JP4050329B2 - プロリルピペプチジルアミノペプチダーゼ活性を有するポリペプチド及びそれをコードする核酸 - Google Patents
プロリルピペプチジルアミノペプチダーゼ活性を有するポリペプチド及びそれをコードする核酸 Download PDFInfo
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| US85788497A | 1997-05-16 | 1997-05-16 | |
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| US6289297P | 1997-10-20 | 1997-10-20 | |
| US60/062,892 | 1997-10-20 | ||
| PCT/US1998/009629 WO1998051803A1 (en) | 1997-05-16 | 1998-05-12 | Polypeptides having prolyl pipeptidyl aminopeptidase activity and nucleic acids encoding same |
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| JP2002511746A JP2002511746A (ja) | 2002-04-16 |
| JP2002511746A5 JP2002511746A5 (enExample) | 2005-12-08 |
| JP4050329B2 true JP4050329B2 (ja) | 2008-02-20 |
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Families Citing this family (30)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP3727780B2 (ja) * | 1998-06-12 | 2005-12-14 | キッコーマン株式会社 | ロイシンアミノペプチダーゼ遺伝子、組み換え体dna及びロイシンアミノペプチダーゼの製造法 |
| BR0207889A (pt) | 2001-03-19 | 2004-07-27 | Ajinomoto Kk | Proteìna, molécula de ácido nucleico codificando a mesma, molécula de ácido nucleico recombinante, hospedeiro de microorganismo transformado, processo para produzir uma aminopeptidase, e , aminopeptidase |
| US7186540B2 (en) * | 2001-12-27 | 2007-03-06 | National Institute of Advanced Indusrtial Science and Technology | Thermostable glutaminase and thermostable glutaminase gene |
| WO2003102195A1 (en) * | 2002-06-04 | 2003-12-11 | Dsm Ip Assets B.V. | Protein hydrolysate rich in tripeptides |
| JP4300289B2 (ja) * | 2002-08-27 | 2009-07-22 | 国立大学法人 岡山大学 | 加水分解又は脱水縮合酵素、及び当該酵素の生産方法、並びに当該酵素を用いたアミドの合成方法 |
| US20040242566A1 (en) | 2003-03-25 | 2004-12-02 | Syrrx, Inc. | Dipeptidyl peptidase inhibitors |
| JP2007511467A (ja) | 2003-05-14 | 2007-05-10 | タケダ サン ディエゴ インコーポレイテッド | ジペプチジルペプチダーゼインヒビター |
| UA89616C2 (ru) * | 2003-08-01 | 2010-02-25 | Калпис Ко., Лтд. | Гидролизат казеина, способ его получения и применения |
| US7678909B1 (en) | 2003-08-13 | 2010-03-16 | Takeda Pharmaceutical Company Limited | Dipeptidyl peptidase inhibitors |
| MXPA06001601A (es) | 2003-08-13 | 2006-08-25 | Takeda Pharmaceutical | Derivados de 4-pirimidona y su uso como inhibidores de dipeptidilpeptidasa. |
| US7169926B1 (en) | 2003-08-13 | 2007-01-30 | Takeda Pharmaceutical Company Limited | Dipeptidyl peptidase inhibitors |
| WO2005026148A1 (en) | 2003-09-08 | 2005-03-24 | Takeda San Diego, Inc. | Dipeptidyl peptidase inhibitors |
| US7732446B1 (en) | 2004-03-11 | 2010-06-08 | Takeda Pharmaceutical Company Limited | Dipeptidyl peptidase inhibitors |
| CN102127057A (zh) | 2004-03-15 | 2011-07-20 | 武田药品工业株式会社 | 二肽基肽酶抑制剂 |
| WO2005118555A1 (en) | 2004-06-04 | 2005-12-15 | Takeda Pharmaceutical Company Limited | Dipeptidyl peptidase inhibitors |
| WO2006019965A2 (en) | 2004-07-16 | 2006-02-23 | Takeda San Diego, Inc. | Dipeptidyl peptidase inhibitors |
