RU2698392C2 - Способ очистки фактора свертывания крови viii - Google Patents
Способ очистки фактора свертывания крови viii Download PDFInfo
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- RU2698392C2 RU2698392C2 RU2015141849A RU2015141849A RU2698392C2 RU 2698392 C2 RU2698392 C2 RU 2698392C2 RU 2015141849 A RU2015141849 A RU 2015141849A RU 2015141849 A RU2015141849 A RU 2015141849A RU 2698392 C2 RU2698392 C2 RU 2698392C2
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- C—CHEMISTRY; METALLURGY
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- C07K—PEPTIDES
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- C07K14/745—Blood coagulation or fibrinolysis factors
- C07K14/755—Factors VIII, e.g. factor VIII C (AHF), factor VIII Ag (VWF)
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
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| DK2561070T3 (en) | 2010-04-20 | 2015-08-17 | Octapharma Ag | NEW STABILIZER FOR PHARMACEUTICAL PROTEINS |
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| KR102001662B1 (ko) | 2011-06-17 | 2019-10-01 | 학교법인 히가시-니뽄-가쿠엔 | 루프스 안티코아귤란트 검출용 혈액 응고시간의 측정방법 |
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| US20140154233A1 (en) * | 2012-12-05 | 2014-06-05 | Csl Limited | Method of purifying therapeutic proteins |
| US10188965B2 (en) | 2012-12-05 | 2019-01-29 | Csl Behring Gmbh | Hydrophobic charge induction chromatographic depletion of a protein from a solution |
| CN103880947B (zh) * | 2012-12-21 | 2016-01-13 | 武汉禾元生物科技股份有限公司 | 一种分离纯化高纯度重组人血清白蛋白的层析方法 |
| RU2768003C2 (ru) * | 2013-03-08 | 2022-03-22 | Джензим Корпорейшн | Интегрированное непрерывное производство терапевтических белковых лекарственных веществ |
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| SG11201508835YA (en) | 2013-07-12 | 2015-11-27 | Merck Patent Gmbh | Removal of fragments from a sample containing a target protein using activated carbon |
| US10947269B2 (en) | 2013-08-08 | 2021-03-16 | Bioverativ Therapeutics Inc. | Purification of chimeric FVIII molecules |
| WO2015044836A1 (en) | 2013-09-24 | 2015-04-02 | Pfizer Inc. | Compositions comprising heterogeneous populations of recombinant human clotting factor xa proteins |
| TWI709569B (zh) | 2014-01-17 | 2020-11-11 | 美商健臻公司 | 無菌層析樹脂及其用於製造方法的用途 |
| TWI671312B (zh) * | 2014-01-17 | 2019-09-11 | 美商健臻公司 | 無菌層析法及製法 |
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| US20160347787A1 (en) | 2014-02-04 | 2016-12-01 | Biogen Ma Inc. | Use of cation-exchange chromatography in the flow-through mode to enrich post-translational modifications |
| CN104861060A (zh) * | 2014-02-21 | 2015-08-26 | 神州细胞工程有限公司 | 一种纯化凝血因子viii的方法 |
| KR20170010750A (ko) | 2014-05-29 | 2017-02-01 | 에이전시 포 사이언스, 테크놀로지 앤드 리서치 | 단백질 추출 방법들 |
| US10626164B2 (en) * | 2014-07-25 | 2020-04-21 | Csl Limited | Purification of VWF |
| GB201506117D0 (en) * | 2015-04-10 | 2015-05-27 | Ge Healthcare Bio Sciences Ab | Method for chromatography |
| GB201506113D0 (en) | 2015-04-10 | 2015-05-27 | Ge Healthcare Bio Sciences Ab | Method for chromatography |
| WO2016207328A1 (en) * | 2015-06-24 | 2016-12-29 | Glycotope Gmbh | PROCESS FOR THE PURIFICATION OF γ-CARBOXYLATED POLYPEPTIDES |
| EP3205665A1 (en) * | 2016-02-11 | 2017-08-16 | Octapharma AG | Method of separating factor viii from blood products |
| GB201617240D0 (en) * | 2016-10-11 | 2016-11-23 | Profactor Pharma Ltd | Purification process |
| CN111183151B (zh) * | 2017-06-23 | 2024-06-07 | 武田药品工业株式会社 | 因子viii亚种的纯化 |
| CN107226859B (zh) * | 2017-08-10 | 2020-11-24 | 博雅生物制药集团股份有限公司 | 一种人凝血因子ⅷ的制备方法 |
| US11584777B2 (en) | 2017-08-31 | 2023-02-21 | Green Cross Corporation | Method for purifying a sulfatase protein |
| ES2991988T3 (es) | 2017-10-30 | 2024-12-05 | Takeda Pharmaceuticals Co | Detergentes compatibles con el medio ambiente para la inactivación de virus con envoltura lipídica |
| AU2019332764B2 (en) | 2018-08-31 | 2025-05-29 | Genzyme Corporation | Sterile chromatography resin and use thereof in manufacturing processes |
| EP4093745A4 (en) * | 2020-01-20 | 2024-03-06 | Wuxi Biologics Ireland Limited | NEW WASH BUFFER SOLUTION FOR AFFINITY CHROMATOGRAPHY |
| CN118217951B (zh) * | 2024-04-01 | 2025-05-23 | 山东建筑大学 | 一种水中的高纯度磷回收装置和方法 |
Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US8022187B2 (en) * | 2007-02-01 | 2011-09-20 | Baxter International Inc. | FVIII-independent FIX-mutant proteins for hemophilia A treatment |
