HU228916B1 - Polyethylen-glycol/carbamate oxydase conjugates and pharmaceutical compositions containing thereof - Google Patents
Polyethylen-glycol/carbamate oxydase conjugates and pharmaceutical compositions containing thereof Download PDFInfo
- Publication number
- HU228916B1 HU228916B1 HU0800112A HUP0800112A HU228916B1 HU 228916 B1 HU228916 B1 HU 228916B1 HU 0800112 A HU0800112 A HU 0800112A HU P0800112 A HUP0800112 A HU P0800112A HU 228916 B1 HU228916 B1 HU 228916B1
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- Hungary
- Prior art keywords
- uricase
- peg
- activity
- conjugates
- lys
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- C12N11/08—Enzymes or microbial cells immobilised on or in an organic carrier the carrier being a synthetic polymer
- C12N11/089—Enzymes or microbial cells immobilised on or in an organic carrier the carrier being a synthetic polymer obtained otherwise than by reactions only involving carbon-to-carbon unsaturated bonds
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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
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/0004—Oxidoreductases (1.)
- C12N9/0012—Oxidoreductases (1.) acting on nitrogen containing compounds as donors (1.4, 1.5, 1.6, 1.7)
- C12N9/0044—Oxidoreductases (1.) acting on nitrogen containing compounds as donors (1.4, 1.5, 1.6, 1.7) acting on other nitrogen compounds as donors (1.7)
- C12N9/0046—Oxidoreductases (1.) acting on nitrogen containing compounds as donors (1.4, 1.5, 1.6, 1.7) acting on other nitrogen compounds as donors (1.7) with oxygen as acceptor (1.7.3)
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- A61K47/59—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being an organic macromolecular compound, e.g. an oligomeric, polymeric or dendrimeric molecule obtained otherwise than by reactions only involving carbon-to-carbon unsaturated bonds, e.g. polyureas or polyurethanes
- A61K47/60—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being an organic macromolecular compound, e.g. an oligomeric, polymeric or dendrimeric molecule obtained otherwise than by reactions only involving carbon-to-carbon unsaturated bonds, e.g. polyureas or polyurethanes the organic macromolecular compound being a polyoxyalkylene oligomer, polymer or dendrimer, e.g. PEG, PPG, PEO or polyglycerol
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Applications Claiming Priority (2)
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| US13039298A | 1998-08-06 | 1998-08-06 | |
| PCT/US1999/017514 WO2000007629A2 (en) | 1998-08-06 | 1999-08-02 | Peg-urate oxidase conjugates and use thereof |
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| HU228916B1 true HU228916B1 (en) | 2013-06-28 |
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| HU0800112A HU228916B1 (en) | 1998-08-06 | 1999-08-02 | Polyethylen-glycol/carbamate oxydase conjugates and pharmaceutical compositions containing thereof |
| HU0103003A HU226294B1 (en) | 1998-08-06 | 1999-08-02 | Peg-urate oxidase conjugates and use thereof |
