IL117320A - PROCESS FOR PURIFYING APOLIPOPROTEINS ApoA AND ApoE OR MIXTURES THEREOF, SUBSTANTIALLY ENDOTOXIN-FREE ApoA OR ApoE PRODUCED BY THIS PROCESS AND THE USE OF APOLIPOPROTEINS PRODUCED BY THIS PROCESS IN THE PREPARATION OF A MEDICAMENT - Google Patents
PROCESS FOR PURIFYING APOLIPOPROTEINS ApoA AND ApoE OR MIXTURES THEREOF, SUBSTANTIALLY ENDOTOXIN-FREE ApoA OR ApoE PRODUCED BY THIS PROCESS AND THE USE OF APOLIPOPROTEINS PRODUCED BY THIS PROCESS IN THE PREPARATION OF A MEDICAMENTInfo
- Publication number
- IL117320A IL117320A IL11732096A IL11732096A IL117320A IL 117320 A IL117320 A IL 117320A IL 11732096 A IL11732096 A IL 11732096A IL 11732096 A IL11732096 A IL 11732096A IL 117320 A IL117320 A IL 117320A
- Authority
- IL
- Israel
- Prior art keywords
- apoa
- apoe
- matrix
- endotoxins
- process according
- Prior art date
Links
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- 229930003231 vitamin Natural products 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/775—Apolipopeptides
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Biophysics (AREA)
- Genetics & Genomics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- Gastroenterology & Hepatology (AREA)
- Zoology (AREA)
- Toxicology (AREA)
- Heart & Thoracic Surgery (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Veterinary Medicine (AREA)
- Animal Behavior & Ethology (AREA)
- Cardiology (AREA)
- Pharmacology & Pharmacy (AREA)
- Public Health (AREA)
- General Chemical & Material Sciences (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Engineering & Computer Science (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicinal Preparation (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| SE9500778A SE9500778D0 (sv) | 1995-03-03 | 1995-03-03 | Process for producing a protein |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| IL117320A0 IL117320A0 (en) | 1996-06-18 |
| IL117320A true IL117320A (en) | 2001-06-14 |
Family
ID=20397430
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| IL11732096A IL117320A (en) | 1995-03-03 | 1996-02-29 | PROCESS FOR PURIFYING APOLIPOPROTEINS ApoA AND ApoE OR MIXTURES THEREOF, SUBSTANTIALLY ENDOTOXIN-FREE ApoA OR ApoE PRODUCED BY THIS PROCESS AND THE USE OF APOLIPOPROTEINS PRODUCED BY THIS PROCESS IN THE PREPARATION OF A MEDICAMENT |
Country Status (15)
| Country | Link |
|---|---|
| US (3) | US5834596A (de) |
| EP (1) | EP0813541B1 (de) |
| JP (1) | JPH11501046A (de) |
| AT (1) | ATE240348T1 (de) |
| AU (1) | AU694623B2 (de) |
| CA (1) | CA2212125A1 (de) |
| DE (1) | DE69628148T2 (de) |
| DK (1) | DK0813541T3 (de) |
| ES (1) | ES2199284T3 (de) |
| IL (1) | IL117320A (de) |
| NZ (1) | NZ303325A (de) |
| PT (1) | PT813541E (de) |
| SE (1) | SE9500778D0 (de) |
| WO (1) | WO1996027608A1 (de) |
| ZA (1) | ZA961679B (de) |
Families Citing this family (56)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| SE9500778D0 (sv) * | 1995-03-03 | 1995-03-03 | Pharmacia Ab | Process for producing a protein |
| SE9603068D0 (sv) * | 1996-08-23 | 1996-08-23 | Pharmacia & Upjohn Ab | Process for purifying a protein |
| SE9603304D0 (sv) | 1996-09-11 | 1996-09-11 | Pharmacia & Upjohn Ab | Process for purifying a compound |
| SE9603303D0 (sv) | 1996-09-11 | 1996-09-11 | Pharmacia & Upjohn Ab | Process for purifying a protein |
