IL91778A - A method for reducing the heterogeneity of monoclonal antibodies - Google Patents
A method for reducing the heterogeneity of monoclonal antibodiesInfo
- Publication number
- IL91778A IL91778A IL9177889A IL9177889A IL91778A IL 91778 A IL91778 A IL 91778A IL 9177889 A IL9177889 A IL 9177889A IL 9177889 A IL9177889 A IL 9177889A IL 91778 A IL91778 A IL 91778A
- Authority
- IL
- Israel
- Prior art keywords
- antibodies
- incubation
- heterogeneity
- culture
- hours
- Prior art date
Links
- 238000000034 method Methods 0.000 title claims description 59
- 230000009467 reduction Effects 0.000 title claims description 11
- 239000012531 culture fluid Substances 0.000 claims description 36
- 206010003445 Ascites Diseases 0.000 claims description 33
- 239000012530 fluid Substances 0.000 claims description 32
- 238000011534 incubation Methods 0.000 claims description 32
- 150000001413 amino acids Chemical class 0.000 claims description 13
- 210000004899 c-terminal region Anatomy 0.000 claims description 12
- 102000005367 Carboxypeptidases Human genes 0.000 claims description 10
- 108010006303 Carboxypeptidases Proteins 0.000 claims description 10
- 239000002253 acid Substances 0.000 claims description 5
- 150000007513 acids Chemical class 0.000 claims description 5
- 210000000628 antibody-producing cell Anatomy 0.000 claims description 5
- 230000001588 bifunctional effect Effects 0.000 claims description 3
- 238000006243 chemical reaction Methods 0.000 description 44
- 210000004027 cell Anatomy 0.000 description 29
- 235000001014 amino acid Nutrition 0.000 description 16
- 210000004408 hybridoma Anatomy 0.000 description 13
- 230000002349 favourable effect Effects 0.000 description 8
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 6
- 238000000746 purification Methods 0.000 description 6
- 108020004705 Codon Proteins 0.000 description 5
- 108020004414 DNA Proteins 0.000 description 5
- 102000004190 Enzymes Human genes 0.000 description 5
- 108090000790 Enzymes Proteins 0.000 description 5
- 125000003275 alpha amino acid group Chemical group 0.000 description 5
- 238000005277 cation exchange chromatography Methods 0.000 description 5
- 239000013256 coordination polymer Substances 0.000 description 5
- 108090000623 proteins and genes Proteins 0.000 description 5
- 108020004511 Recombinant DNA Proteins 0.000 description 4
- 230000000694 effects Effects 0.000 description 4
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 4
- 125000003588 lysine group Chemical group [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 4
- 108090000765 processed proteins & peptides Proteins 0.000 description 4
- 102000003670 Carboxypeptidase B Human genes 0.000 description 3
- 108090000087 Carboxypeptidase B Proteins 0.000 description 3
- 239000012141 concentrate Substances 0.000 description 3
- 238000004519 manufacturing process Methods 0.000 description 3
- 230000008569 process Effects 0.000 description 3
- 239000004017 serum-free culture medium Substances 0.000 description 3
- 239000007974 sodium acetate buffer Substances 0.000 description 3
- 239000011780 sodium chloride Substances 0.000 description 3
- 238000011282 treatment Methods 0.000 description 3
- 101800005309 Carboxy-terminal peptide Proteins 0.000 description 2
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 2
- 108060003951 Immunoglobulin Proteins 0.000 description 2
- 241001465754 Metazoa Species 0.000 description 2
