CN107080842A - 抗体制剂 - Google Patents
抗体制剂 Download PDFInfo
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- CN107080842A CN107080842A CN201611045494.0A CN201611045494A CN107080842A CN 107080842 A CN107080842 A CN 107080842A CN 201611045494 A CN201611045494 A CN 201611045494A CN 107080842 A CN107080842 A CN 107080842A
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Classifications
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- C07K16/12—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria
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- C—CHEMISTRY; METALLURGY
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- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/12—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria
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- C07K16/1228—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-negative bacteria from Enterobacteriaceae (F), e.g. Citrobacter, Serratia, Proteus, Providencia, Morganella, Yersinia
- C07K16/1232—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-negative bacteria from Enterobacteriaceae (F), e.g. Citrobacter, Serratia, Proteus, Providencia, Morganella, Yersinia from Escherichia (G)
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- C07K16/12—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria
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- C07K16/125—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-negative bacteria from Chlamydiales (O)
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
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- C07K16/12—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
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- C—CHEMISTRY; METALLURGY
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- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/22—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against growth factors ; against growth regulators
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
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- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/14—Extraction; Separation; Purification
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- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
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- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
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Landscapes
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| GBGB1006753.6A GB201006753D0 (en) | 2010-04-22 | 2010-04-22 | Process for preparing an immunolobulin composition |
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| CN201611045494.0A Pending CN107080842A (zh) | 2010-04-22 | 2011-04-21 | 抗体制剂 |
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| CN201180029338.4A Active CN102939111B (zh) | 2010-04-22 | 2011-04-21 | 制备免疫球蛋白组合物的方法 |
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| GB201006753D0 (en) | 2010-04-22 | 2010-06-09 | Biotest Ag | Process for preparing an immunolobulin composition |
| FR2959821B1 (fr) * | 2010-05-05 | 2012-07-06 | Lab Francais Du Fractionnement | Procede de mesure de l'activation du complement par des igg |
| FR2974301B1 (fr) | 2011-04-20 | 2013-08-23 | Lab Francais Du Fractionnement | Procede de preparation d'un produit plasmatique deplete en un ou plusieurs facteurs thrombogenes |
