ZA200207206B - Aggregate-free urate oxidase for preparation of non-immunogenic polymer conjugates. - Google Patents

Aggregate-free urate oxidase for preparation of non-immunogenic polymer conjugates. Download PDF

Info

Publication number: ZA200207206B
Authority: ZA; South Africa
Prior art keywords: uricase; poly; conjugate; peg; ethylene glycol
Prior art date: 2000-02-10

Application number

ZA200207206A

Other languages

English (en)

Inventor

Mark G P Saifer

Merry R Sherman

Williams L David

Original Assignee

Mountain View Pharmaceuticals

Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)

2000-02-10

Filing date

2002-09-09

Publication date

2003-05-06

2002-09-09 Application filed by Mountain View Pharmaceuticals filed Critical Mountain View Pharmaceuticals

2003-05-06 Publication of ZA200207206B publication Critical patent/ZA200207206B/en

Links

108010092464 Urate Oxidase Proteins 0.000 title claims description 272
229940005267 urate oxidase Drugs 0.000 title claims description 7
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229920000642 polymer Polymers 0.000 title description 7
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229920003171 Poly (ethylene oxide) Polymers 0.000 claims description 17
LEHOTFFKMJEONL-UHFFFAOYSA-N Uric Acid Chemical compound N1C(=O)NC(=O)C2=C1NC(=O)N2 LEHOTFFKMJEONL-UHFFFAOYSA-N 0.000 claims description 17
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LYCAIKOWRPUZTN-UHFFFAOYSA-N Ethylene glycol Chemical compound OCCO LYCAIKOWRPUZTN-UHFFFAOYSA-N 0.000 claims description 14
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Classifications

- 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)
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K47/00—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
- 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
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- 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)
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- C12N9/96—Stabilising an enzyme by forming an adduct or a composition; Forming enzyme conjugates
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ZA200207206A 2000-02-10 2002-09-09 Aggregate-free urate oxidase for preparation of non-immunogenic polymer conjugates. ZA200207206B (en)