| EP1828192B1 (en) | 2004-12-21 | 2014-12-03 | Takeda Pharmaceutical Company Limited | Dipeptidyl peptidase inhibitors |
| SI1942898T2 (sl) | 2005-09-14 | 2014-08-29 | Takeda Pharmaceutical Company Limited | Dipeptidil-peptidazni inhibitorji za zdravljenje diabetesa |
| EP1924567B1 (en) | 2005-09-16 | 2012-08-22 | Takeda Pharmaceutical Company Limited | Process for the preparation of pyrimidinedione derivatives |
| WO2007112347A1 (en) | 2006-03-28 | 2007-10-04 | Takeda Pharmaceutical Company Limited | Dipeptidyl peptidase inhibitors |
| US8324383B2 (en) | 2006-09-13 | 2012-12-04 | Takeda Pharmaceutical Company Limited | Methods of making polymorphs of benzoate salt of 2-[[6-[(3R)-3-amino-1-piperidinyl]-3,4-dihydro-3-methyl-2,4-dioxo-1(2H)-pyrimidinyl]methyl]-benzonitrile |
| TW200838536A (en) | 2006-11-29 | 2008-10-01 | Takeda Pharmaceutical | Polymorphs of succinate salt of 2-[6-(3-amino-piperidin-1-yl)-3-methyl-2,4-dioxo-3,4-dihydro-2H-pyrimidin-1-ylmethy]-4-fluor-benzonitrile and methods of use therefor |
| US8093236B2 (en) | 2007-03-13 | 2012-01-10 | Takeda Pharmaceuticals Company Limited | Weekly administration of dipeptidyl peptidase inhibitors |
| US9493759B2 (en) | 2008-12-12 | 2016-11-15 | Novozymes, Inc. | Polypeptides having aspartic endopeptidase activity and polynucleotides encoding same |
| CN102333788A (zh) * | 2009-02-19 | 2012-01-25 | 诺沃—诺迪斯克有限公司 | 因子viii的修饰 |
| JP5759132B2 (ja) * | 2010-09-21 | 2015-08-05 | 月桂冠株式会社 | 糸状菌ペプチダーゼの生産方法 |
| WO2013092731A1 (en) * | 2011-12-21 | 2013-06-27 | Dsm Ip Assets B.V. | Method for making a dough with a glutamyl endopeptidase |
| CN103695361B (zh) * | 2013-12-06 | 2015-11-11 | 江南大学 | 一种生产脯氨酸氨肽酶的基因工程菌及其构建方法 |
| GB201705750D0 (en) * | 2017-04-10 | 2017-05-24 | Univ Oxford Innovation Ltd | Peptide ligase and use therof |
| EP4273249A3 (en) * | 2023-07-07 | 2024-05-22 | Novozymes A/S | Improved expression of recombinant proteins |
Family Cites Families (24)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US3857967A (en) | 1971-05-10 | 1974-12-31 | Kikkoman Shoyu Co Ltd | Preparation of food and beverages with peptidoglutaminase |
| US4288627A (en) | 1980-02-12 | 1981-09-08 | Phillips Petroleum Company | Oxidation of thiols employing cobalt molybdate/triethylamine catalyst |
| JPS61279528A (ja) | 1985-06-05 | 1986-12-10 | Hokkai Can Co Ltd | 容器の製造方法 |
| DK122686D0 (da) | 1986-03-17 | 1986-03-17 | Novo Industri As | Fremstilling af proteiner |
| JPH0665280B2 (ja) | 1987-03-04 | 1994-08-24 | 味の素株式会社 | タンパクゲル化剤及びそれを用いるタンパクのゲル化方法 |
| JPS6450382A (en) | 1987-08-20 | 1989-02-27 | Hitachi Heating Appl | Plane-form heating body |
| DE68924654T2 (de) | 1988-01-07 | 1996-04-04 | Novonordisk As | Spezifische Protease. |
| NL194258C (nl) * | 1989-09-01 | 2001-11-05 | Protein Technologies Internat | Werkwijze voor het behandelen van een eiwithoudend materiaal. |
| US5866357A (en) | 1990-03-09 | 1999-02-02 | Novo Nordisk A/S | Method for hydrolyzing proteins with gluyasp specific protease |
