JP2015511637A5 - - Google Patents
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- Publication number
- JP2015511637A5 JP2015511637A5 JP2015503160A JP2015503160A JP2015511637A5 JP 2015511637 A5 JP2015511637 A5 JP 2015511637A5 JP 2015503160 A JP2015503160 A JP 2015503160A JP 2015503160 A JP2015503160 A JP 2015503160A JP 2015511637 A5 JP2015511637 A5 JP 2015511637A5
- Authority
- JP
- Japan
- Prior art keywords
- protein
- amino acid
- separation matrix
- acid residue
- asparagine
- 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.)
- Granted
Links
- 235000018102 proteins Nutrition 0.000 claims description 26
- 102000004169 proteins and genes Human genes 0.000 claims description 26
- 108090000623 proteins and genes Proteins 0.000 claims description 26
- 125000000539 amino acid group Chemical group 0.000 claims description 12
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 claims description 9
- 235000009582 asparagine Nutrition 0.000 claims description 9
- 229960001230 asparagine Drugs 0.000 claims description 9
- 108010025221 plasma protein Z Proteins 0.000 claims description 9
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 claims description 7
- 239000000178 monomer Substances 0.000 claims description 7
- 230000035772 mutation Effects 0.000 claims description 7
- 108060003951 Immunoglobulin Proteins 0.000 claims description 6
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 claims description 6
- 102000018358 immunoglobulin Human genes 0.000 claims description 6
- 238000000034 method Methods 0.000 claims description 6
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 claims description 4
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 claims description 3
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 claims description 3
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 claims description 3
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 claims description 3
- 239000004472 Lysine Substances 0.000 claims description 3
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 claims description 3
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 claims description 3
- 239000004473 Threonine Substances 0.000 claims description 3
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 claims description 2
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 claims description 2
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 claims description 2
- 108010088160 Staphylococcal Protein A Proteins 0.000 claims description 2
- 125000000613 asparagine group Chemical group N[C@@H](CC(N)=O)C(=O)* 0.000 claims description 2
- 235000013922 glutamic acid Nutrition 0.000 claims description 2
- 239000004220 glutamic acid Substances 0.000 claims description 2
- 239000011159 matrix material Substances 0.000 claims 8
- 238000000926 separation method Methods 0.000 claims 7
- 239000012149 elution buffer Substances 0.000 claims 6
- 239000000243 solution Substances 0.000 claims 4
- GNFTZDOKVXKIBK-UHFFFAOYSA-N 3-(2-methoxyethoxy)benzohydrazide Chemical compound COCCOC1=CC=CC(C(=O)NN)=C1 GNFTZDOKVXKIBK-UHFFFAOYSA-N 0.000 claims 3
- 102220491086 ADP-ribosylation factor 6_N28A_mutation Human genes 0.000 claims 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 claims 3