- 108091028043 Nucleic acid sequence Proteins 0.000 description 2
- 210000000776 antibody secreting cell Anatomy 0.000 description 2
- 239000002738 chelating agent Substances 0.000 description 2
- 238000011161 development Methods 0.000 description 2
- 230000018109 developmental process Effects 0.000 description 2
- 102000018358 immunoglobulin Human genes 0.000 description 2
- 238000000338 in vitro Methods 0.000 description 2
- 235000018977 lysine Nutrition 0.000 description 2
- 102000004196 processed proteins & peptides Human genes 0.000 description 2
- 239000011541 reaction mixture Substances 0.000 description 2
- 241000894007 species Species 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 238000004448 titration Methods 0.000 description 2
- 230000009466 transformation Effects 0.000 description 2
- 241000894006 Bacteria Species 0.000 description 1
- 102000053602 DNA Human genes 0.000 description 1
- 108010016626 Dipeptides Proteins 0.000 description 1
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 1
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 1
- 102000006496 Immunoglobulin Heavy Chains Human genes 0.000 description 1
- 108010019476 Immunoglobulin Heavy Chains Proteins 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
- 241000699670 Mus sp. Species 0.000 description 1
- 206010028980 Neoplasm Diseases 0.000 description 1
- 206010035226 Plasma cell myeloma Diseases 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- RRUDCFGSUDOHDG-UHFFFAOYSA-N acetohydroxamic acid Chemical compound CC(O)=NO RRUDCFGSUDOHDG-UHFFFAOYSA-N 0.000 description 1
- 229960001171 acetohydroxamic acid Drugs 0.000 description 1
- 230000004075 alteration Effects 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 210000001124 body fluid Anatomy 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 239000013599 cloning vector Substances 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 238000011109 contamination Methods 0.000 description 1
- 238000012864 cross contamination Methods 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 108010083141 dipeptidyl carboxypeptidase Proteins 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 238000010494 dissociation reaction Methods 0.000 description 1
- 230000005593 dissociations Effects 0.000 description 1
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 230000004927 fusion Effects 0.000 description 1
- 125000003630 glycyl group Chemical group [H]N([H])C([H])([H])C(*)=O 0.000 description 1
- 239000008240 homogeneous mixture Substances 0.000 description 1
- WJRBRSLFGCUECM-UHFFFAOYSA-N hydantoin Chemical compound O=C1CNC(=O)N1 WJRBRSLFGCUECM-UHFFFAOYSA-N 0.000 description 1
- 229940091173 hydantoin Drugs 0.000 description 1
- 238000006698 hydrazinolysis reaction Methods 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 238000011031 large-scale manufacturing process Methods 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 201000000050 myeloid neoplasm Diseases 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 210000003200 peritoneal cavity Anatomy 0.000 description 1
- 239000013612 plasmid Substances 0.000 description 1
- 229920001184 polypeptide Polymers 0.000 description 1
- 230000035935 pregnancy Effects 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 238000004393 prognosis Methods 0.000 description 1
- 125000001500 prolyl group Chemical group [H]N1C([H])(C(=O)[*])C([H])([H])C([H])([H])C1([H])[H] 0.000 description 1