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| Application Number | Title | Priority Date | Filing Date |
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| HU0103003A HU226294B1 (en) | 1998-08-06 | 1999-08-02 | Peg-urate oxidase conjugates and use thereof |
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| PT1100880E (pt) | 1998-08-06 | 2011-01-13 | Univ Duke | Urato-oxidase |
| US6783965B1 (en) | 2000-02-10 | 2004-08-31 | Mountain View Pharmaceuticals, Inc. | Aggregate-free urate oxidase for preparation of non-immunogenic polymer conjugates |
| CN1896231B (zh) | 1998-08-06 | 2012-09-05 | 山景药品公司 | 分离四聚体尿酸氧化酶的方法 |
| WO2000007629A2 (en) * | 1998-08-06 | 2000-02-17 | Mountain View Pharmaceuticals, Inc. | Peg-urate oxidase conjugates and use thereof |
| AU2006203252B8 (en) * | 2000-02-10 | 2009-06-18 | Duke University | Aggregate-free urate oxidase for preparation of non-immunogenic polymer conjugates |
| EP1279406A4 (en) | 2000-04-03 | 2007-10-24 | Santen Pharmaceutical Co Ltd | TRANSPORTERS AND DRUG DISPENSING SYSTEMS USING THESE |
| CA2413201A1 (en) * | 2000-06-28 | 2002-01-03 | Merck & Co., Inc. | Treatment for cardiovascular disease |
| DK1421175T3 (da) | 2001-06-28 | 2009-03-23 | Mountain View Pharmaceuticals | Polymerstabiliserede proteinaser |
| US6913915B2 (en) * | 2001-08-02 | 2005-07-05 | Phoenix Pharmacologics, Inc. | PEG-modified uricase |
| US8129330B2 (en) | 2002-09-30 | 2012-03-06 | Mountain View Pharmaceuticals, Inc. | Polymer conjugates with decreased antigenicity, methods of preparation and uses thereof |
| US20040062748A1 (en) | 2002-09-30 | 2004-04-01 | Mountain View Pharmaceuticals, Inc. | Polymer conjugates with decreased antigenicity, methods of preparation and uses thereof |
| WO2004100997A2 (en) | 2003-05-12 | 2004-11-25 | Affymax, Inc. | Spacer moiety for poly(ethylene glycol) -modified peptides |
| KR101227666B1 (ko) | 2003-05-12 | 2013-01-31 | 아피맥스, 인크. | 에리스로포이에틴 수용체에 결합하는 펩티드 |
| EP1765411B2 (en) * | 2004-06-30 | 2017-10-11 | Nektar Therapeutics | Polymer-factor ix moiety conjugates |
| MX2007012548A (es) | 2005-04-11 | 2008-03-11 | Savient Pharmaceuticals Inc | Formas variantes de urato oxidasa y uso de las mismas. |
| US8148123B2 (en) | 2005-04-11 | 2012-04-03 | Savient Pharmaceuticals, Inc. | Methods for lowering elevated uric acid levels using intravenous injections of PEG-uricase |
| EP2947145A1 (en) | 2005-04-11 | 2015-11-25 | Crealta Pharmaceuticals LLC | Variant forms of urate oxidase and use thereof |
| US8841333B2 (en) | 2005-05-09 | 2014-09-23 | Takeda Pharmaceuticals U.S.A., Inc. | Methods for treating nephrolithiasis |
| US7550433B2 (en) | 2005-06-03 | 2009-06-23 | Affymax, Inc. | Erythropoietin receptor peptide formulations and uses |
| PL2013225T3 (pl) | 2006-04-12 | 2015-06-30 | Crealta Pharmaceuticals Llc | Oczyszczanie białek z zastosowaniem kationowego środka powierzchniowo czynnego |
| JP4890132B2 (ja) * | 2006-07-20 | 2012-03-07 | 東洋紡績株式会社 | ウリカーゼの比活性を向上させる方法、および比活性の向上した改変型ウリカーゼ |
| RU2382048C1 (ru) * | 2008-12-25 | 2010-02-20 | Общество С Ограниченной Ответственностью "Фармапарк" | Лекарственное средство на основе модифицированного интерферона альфа с пролонгированным терапевтическим действием |