- 210000004899 c-terminal region Anatomy 0.000 claims 2
- 210000004027 cell Anatomy 0.000 claims 2
- 235000018417 cysteine Nutrition 0.000 claims 2
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 claims 2
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 claims 2
- 235000018977 lysine Nutrition 0.000 claims 2
- 125000001500 prolyl group Chemical group [H]N1C([H])(C(=O)[*])C([H])([H])C([H])([H])C1([H])[H] 0.000 claims 2
- 235000004400 serine Nutrition 0.000 claims 2
- 239000000126 substance Substances 0.000 claims 2
- 235000008521 threonine Nutrition 0.000 claims 2
- NWUYHJFMYQTDRP-UHFFFAOYSA-N 1,2-bis(ethenyl)benzene;1-ethenyl-2-ethylbenzene;styrene Chemical compound C=CC1=CC=CC=C1.CCC1=CC=CC=C1C=C.C=CC1=CC=CC=C1C=C NWUYHJFMYQTDRP-UHFFFAOYSA-N 0.000 claims 1
- ZNEMGFATAVGQSF-UHFFFAOYSA-N 1-(2-amino-6,7-dihydro-4H-[1,3]thiazolo[4,5-c]pyridin-5-yl)-2-[5-[2-(2,3-dihydro-1H-inden-2-ylamino)pyrimidin-5-yl]-1,3,4-oxadiazol-2-yl]ethanone Chemical compound NC=1SC2=C(CN(CC2)C(CC=2OC(=NN=2)C=2C=NC(=NC=2)NC2CC3=CC=CC=C3C2)=O)N=1 ZNEMGFATAVGQSF-UHFFFAOYSA-N 0.000 claims 1
- 241000588724 Escherichia coli Species 0.000 claims 1
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 claims 1
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 claims 1
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 claims 1
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 claims 1
- 235000004279 alanine Nutrition 0.000 claims 1
- 239000012670 alkaline solution Substances 0.000 claims 1
- 235000003704 aspartic acid Nutrition 0.000 claims 1
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 claims 1
- 239000000872 buffer Substances 0.000 claims 1
- 239000003729 cation exchange resin Substances 0.000 claims 1
- 210000004978 chinese hamster ovary cell Anatomy 0.000 claims 1
- 238000004140 cleaning Methods 0.000 claims 1
- 230000007423 decrease Effects 0.000 claims 1
- 102000028557 immunoglobulin binding proteins Human genes 0.000 claims 1
- 108091009323 immunoglobulin binding proteins Proteins 0.000 claims 1
- 229960000310 isoleucine Drugs 0.000 claims 1
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 claims 1
- 239000011534 wash buffer Substances 0.000 claims 1
- 238000005406 washing Methods 0.000 claims 1
- 238000010828 elution Methods 0.000 description 5
- 229940072221 immunoglobulins Drugs 0.000 description 4
- 235000001014 amino acid Nutrition 0.000 description 3
- 229940024606 amino acid Drugs 0.000 description 3
- 150000001413 amino acids Chemical class 0.000 description 3
- 102000014914 Carrier Proteins Human genes 0.000 description 2
- 108091008324 binding proteins Proteins 0.000 description 2
- 230000037430 deletion Effects 0.000 description 2
- 238000012217 deletion Methods 0.000 description 2
- 125000000487 histidyl group Chemical group [H]N([H])C(C(=O)O*)C([H])([H])C1=C([H])N([H])C([H])=N1 0.000 description 2
- 102000018071 Immunoglobulin Fc Fragments Human genes 0.000 description 1
- 108010091135 Immunoglobulin Fc Fragments Proteins 0.000 description 1
- 102000008300 Mutant Proteins Human genes 0.000 description 1
- 108010021466 Mutant Proteins Proteins 0.000 description 1