| FR2977893B1 (fr) * | 2011-07-11 | 2015-02-20 | Lab Francais Du Fractionnement | Procede de preparation d'un concentre d'immunoglobulines polyvalentes |
| EP2636684A1 (en) | 2012-03-09 | 2013-09-11 | CSL Behring AG | Prevention of infection |
| WO2013132052A1 (en) | 2012-03-09 | 2013-09-12 | Csl Behring Ag | Compositions comprising secretory - like immunoglobulins |
| EP2636681A1 (en) | 2012-03-09 | 2013-09-11 | CSL Behring AG | Process for enriching IgA |
| KR20150115639A (ko) * | 2014-04-04 | 2015-10-14 | 전숙영 | 치료용 면역글로불린 제제 제조에 사용되는 산성 완충액, 이를 이용한 치료용 면역글로불린 제제 제조방법 및 이 제조방법으로 제조된 치료용 면역글로불린 제제 |
| US20170210793A1 (en) * | 2014-07-15 | 2017-07-27 | The Regents Of The University Of California | Novel Treatment for Polycystic Kidney Disease |
| DK3334747T5 (da) | 2015-08-13 | 2024-10-07 | Amgen Inc | Ladet dybdefiltrering af antigenbindende proteiner |
| CN108778333A (zh) | 2016-03-14 | 2018-11-09 | 生物测试股份公司 | 严重社区获得性肺炎的治疗 |
| EP3275897A1 (en) | 2016-07-27 | 2018-01-31 | Biotest AG | Process for preparing immunoglobulin compositions |
| RU2660584C1 (ru) * | 2017-06-06 | 2018-07-06 | Федеральное государственное бюджетное учреждение науки "Кировский научно-исследовательский институт гематологии и переливания крови Федерального медико-биологического агентства" | Способ определения FC-функции препаратов иммуноглобулина человека |
| EP4528277A3 (en) * | 2017-11-29 | 2025-06-18 | F. Hoffmann-La Roche AG | Target interference suppressed anti-drug antibody assay |
| EP3747903A1 (en) | 2019-06-07 | 2020-12-09 | Biotest AG | Method and kit for testing potency of immunoglobulin compositions |
| AU2021251423A1 (en) * | 2020-04-10 | 2022-10-27 | Vanudis GmbH | Natural antibodies in prophylaxis and therapy |
| CN115697408A (zh) * | 2020-06-03 | 2023-02-03 | 基立福环球运营有限公司 | 超免疫igg和/或igm组合物及其制备方法及自捐献者获得超免疫人血浆的方法 |
| CN115768789A (zh) * | 2020-07-10 | 2023-03-07 | 基立福环球运营有限公司 | 用于获得包含人血浆来源的免疫球蛋白m的组合物的方法 |
| CN111944043B (zh) * | 2020-09-01 | 2023-05-09 | 华兰生物工程重庆有限公司 | 一种从血浆废弃物中提取IgM的方法 |
| US20230400453A1 (en) | 2020-11-19 | 2023-12-14 | Biotest Ag | Method and Kit for Testing Immunomodulatory Potency of Immunoglobulin Compositions for Treatment of COVID-19 |
| CA3223881A1 (en) | 2021-07-29 | 2023-02-02 | Roopsee ANAND | Method of purifying immunoglobulin g and uses thereof |
| WO2024200757A1 (en) | 2023-03-29 | 2024-10-03 | Csl Behring Ag | Methods of identifying immunoglobulin associated with adverse reactions |
| WO2025008781A1 (en) | 2023-07-04 | 2025-01-09 | Csl Behring Ag | Method of purification |
| WO2025229607A1 (en) | 2024-05-03 | 2025-11-06 | Csl Behring Ag | Systems and methods for solid-liquid separation |
Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0123029B1 (de) * | 1983-03-21 | 1987-07-29 | Heilmittelwerke Wien Gesellschaft m.b.H. | Verfahren zur Herstellung einer nebenwirkungsfreien IgG-Immunglobulinlösung für die intravenöse Applikation |
| EP0450412A1 (en) * | 1990-04-03 | 1991-10-09 | Bayer Corporation | Heat-treated IgM antibody preparations |
| CN1233258A (zh) * | 1996-10-14 | 1999-10-27 | 瑞士红十字会创立血液捐赠服务中央实验室 | 用于制备静脉内给药的lgM制剂的方法 |
| CN1311797A (zh) * | 1998-06-09 | 2001-09-05 | 斯塔滕斯血清研究所 | 生产用于静脉给药的免疫球蛋白和其他免疫球蛋白产品的方法 |
Family Cites Families (40)
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|---|---|---|---|---|
| US136556A (en) | 1873-03-04 | Improvements in button-fastenings | ||