| DE19859703B4 (de) * | 1998-12-23 | 2009-10-29 | Macherey, Nagel Gmbh & Co. Handelsgesellschaft | Verfahren zur Aufreinigung von Nukleinsäuren sowie Anionenaustauscher zur Durchführung dieses Verfahrens |
| BR0009520A (pt) | 1999-04-01 | 2002-06-11 | Esperion Therapeutics Inc | Composto, método para sintetizar o mesmo, composição, metódos para o tratramento ou prevenção, em um paciente, de doença cardiovascular, dislipidemia, dislipoproteinemia, distúrbio de metabolismo de glucose, doença de alzheimer, sìndrome x ou sìndrome metabólica, septicemia, distúrbio trombótico, distúrbio associado com receptor ativado por proliferador de peroxissoma, obesidade, pancreatite, hipertensão, doença renal, câncer, inflamação, impotência, para reduzir o teor de gordura de carne de gado bovino, e, para reduzir o teor de colesterol de ovos de aves |
| US8568766B2 (en) * | 2000-08-24 | 2013-10-29 | Gattadahalli M. Anantharamaiah | Peptides and peptide mimetics to treat pathologies associated with eye disease |
| JP4344136B2 (ja) | 2000-11-10 | 2009-10-14 | エフ・ホフマン−ラ・ロシュ・リミテッド | アポリポタンパク質類似体 |
| MXPA04002848A (es) * | 2001-09-28 | 2005-06-06 | Esperion Therapeutics Inc | Prevencion y tratamiento de restenosis por administracion local de medicamento. |
| US20030229062A1 (en) * | 2001-12-07 | 2003-12-11 | The Regents Of The University Of California | Treatments for age-related macular degeneration (AMD) |
| US7470659B2 (en) * | 2001-12-07 | 2008-12-30 | The Regents Of The University Of California | Methods to increase reverse cholesterol transport in the retinal pigment epithelium (RPE) and Bruch's membrane (BM) |
| EP1461028A4 (de) * | 2001-12-07 | 2007-07-25 | Univ California | Behandlung für altersbezogene makuladegeneration |
| NZ537006A (en) * | 2002-05-17 | 2008-01-31 | Esperion Therapeutics Inc | The use of apolipoprotein A-I Milano, for the manufacture ofa composition for treating preventing or reducing ischemic reperfusion injury in a tissue or organ |
| US7119221B2 (en) | 2003-01-23 | 2006-10-10 | Esperion Therapeutics, Inc. | Cycloalkyl-hydroxyl compounds and compositions for cholesterol management and related uses |
| TW200526778A (en) * | 2003-11-14 | 2005-08-16 | Sembiosys Genetics Inc | Methods for the production of apolipoproteins in transgenic plants |
| US20050176623A1 (en) * | 2004-02-11 | 2005-08-11 | Neil Wagle | Non-invasive treatment of disease using amphipathic compounds |
| EP1732383A4 (de) * | 2004-04-06 | 2007-05-02 | Cedars Sinai Medical Center | Vorbeugung und behandlung von gefässerkrankungen mit rekombinanten adeno assoziierten virusvektoren, die für apolipoprotein a-i und apolipoprotein a-i milano kodieren |
| KR100560102B1 (ko) * | 2004-06-25 | 2006-03-13 | 한국생명공학연구원 | 프로아포리포단백질 a-ⅰ 변이체와, 이를 포함하는고지혈증 또는 동맥경화증 예방 및 치료제 |
| NZ563187A (en) | 2005-04-29 | 2010-05-28 | Univ California | Peptides and peptide mimetics to treat pathologies characterized by an inflammatory response |
| US20080206142A1 (en) * | 2006-06-16 | 2008-08-28 | Lipid Sciences, Inc. | Novel Peptides That Promote Lipid Efflux |
| US20080199398A1 (en) * | 2006-06-16 | 2008-08-21 | Brewer H Bryan | Novel Peptides That Promote Lipid Efflux |
