CZ303751B6 - Farmaceutický prostredek urikasy, lécivo, pouzití a zpusob prípravy - Google Patents
Farmaceutický prostredek urikasy, lécivo, pouzití a zpusob prípravy Download PDFInfo
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- CZ303751B6 CZ303751B6 CZ20010317A CZ2001317A CZ303751B6 CZ 303751 B6 CZ303751 B6 CZ 303751B6 CZ 20010317 A CZ20010317 A CZ 20010317A CZ 2001317 A CZ2001317 A CZ 2001317A CZ 303751 B6 CZ303751 B6 CZ 303751B6
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- uricase
- peg
- pharmaceutical composition
- conjugates
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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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- A61K47/60—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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Landscapes
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| BR (2) | BRPI9917760B8 (enExample) |
| CZ (1) | CZ303751B6 (enExample) |
| HU (2) | HU226294B1 (enExample) |
| IL (3) | IL141220A0 (enExample) |
| NZ (1) | NZ509595A (enExample) |
| PL (2) | PL220873B1 (enExample) |
| RU (3) | RU2278680C2 (enExample) |
| TW (1) | TW570981B (enExample) |
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| Publication number | Priority date | Publication date | Assignee | Title |
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| CA2338665C (en) | 1998-08-06 | 2011-01-18 | Mountain View Pharmaceuticals, Inc. | Peg-urate oxidase conjugates and use thereof |
| EP2277998B1 (en) | 1998-08-06 | 2016-04-20 | Duke University | Urate oxidase |
| HU226294B1 (en) * | 1998-08-06 | 2008-08-28 | Mountain View Pharmaceuticals | Peg-urate oxidase conjugates and use thereof |
| US6783965B1 (en) | 2000-02-10 | 2004-08-31 | Mountain View Pharmaceuticals, Inc. | Aggregate-free urate oxidase for preparation of non-immunogenic polymer conjugates |
| 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 |
| US7799794B2 (en) | 2000-06-28 | 2010-09-21 | Merck Sharp & Dohme Corp. | Treatment for cardiovascular disease |
| DE60229958D1 (de) | 2001-06-28 | 2009-01-02 | Mountain View Pharmaceuticals | Polymerstabilisierte proteinasen |
| 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 |
| MXPA05012314A (es) | 2003-05-12 | 2006-04-18 | Affymax Inc | Radical separador para peptido modificado con polietilenglicol. |
| DK1625156T3 (da) | 2003-05-12 | 2013-01-07 | Affymax Inc | Peptider, der bindes til erythropoietinreceptoren |
| WO2006005058A2 (en) * | 2004-06-30 | 2006-01-12 | Nektar Therapeutics Al, Corporation | Polymer-factor ix moiety conjugates |
| WO2008051178A2 (en) * | 2006-04-12 | 2008-05-02 | Savient Pharmaceuticals, Inc. | Purification of proteins with cationic surfactant |
| US7811800B2 (en) | 2005-04-11 | 2010-10-12 | Savient Pharmaceuticals, Inc. | Variant form of urate oxidase and use thereof |
| US8148123B2 (en) | 2005-04-11 | 2012-04-03 | Savient Pharmaceuticals, Inc. | Methods for lowering elevated uric acid levels using intravenous injections of PEG-uricase |
| US8188224B2 (en) | 2005-04-11 | 2012-05-29 | Savient Pharmaceuticals, Inc. | Variant forms of urate oxidase and use thereof |
| WO2006121995A2 (en) | 2005-05-09 | 2006-11-16 | Tap Pharmaceutical Products, Inc. | Methods for treating nephrolithiasis |
| US7550433B2 (en) | 2005-06-03 | 2009-06-23 | Affymax, Inc. | Erythropoietin receptor peptide formulations and uses |
| 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 |
| EP4635567A3 (en) | 2009-06-25 | 2025-12-03 | Horizon Therapeutics USA, Inc. | Methods and kits for preventing infusion reaction risk and antibody-mediated loss of response by monitoring serum uric acid during pegylated uricase therapy |
| WO2012033941A1 (en) | 2010-09-10 | 2012-03-15 | Takeda Pharmaceuticals North America, 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 |
| US9744175B2 (en) | 2012-04-06 | 2017-08-29 | Indus Pharmaceuticals, Inc. | Compositions of combinations of non-covalent DNA binding agents and anti-cancer and/or anti-inflammatory agents and their use in disease treatment |
| CN110251675A (zh) | 2013-05-03 | 2019-09-20 | 西莱克塔生物科技公司 | 降低或预防响应于非变应原性抗原的过敏反应的致耐受性合成纳米载体 |
| AU2016265677B2 (en) * | 2015-05-15 | 2021-12-09 | 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 |
| CN110234340A (zh) | 2016-11-11 | 2019-09-13 | 好利恩风湿病制药有限责任公司 | 泼尼松和尿酸酶分子的组合疗法及其用途 |
| US20200237881A1 (en) | 2019-01-30 | 2020-07-30 | Horizon Pharma Rheumatology Llc | Reducing immunogenicity to pegloticase |
| ES3036482T3 (en) | 2017-03-11 | 2025-09-19 | Cartesian Therapeutics Inc | Methods and compositions related to combined treatment with anti-inflammatories and synthetic nanocarriers comprising an immunosuppressant |
| AU2020287627A1 (en) | 2019-06-04 | 2021-11-18 | Selecta Biosciences, Inc. | Formulations and doses of PEGylated uricase |
| 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 |
| KR20230110281A (ko) | 2020-11-03 | 2023-07-21 | 프로탈릭스 리미티드 | 변형된 유리카제(uricase) 및 이의 용도 |
| 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 |
| 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 |
| CA3211023A1 (en) | 2021-02-10 | 2022-08-18 | Oriental Yeast Co., Ltd. | Uricase activator and uric acid measurement reagent |
| 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 |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS57192435A (en) * | 1981-05-20 | 1982-11-26 | Toyobo Co Ltd | Modified polypeptide |
| EP1100542A2 (en) * | 1998-08-06 | 2001-05-23 | Mountain View Pharmaceuticals, Inc. | Peg-urate oxidase conjugates and use thereof |
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| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| FR6301M (enExample) * | 1967-03-29 | 1968-09-09 | ||
| 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 |
| 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 |
| EP2277998B1 (en) * | 1998-08-06 | 2016-04-20 | Duke University | Urate oxidase |
-
1999
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Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS57192435A (en) * | 1981-05-20 | 1982-11-26 | Toyobo Co Ltd | Modified polypeptide |
| EP1100542A2 (en) * | 1998-08-06 | 2001-05-23 | Mountain View Pharmaceuticals, Inc. | Peg-urate oxidase conjugates and use thereof |
Non-Patent Citations (7)
| Title |
|---|
| Chen a kol. (1981) Biochim. Biophys. Acta Enzymology 660, 293-98 * |
| Chua a kol. (1988) Ann. Intern. Med. 109, 114-17 * |
| Montalbini a kol. (1997) Planta 202, 277-283 * |
| Osman a kol. (1989) Comp. Biochem. Physiol. B 94, 469-74 * |
| Tsuji a kol. (1985) Int. J. Immunopharmacol. 7, 725-30 * |
| Veronese a kol. (1997) J. Bioact. Compat. Pol. 12, 196-207 * |
| Yasuda a kol. (1990) Chem. Pharm. Bull. 38, 2053-56, viz Obr. 1 a Tabulka II na str. 2054 * |
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Effective date: 20240802 |