JP2006517415A - ポリペプチドの精製 - Google Patents
ポリペプチドの精製 Download PDFInfo
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- JP2006517415A JP2006517415A JP2006508590A JP2006508590A JP2006517415A JP 2006517415 A JP2006517415 A JP 2006517415A JP 2006508590 A JP2006508590 A JP 2006508590A JP 2006508590 A JP2006508590 A JP 2006508590A JP 2006517415 A JP2006517415 A JP 2006517415A
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- C12P21/00—Preparation of peptides or proteins
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| CN114774500A (zh) * | 2022-04-26 | 2022-07-22 | 成都蜀星饲料有限公司 | 多肽及制备方法、有机复合微量元素及制备方法 |
| US12269875B2 (en) | 2023-08-03 | 2025-04-08 | Jeff R. Peterson | Gout flare prevention methods using IL-1BETA blockers |
Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS5515444B1 (enExample) * | 1969-04-01 | 1980-04-23 |
Family Cites Families (22)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US3607857A (en) * | 1970-03-03 | 1971-09-21 | Upjohn Co | Process of removing acrinol from gamma globulin using siliceous material such as silica gel |
| US3903254A (en) * | 1971-07-23 | 1975-09-02 | Upjohn Co | Separation of erythrocyte stroma from lysing medium and hemoglobin with acrinol |
| DE2308013A1 (de) * | 1973-02-17 | 1974-09-12 | Behringwerke Ag | Katalasearme glucoseoxidase und verfahren zu ihrer gewinnung |
| JPS519035B2 (enExample) | 1973-10-31 | 1976-03-23 | ||
| SU944580A1 (ru) | 1980-02-07 | 1982-07-23 | Кировский научно-исследовательский институт переливания крови | Способ получени поверхностного антигена гепатита В |
| US4563303A (en) * | 1984-04-14 | 1986-01-07 | Judicial Foundation The Chemosero-Therapeutic Research Institute | Method for purification of filamentous hemagglutinin |
| JPS60258127A (ja) | 1984-06-04 | 1985-12-20 | Green Cross Corp:The | B型肝炎ワクチンの製造方法 |
| WO1986007093A1 (fr) | 1985-05-29 | 1986-12-04 | The Green Cross Corporation | Procede de preparation d'une proteine heterogene |
| DE3581412D1 (de) | 1985-07-16 | 1991-02-21 | Green Cross Corp | Verfahren zur herstellung von heteroproteinen. |
| DE3604947A1 (de) | 1986-02-17 | 1987-08-20 | Biotest Pharma Gmbh | Verfahren zur herstellung eines immunglobulinhaltigen praeparates und dessen verwendung zur prophylaxe und therapie von aids |
| FR2600078B1 (fr) | 1986-06-12 | 1989-07-13 | Merieux Inst | Procede de preparation de facteur xiii a partir du placenta |
| DE3929504A1 (de) | 1989-09-06 | 1991-03-07 | Behringwerke Ag | Verfahren zur reinigung von plasminogen-aktivator-inhibitor 2 (pai-2) |
| DE4030264A1 (de) * | 1990-09-25 | 1992-04-23 | Hoechst Ag | Verfahren zur herstellung gereinigter glycolipide durch membrantrennverfahren |
| GB9215540D0 (en) | 1992-07-22 | 1992-09-02 | Celltech Ltd | Protein expression system |
| US5861263A (en) * | 1992-10-20 | 1999-01-19 | Universidad Autonoma De Nuevo Leon | Preparation of preserved entamoeba histolytica antigens without enzymatic inhibitors and their use in immunological methods |
| US5641870A (en) | 1995-04-20 | 1997-06-24 | Genentech, Inc. | Low pH hydrophobic interaction chromatography for antibody purification |
| US5760189A (en) | 1995-06-02 | 1998-06-02 | Genetics Institute, Inc. | Protein recovery & purification methods |
| US5714583A (en) | 1995-06-07 | 1998-02-03 | Genetics Institute, Inc. | Factor IX purification methods |
| ES2287976T3 (es) | 1997-06-13 | 2007-12-16 | Genentech, Inc. | Recuperacion de proteinas mediante cromatografia seguida de filtracion sobre una capa cargada. |
| JPH11341947A (ja) * | 1998-06-02 | 1999-12-14 | Yakult Honsha Co Ltd | 発酵管理方法 |
| US6156514A (en) * | 1998-12-03 | 2000-12-05 | Sunol Molecular Corporation | Methods for making recombinant cells |
| WO2001053335A2 (en) * | 2000-01-20 | 2001-07-26 | Regents Of The University Of Minnesota | Peptides with antibacterial activity |
-
2004
- 2004-01-08 DE DE602004006831T patent/DE602004006831T2/de not_active Expired - Lifetime
