JPH0543719B2 - - Google Patents
Info
- Publication number
- JPH0543719B2 JPH0543719B2 JP3109760A JP10976091A JPH0543719B2 JP H0543719 B2 JPH0543719 B2 JP H0543719B2 JP 3109760 A JP3109760 A JP 3109760A JP 10976091 A JP10976091 A JP 10976091A JP H0543719 B2 JPH0543719 B2 JP H0543719B2
- Authority
- JP
- Japan
- Prior art keywords
- immunoglobulin
- molecules
- protein
- igg
- aqueous
- 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
- 102000004169 proteins and genes Human genes 0.000 claims description 35
- 108090000623 proteins and genes Proteins 0.000 claims description 35
- 229940027941 immunoglobulin g Drugs 0.000 claims description 24
- 239000000243 solution Substances 0.000 claims description 20
- 238000000034 method Methods 0.000 claims description 19
- 229920000936 Agarose Polymers 0.000 claims description 12
- 150000003839 salts Chemical class 0.000 claims description 12
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 claims description 8
- 239000012062 aqueous buffer Substances 0.000 claims description 8
- 206010003445 Ascites Diseases 0.000 claims description 6
- 239000012530 fluid Substances 0.000 claims description 6
- 239000007790 solid phase Substances 0.000 claims description 6
- 239000007853 buffer solution Substances 0.000 claims description 5
- 238000001042 affinity chromatography Methods 0.000 claims description 4
- 239000011260 aqueous acid Substances 0.000 claims description 4
- 239000011780 sodium chloride Substances 0.000 claims description 4
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 claims description 3
- 229910052921 ammonium sulfate Inorganic materials 0.000 claims description 3
- 235000011130 ammonium sulphate Nutrition 0.000 claims description 3
- 238000002156 mixing Methods 0.000 claims description 2
- 239000012148 binding buffer Substances 0.000 description 8
- 238000002955 isolation Methods 0.000 description 8
- 238000012360 testing method Methods 0.000 description 7
- 239000000203 mixture Substances 0.000 description 6
- 239000007864 aqueous solution Substances 0.000 description 4
- 239000000872 buffer Substances 0.000 description 4
- 108060003951 Immunoglobulin Proteins 0.000 description 3
- 229910019142 PO4 Inorganic materials 0.000 description 3
- 229920002684 Sepharose Polymers 0.000 description 3
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 3
- 238000010828 elution Methods 0.000 description 3
- 102000018358 immunoglobulin Human genes 0.000 description 3
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 3
- 239000010452 phosphate Substances 0.000 description 3
- 239000002953 phosphate buffered saline Substances 0.000 description 3
- 239000012266 salt solution Substances 0.000 description 3
- 238000000926 separation method Methods 0.000 description 3
- 102000028180 Glycophorins Human genes 0.000 description 2
- 108091005250 Glycophorins Proteins 0.000 description 2
- 206010035226 Plasma cell myeloma Diseases 0.000 description 2
- 210000004369 blood Anatomy 0.000 description 2
- 239000008280 blood Substances 0.000 description 2
- 210000004027 cell Anatomy 0.000 description 2
- 230000000694 effects Effects 0.000 description 2
- 210000003743 erythrocyte Anatomy 0.000 description 2
- 201000000050 myeloid neoplasm Diseases 0.000 description 2
- 238000012856 packing Methods 0.000 description 2
- 230000009257 reactivity Effects 0.000 description 2
- 238000011084 recovery Methods 0.000 description 2
- 239000001509 sodium citrate Substances 0.000 description 2
- NLJMYIDDQXHKNR-UHFFFAOYSA-K sodium citrate Chemical compound O.O.[Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NLJMYIDDQXHKNR-UHFFFAOYSA-K 0.000 description 2
- 239000007787 solid Substances 0.000 description 2
- 102000009027 Albumins Human genes 0.000 description 1