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EP (3)	EP1254237B1 (fr)
JP (2)	JP5165826B2 (fr)
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CN (2)	CN101735991B (fr)
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ES (2)	ES2343105T3 (fr)
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Families Citing this family (63)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US6057287A (en)	1994-01-11	2000-05-02	Dyax Corp.	Kallikrein-binding "Kunitz domain" proteins and analogues thereof
EP1100542B1 (fr) *	1998-08-06	2005-06-22	Mountain View Pharmaceuticals, Inc.	Conjugues peg-urate oxydase et utilisation associee
CA2337967C (fr)	1998-08-06	2011-11-01	Duke University	Proteine uricase recombinante
US20060188971A1 (en) *	1998-08-06	2006-08-24	Duke University	Urate oxidase
US6783965B1 (en)	2000-02-10	2004-08-31	Mountain View Pharmaceuticals, Inc.	Aggregate-free urate oxidase for preparation of non-immunogenic polymer conjugates
EP2158923B1 (fr)	1998-08-06	2013-02-27	Mountain View Pharmaceuticals, Inc.	Conjugués peg-urate oxydase et utilisation associée
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
DK2311432T3 (en)	2002-06-07	2015-02-02	Dyax Corp	Modified Kunitz domain polypeptides and their use in reducing ischemia or the onset of a systemic inflammatory response associated with a surgical procedure
US7153829B2 (en)	2002-06-07	2006-12-26	Dyax Corp.	Kallikrein-inhibitor therapies
US20040062748A1 (en)	2002-09-30	2004-04-01	Mountain View Pharmaceuticals, Inc.	Polymer conjugates with decreased antigenicity, methods of preparation and uses thereof
US8129330B2 (en) *	2002-09-30	2012-03-06	Mountain View Pharmaceuticals, Inc.	Polymer conjugates with decreased antigenicity, methods of preparation and uses thereof
CN102319437B (zh) *	2002-12-26	2017-10-13	山景医药公司	具有增强的生物学效用的干扰素‑β的聚合物缀合物
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
EP1626983B8 (fr) *	2003-05-12	2010-12-22	Affymax, Inc.	Nouveaux composes modifies par du poly(ethylene glycol) et leurs utilisations
AU2004268145B2 (en) *	2003-08-29	2010-09-16	Takeda Pharmaceutical Company Limited	Poly-PEGylated protease inhibitors
US7235530B2 (en)	2004-09-27	2007-06-26	Dyax Corporation	Kallikrein inhibitors and anti-thrombolytic agents and uses thereof
WO2006060148A2 (fr) *	2004-11-11	2006-06-08	Affymax, Inc.	Nouveaux peptides qui se lient au recepteur d'erythropoietine
WO2006062685A2 (fr) *	2004-11-11	2006-06-15	Affymax, Inc.	Nouveaux peptides se liant au recepteur de l'erythropoietine
EP2314320A2 (fr) *	2005-04-05	2011-04-27	Istituto di Richerche di Biologia Molecolare P. Angeletti S.p.A.	Procédé de protection de sites fonctionnels ou épitopes sur des protéines
TWI418564B (zh) *	2005-04-11	2013-12-11	Savient Pharmaceuticals Inc	利用陽離子界面活性劑之蛋白質純化
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
WO2008051178A2 (fr) *	2006-04-12	2008-05-02	Savient Pharmaceuticals, Inc.	Purification de protéines au moyen d'un tensioactif cationique
DK3321359T3 (da)	2005-04-11	2021-03-08	Horizon Pharma Rheumatology Llc	Variante former af uratoxidase og anvendelse deraf
US20080159976A1 (en) *	2005-04-11	2008-07-03	Jacob Hartman	Methods for lowering elevated uric acid levels using intravenous injections of PEG-uricase
US8148123B2 (en) *	2005-04-11	2012-04-03	Savient Pharmaceuticals, Inc.	Methods for lowering elevated uric acid levels using intravenous injections of PEG-uricase
JP2008545665A (ja) *	2005-05-23	2008-12-18	ユニベルシテドゥジュネーブ	高体温による処置のための注入可能な超常磁性ナノ粒子および高体温インプラントを形成するための使用
US8324159B2 (en) *	2005-06-03	2012-12-04	Affymax, Inc.	Erythropoietin receptor peptide formulations and uses
US7550433B2 (en) *	2005-06-03	2009-06-23	Affymax, Inc.	Erythropoietin receptor peptide formulations and uses
US7919461B2 (en)	2005-06-03	2011-04-05	Affymax, Inc.	Erythropoietin receptor peptide formulations and uses