| US20080227686A1 (en) * | 2006-06-16 | 2008-09-18 | Lipid Sciences, Inc. | Novel Peptides that Promote Lipid Efflux |
| AU2007272494B2 (en) | 2006-07-14 | 2011-07-28 | Wisconsin Alumni Research Foundation | Adsorptive membranes for trapping viruses |
| AU2007284801A1 (en) | 2006-08-08 | 2008-02-21 | The Regents Of The University Of Californina | Salicylanilides enhance oral delivery of therapeutic peptides |
| US20080138284A1 (en) * | 2006-09-26 | 2008-06-12 | Lipid Sciences, Inc. | Novel Peptides That Promote Lipid Efflux |
| CN100586958C (zh) * | 2006-12-20 | 2010-02-03 | 上海莱士血液制品股份有限公司 | 高纯度载脂蛋白a-i的制备方法 |
| US8013122B2 (en) * | 2006-12-20 | 2011-09-06 | Kieu Hoang | Method of purifying apolipoprotein A-1 |
| WO2009032693A2 (en) | 2007-08-28 | 2009-03-12 | Uab Research Foundation | Synthetic apolipoprotein e mimicking polypeptides and methods of use |
| CA2697957A1 (en) | 2007-08-28 | 2009-03-12 | Uab Research Foundation | Synthetic apolipoprotein e mimicking polypeptides and methods of use |
| WO2010054406A1 (en) | 2008-11-10 | 2010-05-14 | Alnylam Pharmaceuticals, Inc. | Novel lipids and compositions for the delivery of therapeutics |
| WO2010088537A2 (en) | 2009-01-29 | 2010-08-05 | Alnylam Pharmaceuticals, Inc. | Improved lipid formulation |
| JP6032724B2 (ja) | 2009-03-12 | 2016-11-30 | アルナイラム ファーマシューティカルズ, インコーポレイテッドAlnylam Pharmaceuticals, Inc. | 脂質製剤組成物およびEg5遺伝子とVEGF遺伝子の発現を阻害する方法 |
| NZ711583A (en) | 2009-05-05 | 2017-03-31 | Arbutus Biopharma Corp | Lipid compositions |
| KR102066189B1 (ko) | 2009-06-10 | 2020-01-14 | 알닐람 파마슈티칼스 인코포레이티드 | 향상된 지질 조성물 |
| US9029338B2 (en) | 2009-08-14 | 2015-05-12 | Alnylam Pharmaceuticals, Inc. | Lipid formulated compositions and methods for inhibiting expression of a gene from the ebola virus |
| EP2509636B1 (de) | 2009-12-07 | 2017-07-19 | Arbutus Biopharma Corporation | Zusammensetzungen für nukleinsäurefreisetzung |
| NZ600725A (en) | 2009-12-18 | 2015-08-28 | Univ British Colombia | Methods and compositions for delivery of nucleic acids |
| WO2011139911A2 (en) | 2010-04-29 | 2011-11-10 | Isis Pharmaceuticals, Inc. | Lipid formulated single stranded rna |
| WO2011143362A1 (en) | 2010-05-11 | 2011-11-17 | Esperion Therapeutics, Inc. | Dimeric oxidation-resistant apolipoprotein a1 variants |
| SG186085A1 (en) | 2010-06-03 | 2013-01-30 | Alnylam Pharmaceuticals Inc | Biodegradable lipids for the delivery of active agents |
| US20130202652A1 (en) | 2010-07-30 | 2013-08-08 | Alnylam Pharmaceuticals, Inc. | Methods and compositions for delivery of active agents |
| WO2012016184A2 (en) | 2010-07-30 | 2012-02-02 | Alnylam Pharmaceuticals, Inc. | Methods and compositions for delivery of active agents |
| US9339513B2 (en) | 2010-11-09 | 2016-05-17 | Alnylam Pharmaceuticals, Inc. | Lipid formulated compositions and methods for inhibiting expression of Eg5 and VEGF genes |
| US9999673B2 (en) | 2011-01-11 | 2018-06-19 | Alnylam Pharmaceuticals, Inc. | PEGylated lipids and their use for drug delivery |
| HUE042314T2 (hu) | 2011-02-07 | 2019-06-28 | Cerenis Therapeutics Holding Sa | Lipoprotein komplexek és azok gyártása és alkalmazásai |
| WO2013049328A1 (en) | 2011-09-27 | 2013-04-04 | Alnylam Pharmaceuticals, Inc. | Di-aliphatic substituted pegylated lipids |