| DE2901822A1 (de) * | 1979-01-18 | 1980-07-31 | Biotest Serum Institut Gmbh | Verfahren zur herstellung einer fuer die intravenoese applikation geeigneten immunglobulinloesung, die igm in ankonzentrierter form enthaelt |
| US4371520A (en) * | 1981-10-28 | 1983-02-01 | The Green Cross Corporation | Process for preparing immunoglobulin suitable for intravenous injection |
| IL90281A (en) | 1988-06-06 | 1994-10-07 | Miles Inc | Preparations containing MGI antibodies |
| DE3825429C2 (de) * | 1988-07-27 | 1994-02-10 | Biotest Pharma Gmbh | Verfahren zur Herstellung eines intravenös verabreichbaren polyklonalen Immunglobulin-Präparates mit hohem IgM-Gehalt |
| US4939176A (en) | 1988-12-20 | 1990-07-03 | Miles Inc. | Viral inactivation process |
| DE3927111C3 (de) * | 1989-08-17 | 1994-09-01 | Biotest Pharma Gmbh | Verfahren zur Herstellung nicht modifizierter intravenös verabreichbarer IgM- und/oderIgA-haltiger Immunglobulinpräparate |
| DE3927112C1 (enExample) | 1989-08-17 | 1990-10-25 | Biotest Pharma Gmbh, 6072 Dreieich, De | |
| US5367054A (en) * | 1993-04-12 | 1994-11-22 | Stolle Research & Development Corp. | Large-scale purification of egg immunoglobulin |
| JPH11509210A (ja) | 1995-07-14 | 1999-08-17 | クロア−ルージュ ド ベルジーク | 血液製剤中の汚染物質を不活性化する方法及び装置 |
| PT764658E (pt) | 1995-09-22 | 2002-06-28 | Zlb Bioplasma Ag | Processo para a obtencao de imunoglobulinas a partir de fraccoes que resultam do fraccionamento do plasma sanguineo humano |
| JP3987599B2 (ja) * | 1996-12-05 | 2007-10-10 | 日本製薬株式会社 | 筋ジストロフィー治療剤 |
| JPH10167894A (ja) * | 1996-12-11 | 1998-06-23 | Mitsubishi Gas Chem Co Inc | ビスマス置換希土類鉄ガーネット単結晶膜の製造法 |
| US6955917B2 (en) * | 1997-06-20 | 2005-10-18 | Bayer Healthcare Llc | Chromatographic method for high yield purification and viral inactivation of antibodies |
| US5886154A (en) | 1997-06-20 | 1999-03-23 | Lebing; Wytold R. | Chromatographic method for high yield purification and viral inactivation of antibodies |
| RU2178309C2 (ru) * | 2000-01-12 | 2002-01-20 | Российский научно-исследовательский институт геронтологии | Антитимоцитарный глобулин для внутривенного введения и способ его получения |
| RU2192279C2 (ru) * | 2000-09-07 | 2002-11-10 | Нижегородское государственное предприятие по производству бактерийных препаратов | Способ получения иммуноглобулинового препарата |
| DK1337280T3 (da) | 2000-11-13 | 2013-12-02 | Bayer Ip Gmbh | Fremgangsmåde til inaktivering af mikroorganismer i en fluid ved anvendelse af ultraviolet stråling |
| FR2824568B1 (fr) | 2001-05-11 | 2004-04-09 | Lab Francais Du Fractionnement | Procede de preparation de concentres d'immunoglobulines humaines a usage therapeutique |
| US7727974B2 (en) | 2001-08-10 | 2010-06-01 | Eisai R & D Management Co., Ltd. | Methods of reducing the severity of mucositis |
| WO2003037504A1 (en) | 2001-11-02 | 2003-05-08 | Japan Techno Co., Ltd. | Vibratory stirrer for sterilization and sterilizer and sterilization method employing vibratory stirrer |
| RU2255766C2 (ru) * | 2003-03-05 | 2005-07-10 | Государственное учреждение "Московский научно-исследовательский институт эпидемиологии и микробиологии им. Г.Н. Габрического Министерства здравоохранения Российской Федерации" | Способ получения иммуноглобулинового препарата для профилактики и терапии бактериальных и вирусных инфекций, иммуноглобулиновый препарат для профилактики и терапии бактериальных и вирусных инфекций (варианты) и суппозитории на основе иммуноглобулинового препарата |