WO2009026334A2 (fr) *	2007-08-21	2009-02-26	Genzyme Corporation	Traitement par des inhibiteurs de la kallikréine
US8637454B2 (en)	2009-01-06	2014-01-28	Dyax Corp.	Treatment of mucositis with kallikrein inhibitors
RU2535038C2 (ru)	2009-06-25	2014-12-10	Криэлта Фармасьютикалз ЭлЭлСи	Способы и наборы для прогнозирования риска инфузионных реакций и опосредованной антителами потери ответа при терапии пэгилированной уриказой с помощью мониторинга содержания мочевой кислоты в сыворотке крови
ES2688093T3 (es)	2010-01-06	2018-10-30	Dyax Corp.	Proteínas de unión a calicreína plasmática
US8940861B2 (en)	2010-04-08	2015-01-27	Georgia Tech Research Corporation	Variants of ancestral uricases and uses thereof
IL269565B2 (en)	2011-01-06	2024-06-01	Dyax Corp	Plasma kallikrein binding proteins
CN102827073A (zh)	2011-06-17	2012-12-19	安吉奥斯医药品有限公司	治疗活性组合物和它们的使用方法
US9474779B2 (en)	2012-01-19	2016-10-25	Agios Pharmaceuticals, Inc.	Therapeutically active compositions and their methods of use
WO2014197806A2 (fr)	2013-06-07	2014-12-11	Allena Pharmaceuticals, Inc.	Compositions, méthodes et dispositifs de dialyse
WO2015003355A2 (fr)	2013-07-11	2015-01-15	Agios Pharmaceuticals, Inc.	Composés thérapeutiquement actifs et leurs méthodes d'utilisation
WO2015003360A2 (fr)	2013-07-11	2015-01-15	Agios Pharmaceuticals, Inc.	Composés thérapeutiquement actifs et leurs méthodes d'utilisation
US10376510B2 (en)	2013-07-11	2019-08-13	Agios Pharmaceuticals, Inc.	2,4- or 4,6-diaminopyrimidine compounds as IDH2 mutants inhibitors for the treatment of cancer
WO2015010297A1 (fr)	2013-07-25	2015-01-29	Agios Pharmaceuticals, Inc.	Composés thérapeutiquement actifs et leurs méthodes d'utilisation
US9968595B2 (en)	2014-03-14	2018-05-15	Agios Pharmaceuticals, Inc.	Pharmaceutical compositions of therapeutically active compounds
EP3122782A4 (fr)	2014-03-27	2017-09-13	Dyax Corp.	Compositions et procédés pour le traitement de l'oedème maculaire diabétique
AU2016265677B2 (en)	2015-05-15	2021-12-09	Medimmune, Llc	Improved uricase sequences and methods of treatment
DK3362066T3 (da)	2015-10-15	2021-11-22	Les Laboratoires Servier Sas	Kombinationsterapi til behandling af maligniteter
UA123401C2 (uk)	2015-10-15	2021-03-31	Аджиос Фармасьютікалз, Інк.	Комбінована терапія для лікування злоякісних пухлин
BR112018011622A2 (pt)	2015-12-11	2018-11-27	Dyax Corp	método para tratar ataque de angioedema hereditário (hae) ou reduzir a taxa de ataque de hae
EP3538135A4 (fr)	2016-11-11	2020-07-29	Horizon Pharma Rheumatology LLC	Polythérapies de molécules de prednisone et d'uricase et leurs utilisations
US20200237881A1 (en)	2019-01-30	2020-07-30	Horizon Pharma Rheumatology Llc	Reducing immunogenicity to pegloticase
CA3069197A1 (fr)	2017-07-07	2019-01-10	Allena Pharmaceuticals, Inc.	Enzyme uricase recombinante
US20190309269A1 (en)	2018-03-20	2019-10-10	Rubius Therapeutics, Inc.	Therapeutic cell systems and methods for treating hyperuricemia and gout
US10980788B2 (en)	2018-06-08	2021-04-20	Agios Pharmaceuticals, Inc.	Therapy for treating malignancies
CN109055260B (zh) *	2018-08-08	2021-11-09	淮海工学院	弯曲芽孢杆菌alkaAU及产尿酸氧化酶方法、产品与应用
US12121566B2 (en)	2019-01-30	2024-10-22	Horizon Therapeutics Usa, Inc.	Methods for treating gout
AU2020276510B2 (en) *	2019-05-10	2024-08-01	Hangzhou Grand Biologic Pharmaceutical Inc.	Polyethylene glycol-modified urate oxidase
CA3167336A1 (fr)	2020-01-13	2021-07-22	Takeda Pharmaceutical Company Limited	Inhibiteurs de la kallicreine plasmatique et leurs utilisations pour traiter une crise d'angio-deme hereditaire pediatrique
AU2021324665A1 (en)	2020-08-10	2023-04-13	Horizon Therapeutics Usa, Inc.	Methods of treating gout
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
CN117051026A (zh) *	2022-05-06	2023-11-14	江苏恰瑞生物科技有限公司	一种特异性尿酸结合物固定化树脂及其制备方法和应用
US12269875B2 (en)	2023-08-03	2025-04-08	Jeff R. Peterson	Gout flare prevention methods using IL-1BETA blockers