- 108010088751 Albumins Proteins 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 239000011324 bead Substances 0.000 description 1
- 230000008033 biological extinction Effects 0.000 description 1
- 238000004132 cross linking Methods 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 239000003480 eluent Substances 0.000 description 1
- 239000012149 elution buffer Substances 0.000 description 1
- 238000002523 gelfiltration Methods 0.000 description 1
- 229940072221 immunoglobulins Drugs 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 229940043515 other immunoglobulins in atc Drugs 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 230000000630 rising effect Effects 0.000 description 1
- 239000001488 sodium phosphate Substances 0.000 description 1
- 229910000162 sodium phosphate Inorganic materials 0.000 description 1
- VGTPCRGMBIAPIM-UHFFFAOYSA-M sodium thiocyanate Chemical compound [Na+].[S-]C#N VGTPCRGMBIAPIM-UHFFFAOYSA-M 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 210000004989 spleen cell Anatomy 0.000 description 1
- 238000010998 test method Methods 0.000 description 1
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
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
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S436/00—Chemistry: analytical and immunological testing
- Y10S436/828—Protein A
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S530/00—Chemistry: natural resins or derivatives; peptides or proteins; lignins or reaction products thereof
- Y10S530/82—Proteins from microorganisms
- Y10S530/825—Bacteria
Landscapes
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Health & Medical Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Life Sciences & Earth Sciences (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Immunology (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US06/623,797 US4704366A (en) | 1984-06-22 | 1984-06-22 | Process for binding IgG to protein A |
| US623797 | 1984-06-22 |
Related Parent Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP60135808A Division JPS6112631A (ja) | 1984-06-22 | 1985-06-21 | 免疫グロブリンｇ分子のプロテインａへの結合方法 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPH04234899A JPH04234899A (ja) | 1992-08-24 |
| JPH0543719B2 true JPH0543719B2 (enExample) | 1993-07-02 |
Family
ID=24499435
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP60135808A Granted JPS6112631A (ja) | 1984-06-22 | 1985-06-21 | 免疫グロブリンｇ分子のプロテインａへの結合方法 |
| JP3109760A Granted JPH04234899A (ja) | 1984-06-22 | 1991-04-15 | 免疫グロブリンｇ分子の単離方法 |
Family Applications Before (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP60135808A Granted JPS6112631A (ja) | 1984-06-22 | 1985-06-21 | 免疫グロブリンｇ分子のプロテインａへの結合方法 |
Country Status (4)
| Country | Link |
|---|---|
| US (1) | US4704366A (enExample) |
| JP (2) | JPS6112631A (enExample) |
| DE (1) | DE3521679A1 (enExample) |
| GB (1) | GB2160530B (enExample) |
Families Citing this family (56)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5283323A (en) * | 1985-08-07 | 1994-02-01 | The United States Of America As Represented By The Department Of Health And Human Services | Method of producing immune response |
| US4977247A (en) * | 1986-02-14 | 1990-12-11 | Genex Corporation | Immobilized protein G variants and the use thereof |
| SE459662B (sv) * | 1986-03-21 | 1989-07-24 | Pharmacia Ab | Hybrid-dna-molekyl som kodar foer ett protein med samma igg specificitet som protein g, plasmid innehaallande densamma samt foerfarande foer framstaellning av proteinet |
| US5089605A (en) * | 1987-03-13 | 1992-02-18 | Repligen Corporation | Immobilized immunoglobulin-binding proteins |
| JPS6419024A (en) * | 1987-07-15 | 1989-01-23 | Tosoh Corp | Separation of immunoglobulin g subclass |