| EP2486936A1 (en) * | 2007-06-13 | 2012-08-15 | CSL Behring GmbH | A composition comprising VWF and FVIII preparations for use in treating of bleeding disorders |
| UA101003C2 (uk) * | 2007-12-04 | 2013-02-25 | Эпитоп Интернешнл Нв | Пептид фактора fviii та його застосування для індукції толерантності у хворих гемофілією |
| RU2563236C2 (ru) * | 2008-07-10 | 2015-09-20 | Цсл Беринг Гмбх | Фактор фон виллебранда или фактор viii и фактор фон виллебранда для лечения коагулопатии, индуцированной ингибиторами тромбоцитов |
Family Cites Families (15)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4540573A (en) | 1983-07-14 | 1985-09-10 | New York Blood Center, Inc. | Undenatured virus-free biologically active protein derivatives |
| US5605884A (en) | 1987-10-29 | 1997-02-25 | Rhone-Poulenc Rorer Pharmaceuticals Inc. | Factor VIII formulations in high ionic strength media |
| US5316680A (en) * | 1992-10-21 | 1994-05-31 | Cornell Research Foundation, Inc. | Multimodal chromatographic separation media and process for using same |
| DE69402716T2 (de) | 1993-06-11 | 1997-12-11 | Northern Telecom Ltd., Montreal, Quebec | Verfahren zur versorgung von durch den anwender gesteuerten anrufverwaltungsdiensten |
| DE4337573C1 (de) * | 1993-11-04 | 1995-05-18 | Octapharma Ag | Verfahren zur Herstellung einer virusinaktivierten Faktor VIII enthaltenden Fraktion mittels chromatographischer Methoden |
| SE9403915D0 (sv) | 1994-11-14 | 1994-11-14 | Annelie Almstedt | Process A |
| AUPR638801A0 (en) * | 2001-07-13 | 2001-08-09 | Life Therapeutics Limited | Factor viii separation |
| AU2005216847B2 (en) * | 2004-02-27 | 2010-04-01 | Cytiva Bioprocess R&D Ab | A process for the purification of antibodies |
| US9624260B2 (en) | 2004-06-07 | 2017-04-18 | Therapure Biopharma Inc. | Process for isolation of plasma or serum proteins |
| EP1707634A1 (en) | 2005-03-29 | 2006-10-04 | Octapharma AG | Method for isolation of recombinantly produced proteins |
| FR2887883B1 (fr) * | 2005-06-29 | 2007-08-31 | Lab Francais Du Fractionnement | Procede de separation des proteines fibrinogene, facteur xiii et colle biologique d'une fraction plasmatique solubilisee et de preparation de concentres lyophilises desdites proteines |
| EP1739179A1 (en) | 2005-06-30 | 2007-01-03 | Octapharma AG | Serum-free stable transfection and production of recombinant human proteins in human cell lines |
| BRPI0713252C1 (pt) * | 2006-07-14 | 2021-05-25 | Genentech Inc | processo para a recuperação de fator de crescimento endotelial vascular (vegf) recombinante reenovelado |
| RU2324495C1 (ru) * | 2006-08-31 | 2008-05-20 | Федеральное государственное унитарное предприятие "Научно-производственное объединение по медицинским иммунобиологическим препаратам "Микроген" Министерства здравоохранения Российской Федерации | Способ получения препарата фактора свертывания viii крови человека |
| WO2009007451A1 (en) * | 2007-07-11 | 2009-01-15 | Novo Nordisk A/S | Purification of factor viii using a mixed-mode or multimodal resin |
-
2009
- 2009-06-24 CN CN200980123974.6A patent/CN102066417B/zh active Active
- 2009-06-24 WO PCT/EP2009/057883 patent/WO2009156430A1/en not_active Ceased
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- 2010-12-21 ZA ZA2010/09162A patent/ZA201009162B/en unknown
-
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- 2013-11-24 IL IL229583A patent/IL229583A0/en unknown
Patent Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US8022187B2 (en) * | 2007-02-01 | 2011-09-20 | Baxter International Inc. | FVIII-independent FIX-mutant proteins for hemophilia A treatment |
| EP2486936A1 (en) * | 2007-06-13 | 2012-08-15 | CSL Behring GmbH | A composition comprising VWF and FVIII preparations for use in treating of bleeding disorders |
| UA101003C2 (uk) * | 2007-12-04 | 2013-02-25 | Эпитоп Интернешнл Нв | Пептид фактора fviii та його застосування для індукції толерантності у хворих гемофілією |
| EA019370B1 (ru) * | 2007-12-04 | 2014-03-31 | Эпитоп Интернэшнл Нв | Пептиды fviii и их применение для индукции толерантности у больных гемофилией |
| RU2563236C2 (ru) * | 2008-07-10 | 2015-09-20 | Цсл Беринг Гмбх | Фактор фон виллебранда или фактор viii и фактор фон виллебранда для лечения коагулопатии, индуцированной ингибиторами тромбоцитов |
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