Family Cites Families (55)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
DE279486C (fr)
FR6301M (fr) *	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
JPS5599189A (en)	1979-01-22	1980-07-28	Mihama Hisaharu	Modified uricase free from antigenicity and its preparation
JPS55135590A (en)	1979-04-05	1980-10-22	Mihama Hisaharu	Modified asparaginase and uricase and their preparation
CH651308A5 (de)	1980-07-01	1985-09-13	Hoffmann La Roche	Interferone und deren herstellung.
JPS57192435A (en)	1981-05-20	1982-11-26	Toyobo Co Ltd	Modified polypeptide
DE3126759A1 (de)	1981-07-07	1983-01-27	Boehringer Mannheim Gmbh, 6800 Mannheim	Loesliche leber-uricase, verfahren zu ihrer herstellung und verwendung
US4917888A (en)	1985-06-26	1990-04-17	Cetus Corporation	Solubilization of immunotoxins for pharmaceutical compositions using polymer conjugation
DE3676670D1 (de) *	1985-06-26	1991-02-07	Cetus Corp	Solubilisierung von proteinen fuer pharmazeutische zusammensetzungen mittels polymerkonjugierung.
US4766106A (en)	1985-06-26	1988-08-23	Cetus Corporation	Solubilization of proteins for pharmaceutical compositions using polymer conjugation
US4847079A (en)	1985-07-29	1989-07-11	Schering Corporation	Biologically stable interferon compositions comprising thimerosal
DD279486A1 (de)	1986-03-10	1990-06-06	Akad Wissenschaften Ddr	Verfahren zur aktivierung von hydroxylgruppenhaltigen polymeren verbindungen
JPS6255079A (ja) *	1986-04-23	1987-03-10	Mihama Hisaharu	修飾ウリカ−ゼ
JPH085506B2 (ja) *	1986-08-25	1996-01-24	日東製器株式会社	缶容器
DD279489A1 (de)	1986-12-11	1990-06-06	Leuna Werke Veb	Verfahren zur herstellung optisch transparenter epoxidharzformmassen
US5080891A (en)	1987-08-03	1992-01-14	Ddi Pharmaceuticals, Inc.	Conjugates of superoxide dismutase coupled to high molecular weight polyalkylene glycols
US4847325A (en)	1988-01-20	1989-07-11	Cetus Corporation	Conjugation of polymer to colony stimulating factor-1
US5955336A (en) *	1988-08-17	1999-09-21	Toyo Boseki Kabushiki Kaisha	DNA sequence for uricase and manufacturing process of uricase
US5349052A (en)	1988-10-20	1994-09-20	Royal Free Hospital School Of Medicine	Process for fractionating polyethylene glycol (PEG)-protein adducts and an adduct for PEG and granulocyte-macrophage colony stimulating factor
US5324844A (en)	1989-04-19	1994-06-28	Enzon, Inc.	Active carbonates of polyalkylene oxides for modification of polypeptides
US5122614A (en)	1989-04-19	1992-06-16	Enzon, Inc.	Active carbonates of polyalkylene oxides for modification of polypeptides
US5382518A (en)	1989-07-13	1995-01-17	Sanofi	Urate oxidase activity protein, recombinant gene coding therefor, expression vector, micro-organisms and transformed cells
NZ234453A (en) *	1989-07-13	1993-01-27	Sanofi Sa	Recombinant dna encoding urate oxidase, and vector, host, protein and pharmaceutical compositions associated therewith
US5286637A (en)	1989-08-07	1994-02-15	Debiopharm, S.A.	Biologically active drug polymer derivatives and method for preparing same
JPH03148298A (ja)	1989-11-01	1991-06-25	Sumitomo Pharmaceut Co Ltd	修飾ペプチドおよびその製造方法
SU1730145A1 (ru) *	1990-05-04	1992-04-30	Всесоюзный научно-исследовательский институт текстильно-галантерейной промышленности	Способ стабилизации уриказы