- 238000010364 biochemical engineering Methods 0.000 description 1
- 102000037865 fusion proteins Human genes 0.000 description 1
- 108020001507 fusion proteins Proteins 0.000 description 1
- 230000002163 immunogen Effects 0.000 description 1
- 150000003147 proline derivatives Chemical group 0.000 description 1
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| SE1250304-1 | 2012-03-28 | ||
| SE1250304 | 2012-03-28 | ||
| SE1250493 | 2012-05-15 | ||
| SE1250493-2 | 2012-05-15 | ||
| PCT/SE2013/050335 WO2013147691A1 (en) | 2012-03-28 | 2013-03-26 | Affinity chromatography matrix |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| JP2015511637A JP2015511637A (ja) | 2015-04-20 |
| JP2015511637A5 true JP2015511637A5 (https=) | 2017-06-08 |
| JP6420756B2 JP6420756B2 (ja) | 2018-11-07 |
Family
ID=49260785
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2015503160A Active JP6420756B2 (ja) | 2012-03-28 | 2013-03-26 | アフィニティークロマトグラフィーマトリックス |
Country Status (4)
| Country | Link |
|---|---|
| US (1) | US10189891B2 (https=) |
| EP (1) | EP2831096B1 (https=) |
| JP (1) | JP6420756B2 (https=) |
| WO (1) | WO2013147691A1 (https=) |
Families Citing this family (22)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP2831096B1 (en) | 2012-03-28 | 2020-04-29 | GE Healthcare BioProcess R&D AB | Affinity chromatography matrix |
| EP3042954A4 (en) * | 2013-09-06 | 2017-03-22 | Kaneka Corporation | Dissociation capacity-boosted ligand for affinity dissociation matrix |
| CN105481954B (zh) * | 2014-09-16 | 2021-03-26 | 亿一生物制药(北京)有限公司 | 一种重组蛋白a及其应用 |
| US11566082B2 (en) | 2014-11-17 | 2023-01-31 | Cytiva Bioprocess R&D Ab | Mutated immunoglobulin-binding polypeptides |
| WO2017014261A1 (ja) * | 2015-07-22 | 2017-01-26 | 株式会社カネカ | 抗体様タンパク質の精製方法 |
| WO2017194592A1 (en) | 2016-05-11 | 2017-11-16 | Ge Healthcare Bioprocess R&D Ab | Method of storing a separation matrix |
| WO2017194593A1 (en) | 2016-05-11 | 2017-11-16 | Ge Healthcare Bioprocess R&D Ab | Method of cleaning and/or sanitizing a separation matrix |
| 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 |
| US10889615B2 (en) | 2016-05-11 | 2021-01-12 | Cytiva Bioprocess R&D Ab | Mutated immunoglobulin-binding polypeptides |
| US10654887B2 (en) | 2016-05-11 | 2020-05-19 | Ge Healthcare Bio-Process R&D Ab | Separation matrix |
| US10703774B2 (en) | 2016-09-30 | 2020-07-07 | Ge Healthcare Bioprocess R&D Ab | Separation method |
| US10513537B2 (en) | 2016-05-11 | 2019-12-24 | Ge Healthcare Bioprocess R&D Ab | Separation matrix |
| KR102579850B1 (ko) | 2016-07-22 | 2023-09-18 | 암젠 인크 | Fc-함유 단백질의 정제 방법 |
| US12448411B2 (en) | 2016-09-30 | 2025-10-21 | Cytiva Bioprocess R&D Ab | Separation method |
| GB201703116D0 (en) * | 2017-02-27 | 2017-04-12 | Ge Healthcare Bioprocess R&D Ab | A seperation matrix and a method of seperating antibodies |
| GB202109246D0 (en) * | 2021-06-28 | 2021-08-11 | Cytiva Bioprocess R & D Ab | A method of separating bispecific antibodies |
| GB202113626D0 (en) | 2021-09-24 | 2021-11-10 | Cytiva Bioprocess R & D Ab | FC binding polypeptides |
| EP4435107A4 (en) * | 2021-11-29 | 2025-12-31 | Tosoh Corp | ANTIBODY ISOLATION METHOD |
| CN114409748A (zh) * | 2022-01-28 | 2022-04-29 | 博格隆(浙江)生物技术有限公司 | 蛋白a的b结构域和z结构域突变体及其应用 |