- 238000011002 quantification Methods 0.000 description 1
- 230000035484 reaction time Effects 0.000 description 1
- 230000003362 replicative effect Effects 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 238000005070 sampling Methods 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 210000004989 spleen cell Anatomy 0.000 description 1
- 230000002311 subsequent effect Effects 0.000 description 1
- 238000001890 transfection Methods 0.000 description 1
- 230000001960 triggered effect Effects 0.000 description 1
- 238000005533 tritiation Methods 0.000 description 1
- 239000013598 vector Substances 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
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)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US25078788A | 1988-09-28 | 1988-09-28 | |
| US25078888A | 1988-09-28 | 1988-09-28 | |
| US25078688A | 1988-09-28 | 1988-09-28 | |
| US07/364,056 US5126250A (en) | 1988-09-28 | 1989-06-09 | Method for the reduction of heterogeneity of monoclonal antibodies |
| CA000613379A CA1332367C (en) | 1988-09-28 | 1989-09-26 | Method for the reduction of heterogeneity of monoclonal antibodies |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| IL91778A true IL91778A (en) | 1994-10-07 |
Family
ID=27508376
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| IL9177889A IL91778A (en) | 1988-09-28 | 1989-09-26 | A method for reducing the heterogeneity of monoclonal antibodies |
Country Status (17)
| Country | Link |
|---|---|
| EP (1) | EP0361902B1 (ro) |
| JP (1) | JP2925181B2 (ro) |
| CN (1) | CN1041392A (ro) |
| AR (1) | AR242986A1 (ro) |
| AT (1) | ATE101876T1 (ro) |
| AU (1) | AU615576B2 (ro) |
| BG (1) | BG60017B2 (ro) |
| CA (1) | CA1332367C (ro) |
| DE (1) | DE68913251T2 (ro) |
| DK (1) | DK475389A (ro) |
| ES (1) | ES2049332T3 (ro) |
| IE (1) | IE63562B1 (ro) |
| IL (1) | IL91778A (ro) |
| MX (1) | MX170441B (ro) |
| NZ (1) | NZ230786A (ro) |
| PL (1) | PL162260B1 (ro) |
| RO (1) | RO105652B1 (ro) |
Families Citing this family (19)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| IN2014DN10515A (ro) | 2006-03-31 | 2015-08-21 | Chugai Pharmaceutical Co Ltd | |
| EP1878747A1 (en) | 2006-07-11 | 2008-01-16 | greenovation Biotech GmbH | Glyco-engineered antibodies |
| EP2031064A1 (de) * | 2007-08-29 | 2009-03-04 | Boehringer Ingelheim Pharma GmbH & Co. KG | Verfahren zur Steigerung von Proteintitern |
| ES2687808T3 (es) | 2007-09-26 | 2018-10-29 | Chugai Seiyaku Kabushiki Kaisha | Región constante de anticuerpo modificado |
| MX369784B (es) | 2007-09-26 | 2019-11-21 | Chugai Pharmaceutical Co Ltd | Metodo de modificacion del punto isoelectrico de anticuerpos mediante la sustitucion de aminoacidos en region de determinacion de complementariedad (cdr). |
| PT2708559T (pt) | 2008-04-11 | 2018-05-16 | Chugai Pharmaceutical Co Ltd | Molécula de ligação ao antigénio capaz de se ligar repetidamente a duas ou mais moléculas de antigénio |
| TWI440469B (zh) * | 2008-09-26 | 2014-06-11 | Chugai Pharmaceutical Co Ltd | Improved antibody molecules |
| US20120071634A1 (en) | 2009-03-19 | 2012-03-22 | Chugai Seiyaku Kabushiki Kaisha | Antibody Constant Region Variant |
| JP5717624B2 (ja) | 2009-03-19 | 2015-05-13 | 中外製薬株式会社 | 抗体定常領域改変体 |
| TWI654204B (zh) | 2010-11-30 | 2019-03-21 | 中外製藥股份有限公司 | 具有鈣依存性的抗原結合能力之抗體 |
| EP2660328A4 (en) * | 2010-12-28 | 2016-07-13 | Chugai Pharmaceutical Co Ltd | ANIMAL CELL CULTURE METHOD |