US5766897A (en) *	1990-06-21	1998-06-16	Incyte Pharmaceuticals, Inc.	Cysteine-pegylated proteins
US5653974A (en)	1990-10-18	1997-08-05	Board Of Regents,The University Of Texas System	Preparation and characterization of liposomal formulations of tumor necrosis factor
GEP20033082B (en) *	1991-03-15	2003-10-27	Amgen Inc	Pegylation of Polypeptides
WO1993000951A1 (fr)	1991-07-02	1993-01-21	Inhale, Inc.	Procede et dispositf d'administration de medicaments en aerosol
WO1994019007A1 (fr)	1993-02-16	1994-09-01	Enzon, Inc.	Compositions proteiques d'inactivation du ribosome presentant une antigenicite reduite
WO1994023740A1 (fr) *	1993-04-22	1994-10-27	Celtrix Pharmaceuticals, Inc.	Conjugues du facteur de croissance et d'inhibiteur de la resorption osseuse
WO1995000162A1 (fr)	1993-06-21	1995-01-05	Enzon, Inc.	Synthese de peptides conjuges modifies, sur des sites specifiques
IT1265101B1 (it) *	1993-07-23	1996-10-30	Erba Carlo Spa	Derivati dell'acido 2-ammino-4-fenil-4-osso butirrico
US5919455A (en)	1993-10-27	1999-07-06	Enzon, Inc.	Non-antigenic branched polymer conjugates
US5643575A (en)	1993-10-27	1997-07-01	Enzon, Inc.	Non-antigenic branched polymer conjugates
DE69430251T2 (de)	1993-11-10	2002-11-07	Enzon, Inc.	Verbesserte interferon-polymerkonjugate
US5824784A (en)	1994-10-12	1998-10-20	Amgen Inc.	N-terminally chemically modified protein compositions and methods
AU697440B2 (en)	1994-12-07	1998-10-08	Novozymes A/S	Polypeptide with reduced allergenicity
US5932462A (en)	1995-01-10	1999-08-03	Shearwater Polymers, Inc.	Multiarmed, monofunctional, polymer for coupling to molecules and surfaces
TW426523B (en)	1995-04-06	2001-03-21	Hoffmann La Roche	Interferon solution
FR2733914B1 (fr) *	1995-05-11	1997-08-01	Sanofi Sa	Composition de liquide stable contenant de l'urate oxydase et composition lyophilisee pour sa preparation
US5853974A (en)	1995-06-07	1998-12-29	Chiron Corporation	Enhancement of alkaline phosphatase with SDS in chemiluminescent substrates
JPH09154581A (ja)	1995-12-05	1997-06-17	Asahi Chem Ind Co Ltd	ウリカーゼを生産する実質上純粋な微生物
CN1168495C (zh)	1997-01-15	2004-09-29	凤凰药理学公司	被修饰的肿瘤坏死因子
EP1084136B1 (fr) *	1998-06-01	2004-08-25	Genentech, Inc.	Separation des monomeres d'un anticorps de ses multimeres par l'utilisation de la chromatographie echangeuse d'ions
CA2337967C (fr)	1998-08-06	2011-11-01	Duke University	Proteine uricase recombinante
US6783965B1 (en)	2000-02-10	2004-08-31	Mountain View Pharmaceuticals, Inc.	Aggregate-free urate oxidase for preparation of non-immunogenic polymer conjugates
EP2158923B1 (fr) *	1998-08-06	2013-02-27	Mountain View Pharmaceuticals, Inc.	Conjugués peg-urate oxydase et utilisation associée
EP1100542B1 (fr)	1998-08-06	2005-06-22	Mountain View Pharmaceuticals, Inc.	Conjugues peg-urate oxydase et utilisation associee
US6425448B1 (en)	2001-01-30	2002-07-30	Cdx Gas, L.L.P.	Method and system for accessing subterranean zones from a limited surface area
US6913915B2 (en)	2001-08-02	2005-07-05	Phoenix Pharmacologics, Inc.	PEG-modified uricase
EP3005545A1 (fr)	2013-05-24	2016-04-13	Zentrum Mikroelektronik Dresden AG	Convertisseur continu - continu numérique non pwm