| WO2026057420A1 (en) | 2024-09-10 | 2026-03-19 | Cytiva Bioprocess R&D Ab | Affinity ligand for purification of antibodies of isotype iga |
| EP4717704A1 (en) * | 2024-09-26 | 2026-04-01 | Cytiva BioProcess R&D AB | Novel protein a ligand that enables milder elution |
Family Cites Families (23)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| SE8505922D0 (sv) | 1985-12-13 | 1985-12-13 | Kabigen Ab | Construction of an igg binding protein to facilitate downstream processing using protein engineering |
| JP2519136B2 (ja) | 1991-07-25 | 1996-07-31 | オリエンタル酵母工業株式会社 | 分子量マ−カ− |
| EP0550771B1 (en) | 1991-07-25 | 1999-09-29 | Oriental Yeast Co., Ltd. | Immunoglobulin-binding artificial protein |
| SE9503925D0 (sv) | 1995-11-07 | 1995-11-07 | Pharmacia Biotech Ab | Separationsmedium för IgG |
| SE9601368D0 (sv) | 1996-04-11 | 1996-04-11 | Pharmacia Biotech Ab | Process for the production of a porous cross-linked polysaccharide gel |
| US6602977B1 (en) | 1999-04-19 | 2003-08-05 | Biovitrum Ab | Receptor structures |
| US7709209B2 (en) | 2002-03-25 | 2010-05-04 | Ge Healthcare Bio-Sciences Ab | Protein ligands |
| SE0200943D0 (sv) * | 2002-03-25 | 2002-03-25 | Amersham Biosciences Ab | Mutant protein |
| CA2531238C (en) * | 2003-07-04 | 2015-02-24 | Affibody Ab | Polypeptides having binding affinity for her2 |
| SE0400274D0 (sv) | 2004-02-09 | 2004-02-09 | Affibody Ab | New polypeptide |
| SE0402322D0 (sv) | 2004-09-22 | 2004-09-22 | Amersham Biosciences Ab | Method of preparing a chromatography matrix |
| WO2006092338A2 (en) * | 2005-03-01 | 2006-09-08 | Affibody Ab | Tnf-alpha binding polypeptide , uses thereof and methods employing it |
| CN102417557B (zh) * | 2005-08-03 | 2015-03-11 | 默克专利股份公司 | 亲水交联聚合物 |
| CN101287503A (zh) * | 2005-08-03 | 2008-10-15 | Rq生物科技有限公司 | 用于诊断IgA和IgM介导的肾脏疾病的方法和组合物 |
| WO2008039141A1 (en) * | 2006-09-29 | 2008-04-03 | Ge Healthcare Bio-Sciences Ab | Chromatography ligand comprising domain c from staphyloccocus aureus protein a for antibody isolation |
| WO2008085988A1 (en) * | 2007-01-05 | 2008-07-17 | Amgen Inc. | Methods of purifying proteins |
| JP5462461B2 (ja) | 2008-09-30 | 2014-04-02 | 株式会社東芝 | 不揮発性半導体記憶装置及びその駆動方法 |
| EP2389386A4 (en) | 2009-01-12 | 2013-11-06 | Ge Healthcare Bio Sciences Ab | affinity chromatography |
| SI2473617T1 (sl) | 2009-09-01 | 2020-07-31 | F. Hoffmann-La Roche Ag | Izboljšano prečiščevanje beljakovin z modificirano elucijo beljakovine A |
| WO2011118699A1 (ja) * | 2010-03-24 | 2011-09-29 | 株式会社カネカ | 免疫グロブリンに特異的に結合するタンパク質および免疫グロブリン結合性アフィニティーリガンド |
| JP5974342B2 (ja) * | 2010-12-20 | 2016-08-23 | ジーイー・ヘルスケア・バイオプロセス・アールアンドディ・アクチボラグ | アフィニティークロマトグラフィーマトリックス |
| CN103269762B (zh) * | 2010-12-20 | 2016-01-27 | 通用电气健康护理生物科学股份公司 | 亲和色谱基质 |
| EP2831096B1 (en) | 2012-03-28 | 2020-04-29 | GE Healthcare BioProcess R&D AB | Affinity chromatography matrix |
-
2013
- 2013-03-26 EP EP13767846.2A patent/EP2831096B1/en active Active
- 2013-03-26 US US14/385,336 patent/US10189891B2/en active Active
- 2013-03-26 WO PCT/SE2013/050335 patent/WO2013147691A1/en not_active Ceased
- 2013-03-26 JP JP2015503160A patent/JP6420756B2/ja active Active
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