RU2246318C2 - Конъюгаты peg-уриказы и их использование - Google Patents
Конъюгаты peg-уриказы и их использование Download PDFInfo
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- RU2246318C2 RU2246318C2 RU2001103144/15A RU2001103144A RU2246318C2 RU 2246318 C2 RU2246318 C2 RU 2246318C2 RU 2001103144/15 A RU2001103144/15 A RU 2001103144/15A RU 2001103144 A RU2001103144 A RU 2001103144A RU 2246318 C2 RU2246318 C2 RU 2246318C2
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- uricase
- peg
- conjugate according
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- C12N11/00—Carrier-bound or immobilised enzymes; Carrier-bound or immobilised microbial cells; Preparation thereof
- C12N11/02—Enzymes or microbial cells immobilised on or in an organic carrier
- 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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- A61K47/50—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
- A61K47/51—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
- A61K47/56—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
- 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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- A61P13/00—Drugs for disorders of the urinary system
- A61P13/02—Drugs for disorders of the urinary system of urine or of the urinary tract, e.g. urine acidifiers
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- A—HUMAN NECESSITIES
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- A61P13/12—Drugs for disorders of the urinary system of the kidneys
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- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P19/00—Drugs for skeletal disorders
- A61P19/06—Antigout agents, e.g. antihyperuricemic or uricosuric agents
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- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Enzymes And Modification Thereof (AREA)
- Medicinal Preparation (AREA)
- Immobilizing And Processing Of Enzymes And Microorganisms (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
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| RU2004104953/15A Division RU2278680C2 (ru) | 1998-08-06 | 1999-08-02 | Способ изолирования тетрамерной формы уриказы и уриказа, полученная данным способом |
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| RU2004104953/15A RU2278680C2 (ru) | 1998-08-06 | 1999-08-02 | Способ изолирования тетрамерной формы уриказы и уриказа, полученная данным способом |
| RU2006107111/15A RU2349341C2 (ru) | 1998-08-06 | 2006-03-09 | Конъюгаты peg-уратоксидазы, их использование, способ изолирования тетрамерной формы уриказы |
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| RU2006107111/15A RU2349341C2 (ru) | 1998-08-06 | 2006-03-09 | Конъюгаты peg-уратоксидазы, их использование, способ изолирования тетрамерной формы уриказы |
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| JP (3) | JP5183836B2 (OSRAM) |
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| CZ (1) | CZ303751B6 (OSRAM) |
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| IL (3) | IL141220A0 (OSRAM) |
| NZ (1) | NZ509595A (OSRAM) |
| PL (2) | PL220873B1 (OSRAM) |
| RU (3) | RU2246318C2 (OSRAM) |
| TW (1) | TW570981B (OSRAM) |
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| RU2382048C1 (ru) * | 2008-12-25 | 2010-02-20 | Общество С Ограниченной Ответственностью "Фармапарк" | Лекарственное средство на основе модифицированного интерферона альфа с пролонгированным терапевтическим действием |
| RU2604795C2 (ru) * | 2010-03-02 | 2016-12-10 | Проталикс Лтд. | Стабилизированная альфа-галактозидаза и ее применение |
| US11598767B2 (en) | 2009-06-25 | 2023-03-07 | Horizon Therapeutics Usa, Inc. | Methods and kits for predicting infusion reaction risk and antibody-mediated loss of response by monitoring serum uric acid during pegylated uricase therapy |
| US11781119B2 (en) | 2005-04-11 | 2023-10-10 | Horizon Therapeutics Usa, Inc. | Variant forms of urate oxidase and use thereof |
| RU2831122C2 (ru) * | 2019-06-04 | 2024-12-02 | Селекта Байосайенсиз, Инк. | Композиции и дозы пегилированной уриказы |
| US12194078B2 (en) | 2017-03-11 | 2025-01-14 | Cartesian Therapeutics, Inc. | Methods and compositions related to combined treatment with anti-inflammatories and synthetic nanocarriers comprising an immunosuppressant |
| US12465631B2 (en) | 2019-01-30 | 2025-11-11 | Horizon Therapeutics Usa, Inc. | Reducing immunogenicity to pegloticase |
| US12472167B2 (en) | 2013-05-03 | 2025-11-18 | Cartesian Therapeutics, Inc. | Methods providing a therapeutic macromolecule and synthetic nanocarriers comprising immunosuppressant locally and concomitantly to reduce both Type 1 and Type IV hypersensitivity |