| WO1991017243A1 (en) | 1990-05-09 | 1991-11-14 | Novo Nordisk A/S | A cellulase preparation comprising an endoglucanase enzyme |
| US5641670A (en) | 1991-11-05 | 1997-06-24 | Transkaryotic Therapies, Inc. | Protein production and protein delivery |
| DE69333718T2 (de) | 1992-01-14 | 2005-12-01 | Ajinomoto Co., Inc. | Gen, das für eine Fisch-Transglutaminase kodiert |
| CA2128032A1 (en) | 1992-01-22 | 1993-08-05 | Birger R. Jensen | Activated factor xiii |
| CN1057127C (zh) * | 1993-04-23 | 2000-10-04 | 北京大学 | 固定化复合外肽酶蛋白质全水解及脱苦方法 |
| DK46793D0 (da) | 1993-04-26 | 1993-04-26 | Novo Nordisk As | Enzym |
| DK52293D0 (enExample) | 1993-05-05 | 1993-05-05 | Novo Nordisk As | |
| DK52393D0 (enExample) | 1993-05-05 | 1993-05-05 | Novo Nordisk As | |
| JPH07115969A (ja) * | 1993-10-25 | 1995-05-09 | Asahi Chem Ind Co Ltd | 加水分解蛋白質の製造方法 |
| CN1192108C (zh) | 1994-06-03 | 2005-03-09 | 诺沃奇梅兹生物技术有限公司 | 纯化的毁丝霉属漆酶及编码该酶的核酸 |
| WO1996000787A1 (en) | 1994-06-30 | 1996-01-11 | Novo Nordisk Biotech, Inc. | Non-toxic, non-toxigenic, non-pathogenic fusarium expression system and promoters and terminators for use therein |
| JP3720363B2 (ja) | 1994-08-26 | 2005-11-24 | ノボザイムス アクティーゼルスカブ | 微生物のトランスグルタミナーゼ、それらの産生及び使用 |
| ATE248219T1 (de) | 1995-01-19 | 2003-09-15 | Novozymes As | Transglutaminasen aus oomyzeten |
| ATE268379T1 (de) | 1995-03-16 | 2004-06-15 | Novozymes As | Enzym mit aminopeptidaseactivität |
| CN1099839C (zh) * | 1996-05-20 | 2003-01-29 | 诺沃奇梅兹有限公司 | 一种获得蛋白质水解物的方法 |
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1998
- 1998-05-12 EP EP98921134A patent/EP0981630B1/en not_active Expired - Lifetime
- 1998-05-12 DK DK98921134T patent/DK0981630T3/da active
- 1998-05-12 AT AT98921134T patent/ATE414775T1/de not_active IP Right Cessation
- 1998-05-12 AU AU73810/98A patent/AU7381098A/en not_active Abandoned
- 1998-05-12 JP JP54941398A patent/JP4050329B2/ja not_active Expired - Fee Related
- 1998-05-12 WO PCT/US1998/009629 patent/WO1998051803A1/en not_active Ceased
- 1998-05-12 DE DE69840230T patent/DE69840230D1/de not_active Expired - Lifetime
- 1998-05-12 CN CNB988051753A patent/CN1227363C/zh not_active Expired - Fee Related
- 1998-05-15 US US09/079,592 patent/US6664092B1/en not_active Expired - Fee Related
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Also Published As
| Publication number | Publication date |
|---|---|
| EP0981630A1 (en) | 2000-03-01 |
| DE69840230D1 (de) | 2009-01-02 |
| EP0981630B1 (en) | 2008-11-19 |
| US6664092B1 (en) | 2003-12-16 |
| CN1268976A (zh) | 2000-10-04 |
| AU7381098A (en) | 1998-12-08 |
| JP2002511746A (ja) | 2002-04-16 |
| CN1227363C (zh) | 2005-11-16 |
| WO1998051803A1 (en) | 1998-11-19 |
| US7098001B2 (en) | 2006-08-29 |
| DK0981630T3 (da) | 2009-03-09 |
| US20040171104A1 (en) | 2004-09-02 |
| ATE414775T1 (de) | 2008-12-15 |
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