Citing this family (56)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB9022545D0 (en) | 1990-10-17 | 1990-11-28 | Wellcome Found | Culture medium |
| CA2120911A1 (en) * | 1991-10-15 | 1993-04-29 | Geoffrey Hale | Medicaments |
| 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 |
| KR19990036028A (ko) † | 1995-08-01 | 1999-05-25 | 다니엘 케르니 | 일본뇌염 백신의 공업적인 생산방법 및 이에 의한 백신 |
| US6090382A (en) * | 1996-02-09 | 2000-07-18 | Basf Aktiengesellschaft | Human antibodies that bind human TNFα |
| KR100317188B1 (ko) | 1996-02-09 | 2002-02-19 | 스타르크, 카르크 | 사람TNFα와결합하는사람항체 |
| 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 |
| DK1404428T3 (da) * | 2001-06-05 | 2006-10-30 | Genetics Inst Llc | Fremgangsmåder til oprensning af stærkt anioniske proteiner |
| GB0220894D0 (en) * | 2002-09-09 | 2002-10-16 | Millipore Uk Ltd | Method of separation |
| DK2261230T3 (en) | 2002-09-11 | 2017-06-12 | Chugai Pharmaceutical Co Ltd | Method of Protein Purification. |
| AU2003274011B2 (en) | 2002-10-15 | 2010-03-04 | Intercell Ag | Nucleic acids coding for adhesion factor 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 |
| CN1956731A (zh) * | 2003-12-22 | 2007-05-02 | 根茨美公司 | 抗－cd52抗体对糖尿病的治疗 |
| EP1869065B1 (en) | 2005-03-11 | 2020-05-06 | Wyeth LLC | A method of weak partitioning chromatography |
| CA2647846C (en) | 2006-03-31 | 2016-06-21 | Chugai Seiyaku Kabushiki Kaisha | Methods for controlling blood pharmacokinetics of antibodies |
| MX336725B (es) | 2007-09-26 | 2016-01-28 | Chugai Pharmaceutical Co Ltd | Metodo de modificacion del punto isoelectrico de anticuerpos medinate la sustitucion de aminoacidos en region de determinacion de complementariedad (cdr). |
| CA2721052C (en) | 2008-04-11 | 2023-02-21 | Chugai Seiyaku Kabushiki Kaisha | Antigen-binding molecule capable of binding to two or more antigen molecules repeatedly |
| KR20170113704A (ko) | 2009-05-13 | 2017-10-12 | 젠자임 코포레이션 | 항-인간 ｃｄ52 면역글루불린 |
| CA2761885A1 (en) | 2009-05-13 | 2010-11-18 | Genzyme Corporation | Methods and compositions for treating lupus |
| EP2519536A4 (en) * | 2009-12-29 | 2013-06-05 | Reddys Lab Ltd Dr | 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 |
| US20140234340A1 (en) | 2010-11-30 | 2014-08-21 | Chugai Seiyaku Kabushiki Kaisha | Antigen-binding molecule capable of binding to plurality of antigen molecules repeatedly |
| WO2012149197A2 (en) | 2011-04-27 | 2012-11-01 | Abbott Laboratories | 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 |
| US9150645B2 (en) | 2012-04-20 | 2015-10-06 | Abbvie, Inc. | Cell culture methods to reduce acidic species |
| US9181572B2 (en) | 2012-04-20 | 2015-11-10 | Abbvie, Inc. | Methods to modulate lysine variant distribution |
| US9249182B2 (en) | 2012-05-24 | 2016-02-02 | Abbvie, Inc. | Purification of antibodies using hydrophobic interaction chromatography |
| US9650411B2 (en) | 2012-08-07 | 2017-05-16 | Kyowa Hakko Kirin Co., Ltd. | Method of purifying protein |
| US9512214B2 (en) | 2012-09-02 | 2016-12-06 | Abbvie, Inc. | Methods to control protein heterogeneity |
| CA2883272A1 (en) | 2012-09-02 | 2014-03-06 | Abbvie Inc. | Methods to control protein heterogeneity |
| AU2013381687A1 (en) | 2013-03-12 | 2015-09-24 | Abbvie Inc. | Human antibodies that bind human TNF-alpha and methods of preparing the same |
| US9499614B2 (en) | 2013-03-14 | 2016-11-22 | Abbvie Inc. | Methods for modulating protein glycosylation profiles of recombinant protein therapeutics using monosaccharides and oligosaccharides |
| WO2014159579A1 (en) | 2013-03-14 | 2014-10-02 | Abbvie Inc. | MUTATED ANTI-TNFα ANTIBODIES AND METHODS OF THEIR USE |
| 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 |
| AR095199A1 (es) | 2013-03-15 | 2015-09-30 | Genzyme Corp | Anticuerpos anti-cd52 |
| 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 |
| US9598667B2 (en) | 2013-10-04 | 2017-03-21 | Abbvie Inc. | Use of metal ions for modulation of protein glycosylation profiles of recombinant proteins |
| US9085618B2 (en) | 2013-10-18 | 2015-07-21 | Abbvie, Inc. | Low acidic species compositions and methods for producing and using the same |
| US9181337B2 (en) | 2013-10-18 | 2015-11-10 | Abbvie, Inc. | Modulated lysine variant 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 |
| MY181081A (en) | 2013-12-27 | 2020-12-17 | Chugai Pharmaceutical Co Ltd | Method for purifying antibody having low isoelectric point |
| NZ730607A (en) | 2014-12-19 | 2022-07-01 | Chugai Pharmaceutical Co Ltd | Anti-myostatin antibodies, polypeptides containing variant fc regions, and methods of use |
| US10858391B2 (en) | 2015-07-31 | 2020-12-08 | Chugai Seiyaku Kabushiki Kaisha | Method for purifying composition comprising antibodies with anionic polymer |
| WO2017110981A1 (en) | 2015-12-25 | 2017-06-29 | Chugai Seiyaku Kabushiki Kaisha | Anti-myostatin antibodies and methods of use |
| ES2994244T3 (en) | 2016-07-25 | 2025-01-21 | Cephalon Llc | Affinity chromatography wash buffer |
| IL264626B (en) | 2016-08-05 | 2022-07-01 | Chugai Pharmaceutical Co Ltd | Composition for prophylaxis or treatment of il-8 related diseases |
| JP7273142B2 (ja) | 2019-03-29 | 2023-05-12 | 旭化成メディカル株式会社 | タンパク質の精製方法 |
| CN113692420B (zh) | 2019-04-08 | 2023-09-12 | 旭化成医疗株式会社 | 用于纯化含蛋白质的溶液的聚酰胺介质及其制造方法 |
| WO2020209318A1 (ja) | 2019-04-10 | 2020-10-15 | 中外製薬株式会社 | Ｆｃ領域改変抗体の精製方法 |
| EP4353735A4 (en) | 2021-06-10 | 2024-10-16 | Mitsubishi Chemical Corporation | SYNTHETIC ADSORBENT, ANTIBODY PURIFYING METHOD, AND ANTIBODY PRODUCTION METHOD |
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 |
| GB2216126B (en) * | 1988-02-12 | 1992-06-03 | Medical Res Council | Antibodies to the antigen campath-1 |
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1990
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