- 2004-01-08 DK DK04700878T patent/DK1581644T3/da active
- 2004-01-08 CA CA002511946A patent/CA2511946A1/en not_active Abandoned
- 2004-01-08 US US10/754,212 patent/US7169908B2/en not_active Expired - Fee Related
- 2004-01-08 EP EP04700878A patent/EP1581644B1/en not_active Expired - Lifetime
- 2004-01-08 NZ NZ540895A patent/NZ540895A/en not_active IP Right Cessation
- 2004-01-08 KR KR1020057012831A patent/KR20050095605A/ko not_active Ceased
- 2004-01-08 RU RU2005125210/13A patent/RU2337968C2/ru not_active IP Right Cessation
- 2004-01-08 WO PCT/US2004/000499 patent/WO2004092393A1/en not_active Ceased
- 2004-01-08 ZA ZA200504990A patent/ZA200504990B/en unknown
- 2004-01-08 AT AT04700878T patent/ATE364092T1/de active
- 2004-01-08 BR BR0406470-4A patent/BRPI0406470A/pt not_active Application Discontinuation
- 2004-01-08 MX MXPA05007378A patent/MXPA05007378A/es active IP Right Grant
- 2004-01-08 CN CNB2004800063965A patent/CN100467611C/zh not_active Expired - Fee Related
- 2004-01-08 PL PL377653A patent/PL377653A1/pl not_active Application Discontinuation
- 2004-01-08 JP JP2006508590A patent/JP2006517415A/ja not_active Withdrawn
- 2004-01-08 ES ES04700878T patent/ES2287687T3/es not_active Expired - Lifetime
- 2004-01-08 AU AU2004230670A patent/AU2004230670B2/en not_active Expired - Fee Related
-
2006
- 2006-12-12 US US11/609,529 patent/US7579448B2/en not_active Expired - Fee Related
Patent Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS5515444B1 (enExample) * | 1969-04-01 | 1980-04-23 |
Cited By (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2012504586A (ja) * | 2008-10-06 | 2012-02-23 | フジフィルム・ダイオシンス・バイオテクノロジーズ ・ユーケイ・リミテッド | 断片抗体のための精製方法 |
| JP2015525213A (ja) * | 2012-05-31 | 2015-09-03 | エイジェンシー フォー サイエンス,テクノロジー アンド リサーチ | タンパク質製剤中の凝集物含量を低減するために混合型多官能表面を使用する方法 |
| US9920125B2 (en) | 2012-05-31 | 2018-03-20 | Agency For Science, Technology And Research | Methods for use of mixed multifunctional surfaces for reducing aggregate content in protein preparations |
| JP2016506953A (ja) * | 2013-02-06 | 2016-03-07 | エイジェンシー・フォー・サイエンス,テクノロジー・アンド・リサーチ | タンパク質精製方法 |
| JP2016507588A (ja) * | 2013-02-26 | 2016-03-10 | エイジェンシー・フォー・サイエンス,テクノロジー・アンド・リサーチ | 非イオン性有機ポリマーおよび電気陽性表面の存在下でのタンパク質精製 |
| US10112971B2 (en) | 2013-02-26 | 2018-10-30 | Agency For Science, Technology And Research | Protein purification in the presence of nonionic organic polymers and electropositive surfaces |
| JP2016509069A (ja) * | 2013-02-28 | 2016-03-24 | エイジェンシー・フォー・サイエンス,テクノロジー・アンド・リサーチ | 非イオン性有機ポリマー存在下、高導電率でのタンパク質精製 |
| JP2016509068A (ja) * | 2013-02-28 | 2016-03-24 | エイジェンシー・フォー・サイエンス,テクノロジー・アンド・リサーチ | クロマチン欠損細胞培養採取物からの抗体のクロマトグラフィー精製 |
| US10253063B2 (en) | 2013-02-28 | 2019-04-09 | Agency For Science, Technology And Research | Protein purification in the presence of nonionic organic polymers at elevated conductivity |
Also Published As
| Publication number | Publication date |
|---|---|
| EP1581644B1 (en) | 2007-06-06 |
| DE602004006831D1 (de) | 2007-07-19 |
| CN100467611C (zh) | 2009-03-11 |
| CN1759186A (zh) | 2006-04-12 |
| DK1581644T3 (da) | 2007-10-08 |
| AU2004230670B2 (en) | 2010-11-25 |
| RU2337968C2 (ru) | 2008-11-10 |
| NZ540895A (en) | 2007-03-30 |
| KR20050095605A (ko) | 2005-09-29 |
| AU2004230670A1 (en) | 2004-10-28 |
| US7169908B2 (en) | 2007-01-30 |
| ZA200504990B (en) | 2006-08-30 |
| DE602004006831T2 (de) | 2008-02-14 |
| CA2511946A1 (en) | 2004-10-28 |
| WO2004092393A1 (en) | 2004-10-28 |
| US7579448B2 (en) | 2009-08-25 |
| ATE364092T1 (de) | 2007-06-15 |
| MXPA05007378A (es) | 2005-11-23 |
| PL377653A1 (pl) | 2006-02-06 |
| ES2287687T3 (es) | 2007-12-16 |
| RU2005125210A (ru) | 2006-01-10 |
| US20050037456A1 (en) | 2005-02-17 |
| BRPI0406470A (pt) | 2005-12-06 |
| US20070077625A1 (en) | 2007-04-05 |
| EP1581644A1 (en) | 2005-10-05 |
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