| US4981961A (en) * | 1988-09-12 | 1991-01-01 | Bioprobe International, Inc. | Synthetic affinity ligand compositions and methods for purification and recovery of organic molecules |
| US4933435A (en) | 1989-04-05 | 1990-06-12 | Bioprobe International | Antibody purification process |
| US5151504A (en) * | 1989-11-17 | 1992-09-29 | E. R. Squibb & Sons, Inc. | Method for purification of monoclonal antibodies |
| US5077391A (en) * | 1989-12-01 | 1991-12-31 | Raison Robert L | Purification of immunoglobulin M |
| JPH03185000A (ja) * | 1989-12-15 | 1991-08-12 | Tosoh Corp | プロテインＡと免疫グロブリンＧ（ＩｇＧ）との結合方法 |
| US5200471A (en) * | 1990-11-05 | 1993-04-06 | Minnesota Mining And Manufacturing Company | Biomolecules covalently immobilized with a high bound specific biological activity and method of preparing same |
| US5245016A (en) * | 1991-01-31 | 1993-09-14 | University Of Utah Research Foundation | Pseudomonas maltophilia immunoglobulin binding protein and methods for its use |
| JP3607289B2 (ja) * | 1993-03-29 | 2005-01-05 | ミネソタ マイニング アンド マニュファクチャリング カンパニー | 多孔質支持体（ｐ．ｅ．アズラクトン）の内部にリガンドをカップリングする方法及びその使用法 |
| US5593822A (en) * | 1993-12-07 | 1997-01-14 | John Wayne Cancer Institute | IgG depleted serum preparations and methods for antibody production |
| US5561045A (en) * | 1994-01-04 | 1996-10-01 | Intracel Corporation | Detection reagent, article, and immunoassay method |
| JPH08511280A (ja) * | 1994-04-01 | 1996-11-26 | ユニシン・テクノロジーズ・インコーポレーテッド | 合成親和性リガンドを用いた免疫グロブリンの精製のための高塩濃度結合バッファー |
| KR20110140143A (ko) * | 2002-11-26 | 2011-12-30 | 애보트 바이오테라퓨틱스 코포레이션 | 혈관형성을 조절하는 α5β1 인테그린에 대한 키메라성 및 인간화 항체 |
| US7285268B2 (en) * | 2002-11-26 | 2007-10-23 | Pdl Biopharma, Inc. | Chimeric and humanized antibodies to α5β1 integrin that modulate angiogenesis |
| US7276589B2 (en) | 2002-11-26 | 2007-10-02 | Pdl Biopharma, Inc. | Chimeric and humanized antibodies to α5β1 integrin that modulate angiogenesis |
| NZ549893A (en) * | 2004-03-24 | 2010-05-28 | Facet Biotech Corp | Use of anti-alpha5beta1 antibodiesin a stabilising solution to inhibit cancer cell proliferation |
| CA2694644A1 (en) * | 2007-07-27 | 2009-02-05 | Vanitha Ramakrishnan | Pharmaceutical combinations |
| US20100158893A1 (en) * | 2008-12-19 | 2010-06-24 | Baxter International Inc. | Systems and methods for obtaining immunoglobulin from blood |
| WO2011064910A1 (ja) * | 2009-11-25 | 2011-06-03 | パナソニック株式会社 | 免疫測定方法 |
| PT2513134T (pt) | 2009-12-18 | 2017-12-14 | Novartis Ag | Solução de lavagem e método para cromatografia de afinidade |
| WO2012149197A2 (en) | 2011-04-27 | 2012-11-01 | Abbott Laboratories | Methods for controlling the galactosylation profile of recombinantly-expressed proteins |
| EP3489685B1 (en) | 2011-11-21 | 2023-11-01 | Zoetis Services LLC | Signal amplification in lateral flow and related immunoassays |
| US9150645B2 (en) | 2012-04-20 | 2015-10-06 | Abbvie, Inc. | Cell culture methods to reduce acidic species |
| US9067990B2 (en) | 2013-03-14 | 2015-06-30 | Abbvie, Inc. | Protein purification using displacement chromatography |
| US9181572B2 (en) | 2012-04-20 | 2015-11-10 | Abbvie, Inc. | Methods to modulate lysine variant distribution |
| US20140010820A1 (en) * | 2012-05-21 | 2014-01-09 | Abbvie, Inc. | Novel purification of non-human antibodies using protein a affinity chromatography |
| US9249182B2 (en) | 2012-05-24 | 2016-02-02 | Abbvie, Inc. | Purification of antibodies using hydrophobic interaction chromatography |
| CA2883272A1 (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 |
| AU2013381687A1 (en) | 2013-03-12 | 2015-09-24 | Abbvie Inc. | Human antibodies that bind human TNF-alpha and methods of preparing the same |
| 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 |
