DE3521679C2 - - Google Patents
Info
- Publication number
- DE3521679C2 DE3521679C2 DE3521679A DE3521679A DE3521679C2 DE 3521679 C2 DE3521679 C2 DE 3521679C2 DE 3521679 A DE3521679 A DE 3521679A DE 3521679 A DE3521679 A DE 3521679A DE 3521679 C2 DE3521679 C2 DE 3521679C2
- Authority
- DE
- Germany
- Prior art keywords
- protein
- immunoglobulin
- molecules
- solution
- buffer solution
- 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
- 102000004169 proteins and genes Human genes 0.000 claims description 42
- 108090000623 proteins and genes Proteins 0.000 claims description 42
- 229940027941 immunoglobulin g Drugs 0.000 claims description 17
- 238000000034 method Methods 0.000 claims description 17
- 108060003951 Immunoglobulin Proteins 0.000 claims description 13
- 102000018358 immunoglobulin Human genes 0.000 claims description 13
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 claims description 11
- 239000000243 solution Substances 0.000 claims description 11
- 239000007853 buffer solution Substances 0.000 claims description 10
- 150000003839 salts Chemical class 0.000 claims description 10
- 239000000203 mixture Substances 0.000 claims description 9
- 229920000936 Agarose Polymers 0.000 claims description 8
- 239000000872 buffer Substances 0.000 claims description 7
- 206010003445 Ascites Diseases 0.000 claims description 6
- 239000012530 fluid Substances 0.000 claims description 6
- 238000001042 affinity chromatography Methods 0.000 claims description 5
- 229910017053 inorganic salt Inorganic materials 0.000 claims description 5
- 239000011780 sodium chloride Substances 0.000 claims description 5
- 239000007790 solid phase Substances 0.000 claims description 5
- 230000007935 neutral effect Effects 0.000 claims description 4
- 239000007787 solid Substances 0.000 claims description 4
- 239000003513 alkali Substances 0.000 claims description 2
- 239000012266 salt solution Substances 0.000 claims description 2
- 239000007864 aqueous solution Substances 0.000 claims 4
- 230000002378 acidificating effect Effects 0.000 claims 2
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 claims 2
- 229910052921 ammonium sulfate Inorganic materials 0.000 claims 2
- 235000011130 ammonium sulphate Nutrition 0.000 claims 2
- 239000012062 aqueous buffer Substances 0.000 claims 2
- QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 claims 1
- QGZKDVFQNNGYKY-UHFFFAOYSA-O ammonium group Chemical group [NH4+] QGZKDVFQNNGYKY-UHFFFAOYSA-O 0.000 claims 1
- 150000004820 halides Chemical class 0.000 claims 1
- 238000000926 separation method Methods 0.000 description 10
- 239000012148 binding buffer Substances 0.000 description 9
- 229940072221 immunoglobulins Drugs 0.000 description 8
- QGZKDVFQNNGYKY-UHFFFAOYSA-N Ammonia Chemical compound N QGZKDVFQNNGYKY-UHFFFAOYSA-N 0.000 description 6
- 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 6
- 239000002953 phosphate buffered saline Substances 0.000 description 6
- 229920002684 Sepharose Polymers 0.000 description 4
- 238000010828 elution Methods 0.000 description 4
- 230000001900 immune effect Effects 0.000 description 4
- -1 For example Chemical class 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- 102000028180 Glycophorins Human genes 0.000 description 2
- 108091005250 Glycophorins Proteins 0.000 description 2
- 206010035226 Plasma cell myeloma Diseases 0.000 description 2
- 229910001615 alkaline earth metal halide Inorganic materials 0.000 description 2
- 238000004458 analytical method Methods 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
- 238000010790 dilution Methods 0.000 description 2
- 239000012895 dilution Substances 0.000 description 2
- 238000011049 filling Methods 0.000 description 2
- 201000000050 myeloid neoplasm Diseases 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 241000894007 species Species 0.000 description 2
- 102000009027 Albumins Human genes 0.000 description 1
- 108010088751 Albumins Proteins 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 230000002745 absorbent Effects 0.000 description 1
- 239000002250 absorbent Substances 0.000 description 1
- 239000012736 aqueous medium Substances 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 239000011324 bead Substances 0.000 description 1
- 102000023732 binding proteins Human genes 0.000 description 1
- 108091008324 binding proteins Proteins 0.000 description 1
- 230000008033 biological extinction Effects 0.000 description 1
- 210000002798 bone marrow cell Anatomy 0.000 description 1
- 230000003139 buffering effect Effects 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 239000001913 cellulose Substances 0.000 description 1
- 229920002678 cellulose Polymers 0.000 description 1
- 238000004132 cross linking Methods 0.000 description 1
- 239000003480 eluent Substances 0.000 description 1
- 239000012149 elution buffer Substances 0.000 description 1
- 210000003743 erythrocyte Anatomy 0.000 description 1
- 210000003617 erythrocyte membrane Anatomy 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 238000002523 gelfiltration Methods 0.000 description 1
- 210000004408 hybridoma Anatomy 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 229910021645 metal ion Inorganic materials 0.000 description 1
- 229940043515 other immunoglobulins in atc Drugs 0.000 description 1
- 230000010412 perfusion Effects 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 239000001509 sodium citrate Substances 0.000 description 1
- 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 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
- 210000004989 spleen cell Anatomy 0.000 description 1
- 150000003467 sulfuric acid derivatives Chemical class 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 (1)
| 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 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| DE3521679A1 DE3521679A1 (de) | 1986-01-02 |
| DE3521679C2 true DE3521679C2 (enExample) | 1989-08-24 |
Family
ID=24499435
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| DE19853521679 Granted DE3521679A1 (de) | 1984-06-22 | 1985-06-18 | Verfahren zum binden von igg an protein a |
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 |
|---|---|
| JPH0543719B2 (enExample) | 1993-07-02 |
| GB2160530A (en) | 1985-12-24 |
| 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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Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| 8110 | Request for examination paragraph 44 | ||
| D2 | Grant after examination | ||
| 8363 | Opposition against the patent | ||
| 8331 | Complete revocation |