2000
- 2000-02-10 US US09/501,730 patent/US6783965B1/en not_active Expired - Lifetime
2001
- 2001-02-06 TW TW097145974A patent/TW200914617A/zh unknown
- 2001-02-06 TW TW090102540A patent/TWI322184B/zh not_active IP Right Cessation
- 2001-02-07 HU HU0204544A patent/HU227127B1/hu active Protection Beyond IP Right Term
- 2001-02-07 PT PT01923265T patent/PT1254237E/pt unknown
- 2001-02-07 PT PT101804284T patent/PT2305819E/pt unknown
- 2001-02-07 AU AU2001249975A patent/AU2001249975B2/en not_active Revoked
- 2001-02-07 MX MXPA02007545A patent/MXPA02007545A/es active IP Right Grant
- 2001-02-07 DK DK01923265.1T patent/DK1254237T3/da active
- 2001-02-07 CN CN2009101278530A patent/CN101735991B/zh not_active Expired - Lifetime
- 2001-02-07 DK DK10180428.4T patent/DK2305819T3/en active
- 2001-02-07 DE DE60141742T patent/DE60141742D1/de not_active Expired - Lifetime
- 2001-02-07 EP EP01923265A patent/EP1254237B1/fr not_active Expired - Lifetime
- 2001-02-07 NZ NZ520434A patent/NZ520434A/en not_active IP Right Cessation
- 2001-02-07 IL IL15106501A patent/IL151065A0/xx unknown
- 2001-02-07 AU AU4997501A patent/AU4997501A/xx active Pending
- 2001-02-07 WO PCT/US2001/040069 patent/WO2001059078A2/fr not_active Ceased
- 2001-02-07 EP EP10180428.4A patent/EP2305819B1/fr not_active Expired - Lifetime
- 2001-02-07 KR KR1020077018682A patent/KR20070092329A/ko not_active Ceased
- 2001-02-07 BR BRPI0108386A patent/BRPI0108386B8/pt not_active Application Discontinuation
- 2001-02-07 RU RU2002120486/13A patent/RU2281954C2/ru not_active IP Right Cessation
- 2001-02-07 JP JP2001558218A patent/JP5165826B2/ja not_active Expired - Lifetime
- 2001-02-07 RU RU2006107110/13A patent/RU2352354C2/ru active
- 2001-02-07 EP EP10158016.5A patent/EP2196538B1/fr not_active Expired - Lifetime
- 2001-02-07 ES ES01923265T patent/ES2343105T3/es not_active Expired - Lifetime
- 2001-02-07 KR KR1020087024272A patent/KR101054247B1/ko not_active Expired - Lifetime
- 2001-02-07 KR KR1020027010189A patent/KR100884724B1/ko not_active Expired - Lifetime
- 2001-02-07 PL PL358539A patent/PL208064B1/pl unknown
- 2001-02-07 CZ CZ2002-2982A patent/CZ304864B6/cs not_active IP Right Cessation
- 2001-02-07 CA CA2398679A patent/CA2398679C/fr not_active Expired - Lifetime
- 2001-02-07 CN CNB018077501A patent/CN100491532C/zh not_active Expired - Lifetime
- 2001-02-07 ES ES10180428.4T patent/ES2524153T3/es not_active Expired - Lifetime
- 2001-02-07 AT AT01923265T patent/ATE463576T1/de active
- 2001-02-07 DK DK10158016.5T patent/DK2196538T3/en active
2002
- 2002-08-05 IL IL151065A patent/IL151065A/en active Protection Beyond IP Right Term
- 2002-09-09 ZA ZA200207206A patent/ZA200207206B/en unknown
2007
- 2007-08-03 US US11/882,750 patent/US7927852B2/en not_active Expired - Fee Related
2008
- 2008-08-11 IL IL193365A patent/IL193365A/en active IP Right Grant
2009
- 2009-02-06 RU RU2009104003/10A patent/RU2557318C9/ru active
- 2009-09-02 AU AU2009212900A patent/AU2009212900B2/en not_active Expired
2010
- 2010-06-29 CY CY20101100597T patent/CY1110142T1/el unknown
2011
- 2011-04-12 JP JP2011088663A patent/JP5341945B2/ja not_active Expired - Lifetime
- 2011-04-13 US US13/085,793 patent/US8921064B2/en not_active Expired - Fee Related
2013
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- 2013-07-03 BE BE2013C045C patent/BE2013C045I2/fr unknown
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- 2013-07-04 FR FR13C0036C patent/FR13C0036I2/fr active Active
2015
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Also Published As