| US9499614B2 (en) | 2013-03-14 | 2016-11-22 | Abbvie Inc. | Methods for modulating protein glycosylation profiles of recombinant protein therapeutics using monosaccharides and oligosaccharides |
| US9598667B2 (en) | 2013-10-04 | 2017-03-21 | 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 |
| US8946395B1 (en) | 2013-10-18 | 2015-02-03 | Abbvie Inc. | Purification of proteins using hydrophobic interaction chromatography |
| US9085618B2 (en) | 2013-10-18 | 2015-07-21 | Abbvie, Inc. | Low acidic species compositions and methods for producing and using the same |
| WO2015073884A2 (en) | 2013-11-15 | 2015-05-21 | Abbvie, Inc. | Glycoengineered binding protein compositions |
| TWI691716B (zh) | 2014-08-13 | 2020-04-21 | 美商艾巴希斯公司 | 電漿特異性結合搭配物檢定中之信號放大 |
| US11566082B2 (en) | 2014-11-17 | 2023-01-31 | Cytiva Bioprocess R&D Ab | Mutated immunoglobulin-binding polypeptides |
| PL3331818T3 (pl) | 2015-08-04 | 2024-10-21 | Zoetis Services Llc | Wzmocnienie sygnału w testach plazmonowych partnerów swoistego wiązania na bazie roztworu |
| US10889615B2 (en) | 2016-05-11 | 2021-01-12 | Cytiva Bioprocess R&D Ab | Mutated immunoglobulin-binding polypeptides |
| CN109071613A (zh) | 2016-05-11 | 2018-12-21 | 通用电气医疗集团生物工艺研发股份公司 | 分离基质 |
| JP7031934B2 (ja) | 2016-05-11 | 2022-03-08 | サイティバ・バイオプロセス・アールアンドディ・アクチボラグ | 分離マトリックス |
| US10730908B2 (en) | 2016-05-11 | 2020-08-04 | Ge Healthcare Bioprocess R&D Ab | Separation method |
| US10654887B2 (en) | 2016-05-11 | 2020-05-19 | Ge Healthcare Bio-Process R&D Ab | Separation matrix |
| JP6987424B2 (ja) | 2016-05-11 | 2022-01-05 | サイティバ・バイオプロセス・アールアンドディ・アクチボラグ | 分離マトリックスを洗浄および／または消毒する方法 |
| CN109311949B (zh) | 2016-05-11 | 2022-09-16 | 思拓凡生物工艺研发有限公司 | 储存分离基质的方法 |
| US10703774B2 (en) | 2016-09-30 | 2020-07-07 | Ge Healthcare Bioprocess R&D Ab | Separation method |
| US12448411B2 (en) | 2016-09-30 | 2025-10-21 | Cytiva Bioprocess R&D Ab | Separation method |
| US11977072B2 (en) | 2017-01-30 | 2024-05-07 | Zoetis Services Llc | Solution-based plasmonic specific-binding partner assays using metallic nanostructures |
| CN119881293A (zh) | 2018-03-21 | 2025-04-25 | 沃特世科技公司 | 基于非抗体高亲和力的样品制备、吸附剂、装置和方法 |
Family Cites Families (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| SE413986B (sv) * | 1973-03-23 | 1980-07-07 | Exploaterings Ab Tbf | Sett att separera amfipatiska emnen innehallande bade hydrofila och hydrofoba grupper samt gelprodukt for genomforande av separationen |
| US4430318A (en) * | 1978-11-29 | 1984-02-07 | The United States Of America As Represented By The Department Of Health And Human Services | Immunoassay utilizing 125 I Protein A |
| US4230685A (en) * | 1979-02-28 | 1980-10-28 | Northwestern University | Method of magnetic separation of cells and the like, and microspheres for use therein |
| AU570911B2 (en) * | 1981-11-06 | 1988-03-31 | Baylor College Of Medicine | Immunoadsorbent based on immobilized protein a and its use |
-
1984
- 1984-06-22 US US06/623,797 patent/US4704366A/en not_active Expired - Fee Related
-
1985
- 1985-06-17 GB GB08515261A patent/GB2160530B/en not_active Expired
- 1985-06-18 DE DE19853521679 patent/DE3521679A1/de active Granted
- 1985-06-21 JP JP60135808A patent/JPS6112631A/ja active Granted
-
1991
- 1991-04-15 JP JP3109760A patent/JPH04234899A/ja active Granted
Also Published As
| Publication number | Publication date |
|---|---|
| GB2160530A (en) | 1985-12-24 |
| DE3521679C2 (enExample) | 1989-08-24 |
| JPH0455440B2 (enExample) | 1992-09-03 |
| GB2160530B (en) | 1987-10-28 |
| US4704366A (en) | 1987-11-03 |
| DE3521679A1 (de) | 1986-01-02 |
| JPH04234899A (ja) | 1992-08-24 |
| GB8515261D0 (en) | 1985-07-17 |
| JPS6112631A (ja) | 1986-01-21 |
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