| CA2520381A1 (en) | 2003-03-26 | 2004-10-14 | Sudhir Paul | Proteolytic and covalent antibodies |
| EP1678208B1 (en) | 2003-10-27 | 2013-05-15 | Wyeth LLC | Removal of high molecular weight aggregates using hydroxyapatite chromatography |
| EP1532983A1 (en) | 2003-11-18 | 2005-05-25 | ZLB Bioplasma AG | Immunoglobulin preparations having increased stability |
| JP2008500959A (ja) | 2004-01-30 | 2008-01-17 | スオメン プナイネン リスティ ヴェリパルヴェル | ウイルスについて安全な免疫グロブリンの製造方法 |
| EP1718675B2 (en) | 2004-02-27 | 2017-01-25 | Octapharma AG | A method of providing a purified, virus safe antibody preparation |
| PL1830881T3 (pl) | 2004-12-10 | 2010-11-30 | Novimmune Sa | Terapie skojarzone celowane na wiele receptorów Toll-podobnych i ich zastosowanie |
| WO2006064373A2 (en) | 2004-12-16 | 2006-06-22 | Genzyme Polyclonals S.A.S. | Methods of purifying immunologlobulins |
| KR101157174B1 (ko) | 2005-11-24 | 2012-06-20 | 삼성전자주식회사 | 세포 또는 바이러스의 신속한 파괴 방법 및 장치 |
| DE102005062634A1 (de) | 2005-12-23 | 2007-06-28 | Blutspendedienst der Landesverbände des Deutschen Roten Kreuzes Niedersachsen, Sachsen-Anhalt, Thüringen, Oldenburg und Bremen gGmbH | Verfahren zur Inaktivierung von Pathogenen in Spenderblut, Blutplasma oder Erythrozytenkonzentraten in flexiblen Behältnissen unter Bewegung |
| FR2899111B1 (fr) | 2006-03-31 | 2010-09-03 | Lab Francais Du Fractionnement | Concentre d'immunoglobulines specifiques du chikungunya en tant que medicament. |
| FR2899112B1 (fr) * | 2006-03-31 | 2010-09-03 | Lab Francais Du Fractionnement | Concentre d'immunoglobulines et de fragments f (ab)'2 et/ou fab specifiques d'un arbovirus en tant que medicament. |
| US8354076B2 (en) | 2006-10-02 | 2013-01-15 | Palo Alto Research Center Incorporated | Fluid stirring mechanism |
| EP1950225A1 (de) | 2007-01-25 | 2008-07-30 | Octapharma AG | Verfahren zur Steigerung von Proteinausbeuten |
| CN102089005A (zh) | 2008-05-12 | 2011-06-08 | 斯特罗克斯生物制药有限责任公司 | 金黄色葡萄球菌特异性抗体制剂 |
| RU2457863C2 (ru) * | 2008-08-05 | 2012-08-10 | Виктор Владимирович Чалов | Композиция, обладающая противовирусным и антимикробным действием, содержащая консорциум иммуноглобулинов |
| RU2457861C2 (ru) * | 2008-08-05 | 2012-08-10 | Виктор Владимирович Чалов | Композиция, обладающая противовирусным и антимикробным действием, содержащая консорциум иммуноглобулинов |
| GB201006753D0 (en) | 2010-04-22 | 2010-06-09 | Biotest Ag | Process for preparing an immunolobulin composition |
| NZ591514A (en) | 2011-03-03 | 2013-11-29 | Kode Biotech Ltd | Assay method |
-
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Patent Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0123029B1 (de) * | 1983-03-21 | 1987-07-29 | Heilmittelwerke Wien Gesellschaft m.b.H. | Verfahren zur Herstellung einer nebenwirkungsfreien IgG-Immunglobulinlösung für die intravenöse Applikation |
| EP0450412A1 (en) * | 1990-04-03 | 1991-10-09 | Bayer Corporation | Heat-treated IgM antibody preparations |
| CN1233258A (zh) * | 1996-10-14 | 1999-10-27 | 瑞士红十字会创立血液捐赠服务中央实验室 | 用于制备静脉内给药的lgM制剂的方法 |
| CN1311797A (zh) * | 1998-06-09 | 2001-09-05 | 斯塔滕斯血清研究所 | 生产用于静脉给药的免疫球蛋白和其他免疫球蛋白产品的方法 |
Non-Patent Citations (1)
| Title |
|---|
| 郭中平等: "影响静注免疫球蛋白抗补体活性分析"", 《中国生物制品学杂志》 * |
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