| US12496331B2 (en) | 2016-11-11 | 2025-12-16 | Horizon Therapeutics Usa, Inc. | Combination therapies of prednisone and uricase molecules and uses thereof |
| US12553041B2 (en) | 2019-06-04 | 2026-02-17 | Cartesian Therapeutics Inc. | Formulations and doses of pegylated uricase |
Families Citing this family (32)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP2158923B1 (en) | 1998-08-06 | 2013-02-27 | Mountain View Pharmaceuticals, Inc. | 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 |
| CA2337967C (en) | 1998-08-06 | 2011-11-01 | Duke University | Recombinant uricase protein |
| EP1100542B1 (en) * | 1998-08-06 | 2005-06-22 | 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 |
| AU2001268734A1 (en) | 2000-06-28 | 2002-01-08 | Merck & Co., Inc. | Use of agents capable of reducing uric acid levels for the treatment of cardiovascular disease |
| AU2002345938A1 (en) | 2001-06-28 | 2003-03-03 | Mountain View Pharmaceuticals, Inc. | Polymer stabilized proteinases |
| 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 |
| JP2007500218A (ja) | 2003-05-12 | 2007-01-11 | アフィーマックス・インコーポレイテッド | ポリ（エチレングリコール）修飾ペプチド系化合物の新規スペーサー部分 |
| ES2395413T3 (es) | 2003-05-12 | 2013-02-12 | Affymax, Inc. | Péptidos que se unen al receptor de eritropoyetina |
| CA2571292C (en) * | 2004-06-30 | 2013-05-21 | Nektar Therapeutics Al, Corporation | Polymer-factor ix moiety conjugates |
| US8148123B2 (en) | 2005-04-11 | 2012-04-03 | Savient Pharmaceuticals, Inc. | Methods for lowering elevated uric acid levels using intravenous injections of PEG-uricase |
| WO2008051178A2 (en) * | 2006-04-12 | 2008-05-02 | Savient Pharmaceuticals, Inc. | Purification of proteins with cationic surfactant |
| CN102807973A (zh) * | 2005-04-11 | 2012-12-05 | 萨文特医药公司 | 尿酸氧化酶的变体形式及其用途 |
| CA2607953A1 (en) | 2005-05-09 | 2006-11-16 | Tap Pharmaceutical Products, Inc. | Methods for treating nephrolithiasis |
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| 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 |
| ES2532210T3 (es) | 2010-09-10 | 2015-03-25 | Takeda Pharmaceuticals U.S.A., Inc. | Métodos para el tratamiento concomitante de teofilina y 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 |
| 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 |
| 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 |
| CN117098559A (zh) | 2020-11-03 | 2023-11-21 | 波塔力克斯有限公司 | 修饰的尿酸酶及其用途 |
| 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 |
| WO2022172343A1 (ja) | 2021-02-10 | 2022-08-18 | オリエンタル酵母工業株式会社 | ウリカーゼ活性化剤及び尿酸測定試薬 |
| 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 |
|---|---|---|---|---|
| US4179337A (en) * | 1973-07-20 | 1979-12-18 | Davis Frank F | Non-immunogenic polypeptides |
| RU2105812C1 (ru) * | 1989-07-13 | 1998-02-27 | Санофи | Полипептид, обладающий уратоксидазной активностью, фрагмент днк, обеспечивающий экспрессию полипептида с уратоксидазной активностью (варианты), вектор экспрессии, содержащий фрагмент днк, обеспечивающий экспрессию полипептида с уратоксидазной активностью (варианты), штамм, экспрессирующий полипептид, обладающий уратоксидазной активностью (варианты), способ получения полипептида, обладающего уратоксидазной активностью |
Family Cites Families (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| FR6301M (OSRAM) * | 1967-03-29 | 1968-09-09 | ||
| US3616231A (en) * | 1968-11-14 | 1971-10-26 | Boehringer Mannheim Gmbh | Process for the production of uricase |
| 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 |
| EP1100542B1 (en) * | 1998-08-06 | 2005-06-22 | Mountain View Pharmaceuticals, Inc. | 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 |
| CA2337967C (en) * | 1998-08-06 | 2011-11-01 | Duke University | Recombinant uricase protein |
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1999
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Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4179337A (en) * | 1973-07-20 | 1979-12-18 | Davis Frank F | Non-immunogenic polypeptides |
| RU2105812C1 (ru) * | 1989-07-13 | 1998-02-27 | Санофи | Полипептид, обладающий уратоксидазной активностью, фрагмент днк, обеспечивающий экспрессию полипептида с уратоксидазной активностью (варианты), вектор экспрессии, содержащий фрагмент днк, обеспечивающий экспрессию полипептида с уратоксидазной активностью (варианты), штамм, экспрессирующий полипептид, обладающий уратоксидазной активностью (варианты), способ получения полипептида, обладающего уратоксидазной активностью |
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