Publication number	Publication date
KR100884724B1 (ko)	2009-02-19
CY1110142T1 (el)	2015-01-14
JP2003521937A (ja)	2003-07-22
ES2343105T8 (es)	2013-07-15
DK1254237T3 (da)	2010-07-19
ES2343105T3 (es)	2010-07-23
BR0108386B1 (pt)	2017-10-31
TWI322184B (en)	2010-03-21
CY2013028I2 (el)	2015-11-04
EP2305819A1 (fr)	2011-04-06
US6783965B1 (en)	2004-08-31
MXPA02007545A (es)	2002-12-13
DK2196538T3 (en)	2015-01-05
FR13C0036I1 (fr)	2013-08-09
KR101054247B1 (ko)	2011-08-08
AU4997501A (en)	2001-08-20
IL151065A0 (en)	2003-04-10
RU2557318C9 (ru)	2015-09-10
CN101735991B (zh)	2013-09-11
PT1254237E (pt)	2010-06-07
PT2305819E (pt)	2015-06-01
RU2006107110A (ru)	2007-09-20
CZ304864B6 (cs)	2014-12-17
CA2398679C (fr)	2015-11-17
CN1423699A (zh)	2003-06-11
KR20020087934A (ko)	2002-11-23
RU2557318C2 (ru)	2015-07-20
WO2001059078A2 (fr)	2001-08-16
JP5165826B2 (ja)	2013-03-21
WO2001059078A3 (fr)	2002-03-07
HU227127B1 (en)	2010-07-28
PL208064B1 (pl)	2011-03-31
JP2011188861A (ja)	2011-09-29
CY1117264T1 (el)	2017-04-26
AU2009212900A1 (en)	2009-10-01
CN100491532C (zh)	2009-05-27
EP1254237B1 (fr)	2010-04-07
FR13C0036I2 (fr)	2014-05-16
HK1155203A1 (en)	2012-05-11
AU2009212900B2 (en)	2011-12-08
NZ520434A (en)	2004-05-28
HK1056742A1 (zh)	2004-02-27
BR0108386A (pt)	2002-10-29
US8921064B2 (en)	2014-12-30
CZ20022982A3 (cs)	2003-01-15
KR20080098686A (ko)	2008-11-11
US20080057048A1 (en)	2008-03-06
EP2196538A1 (fr)	2010-06-16
DK2305819T3 (en)	2015-01-05
CA2398679A1 (fr)	2001-08-16
EP2196538B1 (fr)	2014-10-01
CN101735991A (zh)	2010-06-16
RU2281954C2 (ru)	2006-08-20
BR0108386C1 (pt)	2011-12-20
PL358539A1 (en)	2004-08-09
IL193365A (en)	2011-08-31
BRPI0108386B8 (pt)	2021-05-25
IL151065A (en)	2008-12-29
JP5341945B2 (ja)	2013-11-13
HUP0204544A3 (en)	2007-05-02
ATE463576T1 (de)	2010-04-15
KR20070092329A (ko)	2007-09-12
US7927852B2 (en)	2011-04-19
RU2009104003A (ru)	2010-08-20
EP1254237A2 (fr)	2002-11-06
HK1144701A1 (en)	2011-03-04
BE2013C045I2 (fr)	2020-06-24
HUP0204544A2 (en)	2003-05-28
CY2013028I1 (el)	2015-11-04
RU2352354C2 (ru)	2009-04-20
EP2305819B1 (fr)	2014-11-12
HK1143989A1 (en)	2011-01-21
IL193365A0 (en)	2009-02-11
AU2001249975B2 (en)	2006-06-08
LU92237I2 (fr)	2013-09-03
DE60141742D1 (de)	2010-05-20
ES2524153T3 (es)	2014-12-04
US20110287466A1 (en)	2011-11-24
TW200914617A (en)	2009-04-01

Publication	Publication Date	Title
AU2001249975B2 (en)	2006-06-08	Aggregate-free urate oxidase for preparation of non-immunogenic polymer conjugates
US20180223263A1 (en)	2018-08-09	Aggregate-free urate oxidase for preparation of non-immunogenic polymer conjugates
AU2001249975A1 (en)	2001-11-01	Aggregate-free urate oxidase for preparation of non-immunogenic polymer conjugates
AU2006203252B2 (en)	2009-06-04	Aggregate-free urate oxidase for preparation of non-immunogenic polymer conjugates
HK1155203B (en)	2015-09-25	Conjugates prepared with aggregate-free proteins
HK1143989B (en)	2015-08-14	Conjugates prepared with aggregate-free proteins
HK1155080A (en)	2012-05-11	Isolated tetrameric uricase
HK1141738B (en)	2013-11-22	Peg-urate oxidase conjugates and use thereof