| NZ714549A (en) | 2012-04-30 | 2016-10-28 | Biocon Ltd | Targeted/immunomodulatory fusion proteins and methods for making same |
| PL2970512T3 (pl) | 2013-03-12 | 2019-03-29 | Biocon Limited | Immunomodulujące białka fuzyjne i sposoby ich otrzymywania |
| EP3009518B1 (en) | 2013-06-11 | 2020-08-12 | National Center of Neurology and Psychiatry | Method for predicting post-therapy prognosis of relapsing-remitting multiple sclerosis (rrms) patient, and method for determining applicability of novel therapy |
| CA2972393A1 (en) | 2015-02-27 | 2016-09-01 | Chugai Seiyaku Kabushiki Kaisha | Composition for treating il-6-related diseases |
| US10697883B2 (en) | 2015-05-19 | 2020-06-30 | National Center Of Neurology And Psychiatry | Method for determining application of therapy to multiple sclerosis (MS) patient |
| JP6976343B2 (ja) * | 2016-10-17 | 2021-12-08 | エンゼン・バイオサイエンシズ・リミテッドEnzene Biosciences Limited | 治療用タンパク質の不均質性を低減するための連続的方法 |
| JP7185884B2 (ja) | 2017-05-02 | 2022-12-08 | 国立研究開発法人国立精神・神経医療研究センター | Ｉｌ－６及び好中球の関連する疾患の治療効果の予測及び判定方法 |
| KR102771895B1 (ko) | 2017-10-20 | 2025-02-21 | 가꼬우호우징 효고 이카다이가쿠 | 항il-6 수용체 항체를 함유하는 수술 후의 유착을 억제하기 위한 의약 조성물 |
-
1989
- 1989-09-26 CA CA000613379A patent/CA1332367C/en not_active Expired - Fee Related
- 1989-09-26 IL IL9177889A patent/IL91778A/en not_active IP Right Cessation
- 1989-09-26 AR AR89310004A patent/AR242986A1/es active
- 1989-09-26 RO RO141765A patent/RO105652B1/ro unknown
- 1989-09-26 BG BG089846A patent/BG60017B2/bg unknown
- 1989-09-26 NZ NZ230786A patent/NZ230786A/xx unknown
- 1989-09-27 IE IE309489A patent/IE63562B1/en not_active IP Right Cessation
- 1989-09-27 DE DE68913251T patent/DE68913251T2/de not_active Expired - Fee Related
- 1989-09-27 AT AT89309851T patent/ATE101876T1/de not_active IP Right Cessation
- 1989-09-27 ES ES89309851T patent/ES2049332T3/es not_active Expired - Lifetime
- 1989-09-27 EP EP89309851A patent/EP0361902B1/en not_active Expired - Lifetime
- 1989-09-27 PL PL89281598A patent/PL162260B1/pl unknown
- 1989-09-27 MX MX017721A patent/MX170441B/es unknown
- 1989-09-27 AU AU42343/89A patent/AU615576B2/en not_active Ceased
- 1989-09-27 DK DK475389A patent/DK475389A/da not_active Application Discontinuation
- 1989-09-28 CN CN89107508.9A patent/CN1041392A/zh active Pending
- 1989-09-28 JP JP1256890A patent/JP2925181B2/ja not_active Expired - Fee Related
Also Published As
| Publication number | Publication date |
|---|---|
| IE893094L (en) | 1990-03-28 |
| JPH02163096A (ja) | 1990-06-22 |
| AU4234389A (en) | 1990-04-05 |
| ATE101876T1 (de) | 1994-03-15 |
| CA1332367C (en) | 1994-10-11 |
| AU615576B2 (en) | 1991-10-03 |
| AR242986A1 (es) | 1993-06-30 |
| DE68913251T2 (de) | 1994-06-23 |
| ES2049332T3 (es) | 1994-04-16 |
| RO105652B1 (ro) | 1992-11-30 |
| DE68913251D1 (de) | 1994-03-31 |
| NZ230786A (en) | 1991-11-26 |
| EP0361902A3 (en) | 1990-08-16 |
| PL162260B1 (pl) | 1993-09-30 |
| JP2925181B2 (ja) | 1999-07-28 |
| MX170441B (es) | 1993-08-23 |
| IE63562B1 (en) | 1995-05-17 |
| BG60017B2 (bg) | 1993-06-30 |
| CN1041392A (zh) | 1990-04-18 |
| EP0361902B1 (en) | 1994-02-23 |
| DK475389A (da) | 1990-03-29 |
| DK475389D0 (da) | 1989-09-27 |
| EP0361902A2 (en) | 1990-04-04 |
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Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| KB | Patent renewed | ||
| KB | Patent renewed | ||
| MM9K | Patent not in force due to non-payment of renewal fees |