| US9377454B2 (en) | 2009-06-25 | 2016-06-28 | Crealta Pharmaceuticals Llc | Methods and kits for predicting infusion reaction risk and antibody-mediated loss of response by monitoring serum uric acid during pegylated uricase therapy |
| EP2613780B1 (en) | 2010-09-10 | 2014-11-12 | Takeda Pharmaceuticals U.S.A., Inc. | Methods for concomitant treatment of theophylline and febuxostat |
| CN102634492B (zh) | 2011-02-14 | 2015-06-10 | 重庆富进生物医药有限公司 | 聚乙二醇化犬源尿酸氧化酶类似物及其制备方法和应用 |
| EP2833883A4 (en) | 2012-04-06 | 2015-12-23 | Indus Pharmaceuticals Inc | NOVEL COMPOSITIONS OF COMBINATIONS OF NONCOVALENT DNA BINDER AND CANCER-INHIBITING AND / OR INFLAMMATORY ACTIVE SUBSTANCES AND THEIR USE IN THE TREATMENT OF ILLNESSES |
| MY190411A (en) | 2015-05-15 | 2022-04-21 | Medimmune Llc | Improved uricase sequences and methods of treatment |
| CN105412942B (zh) * | 2015-12-23 | 2019-02-26 | 沈阳三生制药有限责任公司 | 聚乙二醇化的重组产朊假丝酵母尿酸氧化酶冻干注射剂 |
| JP7523909B2 (ja) | 2017-03-11 | 2024-07-29 | セレクタ バイオサイエンシーズ インコーポレーテッド | 抗炎症剤および免疫抑制剤を含む合成ナノキャリアによる組み合わせ処置に関連する方法および組成物 |
| CN112980808B (zh) * | 2019-12-12 | 2024-10-29 | 深圳迈瑞生物医疗电子股份有限公司 | 尿酸酶、及其制备方法和用途 |
| JP2023548496A (ja) | 2020-11-03 | 2023-11-17 | プロタリクス リミテッド | 修飾ウリカーゼ及びその使用 |
| CN114438047B (zh) * | 2020-11-05 | 2024-11-22 | 重庆派金生物科技有限公司 | 制备聚乙二醇修饰的尿酸氧化酶的方法 |
| CN114438048B (zh) * | 2020-11-05 | 2024-10-22 | 重庆派金生物科技有限公司 | 尿酸氧化酶制剂及其应用 |
| JPWO2022172343A1 (GUID-C5D7CC26-194C-43D0-91A1-9AE8C70A9BFF.html) | 2021-02-10 | 2022-08-18 | ||
| CN114181917B (zh) * | 2022-02-14 | 2022-06-03 | 潍坊华卓生物科技有限公司 | 一种改造尿酸酶、基因序列、制备方法及应用 |
| US12269875B2 (en) | 2023-08-03 | 2025-04-08 | Jeff R. Peterson | Gout flare prevention methods using IL-1BETA blockers |
Family Cites Families (11)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| FR1529675A (fr) * | 1967-03-29 | 1968-06-21 | Applic Biochimiques Soc Et | Urate oxydase à haute activité et sa préparation |
| US3616231A (en) * | 1968-11-14 | 1971-10-26 | Boehringer Mannheim Gmbh | Process for the production of uricase |
| US4179337A (en) * | 1973-07-20 | 1979-12-18 | Davis Frank F | Non-immunogenic polypeptides |
| JPS6031472B2 (ja) * | 1978-12-14 | 1985-07-22 | 協和醗酵工業株式会社 | 酸性ウリカ−ゼ |
| JPS55135590A (en) * | 1979-04-05 | 1980-10-22 | Mihama Hisaharu | Modified asparaginase and uricase and their preparation |
| JPS57192435A (en) * | 1981-05-20 | 1982-11-26 | Toyobo Co Ltd | Modified polypeptide |
| JPS6255079A (ja) * | 1986-04-23 | 1987-03-10 | Mihama Hisaharu | 修飾ウリカ−ゼ |
| NZ234453A (en) * | 1989-07-13 | 1993-01-27 | Sanofi Sa | Recombinant dna encoding urate oxidase, and vector, host, protein and pharmaceutical compositions associated therewith |
| US6783965B1 (en) * | 2000-02-10 | 2004-08-31 | Mountain View Pharmaceuticals, Inc. | Aggregate-free urate oxidase for preparation of non-immunogenic polymer conjugates |
| WO2000007629A2 (en) * | 1998-08-06 | 2000-02-17 | Mountain View Pharmaceuticals, Inc. | Peg-urate oxidase conjugates and use thereof |
| PT1100880E (pt) * | 1998-08-06 | 2011-01-13 | Univ Duke | Urato-oxidase |
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