| KR102069395B1 (ko) | 2011-12-12 | 2020-01-22 | 멜리어 파마슈티칼스 아이, 인코포레이티드 | 제i형 및 제ii형 당뇨병의 치료 |
| WO2013180650A1 (en) | 2012-05-31 | 2013-12-05 | Agency For Science, Technology And Research | Methods for reducing levels of protein-contaminant complexes and aggregates in protein preparations by treatment with electropositive organic additives |
| US9610324B2 (en) | 2012-07-11 | 2017-04-04 | Esperion Therapeutics, Inc. | Apolipoprotein mixtures |
| BR112016025470A2 (pt) | 2014-05-02 | 2017-08-15 | Cerenis Therapeutics Holding S A | ?hdl terapêutico? |
| WO2016018665A1 (en) | 2014-07-31 | 2016-02-04 | Uab Research Foundation | Apoe mimetic peptides and higher potency to clear plasma cholesterol |
| KR102370582B1 (ko) | 2015-03-13 | 2022-03-04 | 에스페리온 테라피유틱스 인코포레이티드 | Etc1002 및 에제티미브를 포함하는 고정 용량 조합 및 제형 및 심혈관 질환의 치료 또는 이의 위험의 감소 방법 |
| MA41793A (fr) | 2015-03-16 | 2018-01-23 | Esperion Therapeutics Inc | Associations de doses fixes comprenant du etc1002 et une ou plusieurs statines permettant de traiter ou de réduire un risque cardiovasculaire |
| CN107033237B (zh) * | 2017-05-11 | 2021-07-20 | 深圳市卫光生物制品股份有限公司 | 一种人血浆载脂蛋白a-i的分离纯化方法 |
| JP2022537049A (ja) | 2019-06-21 | 2022-08-23 | エスペリオン・セラピューティクス・インコーポレイテッド | ベンペド酸の製造方法及びその組成物 |
| CA3188232A1 (en) * | 2020-08-10 | 2022-02-17 | Kushee-Nidhi Kush KUMAR | Antifungal matrix formed from peptide hydrogels |
Family Cites Families (28)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS6196998A (ja) | 1984-10-16 | 1986-05-15 | Mitsubishi Chem Ind Ltd | ヒトアポリポプロテインa−i様蛋白の産生方法 |
| AU587989B2 (en) * | 1984-10-16 | 1989-09-07 | Mitsubishi Chemical Corporation | DMA fragments, expression vectors, proteins, hosts, and process for production of the proteins |
| SE462100B (sv) * | 1985-08-08 | 1990-05-07 | Perstorp Ab | Komposition och dess anvaendning i ett tvaa- eller flerfassystem |
| EP0262651A3 (de) * | 1986-09-30 | 1990-06-20 | Union Carbide Corporation | Isolierung von Enzymen aus einer Lösung |
| GB8625435D0 (en) * | 1986-10-23 | 1986-11-26 | Erba Farmitalia | Human apolipoprotein ai |
| US5128318A (en) * | 1987-05-20 | 1992-07-07 | The Rogosin Institute | Reconstituted HDL particles and uses thereof |
| GB8712540D0 (en) * | 1987-05-28 | 1987-07-01 | Ucb Sa | Expression of human proapolipoprotein a-i |
| JP2606228B2 (ja) * | 1987-09-18 | 1997-04-30 | 三菱化学株式会社 | ヒトプロアポリポプロテインa−i様蛋白の産生法 |
| JP2561674B2 (ja) | 1987-10-06 | 1996-12-11 | 三菱化学株式会社 | 蛋白質の産生方法 |
| CA1335077C (en) * | 1988-02-08 | 1995-04-04 | Henri Isliker | Process for the manufacture of apolipoproteins from human blood plasma or serum |
| JPH01238534A (ja) * | 1988-03-17 | 1989-09-22 | Mitsui Toatsu Chem Inc | エンドトキシンの除去方法 |
| EP0345155B1 (de) * | 1988-05-31 | 1994-08-10 | Mitsubishi Kasei Corporation | Verfahren zur Herstellung von Proteinen, die ähnlich dem natürlich-menschlichen Apolipoprotein-E sind |
| DE3819463A1 (de) * | 1988-06-08 | 1989-12-14 | Behringwerke Ag | Expressionsvektoren zur herstellung unfusionierter proteine in mikroorganismen |
| IT1229996B (it) * | 1989-04-20 | 1991-09-20 | Cesare Sirtori | Espressione di apolipoproteina ai e apolipoproteina ai-milano in lievito e composizioni farmaceutiche che contengono dette apolipoproteine. |
| EP0497757B1 (de) * | 1989-10-31 | 1994-06-22 | Schering Corporation | Sekretorische e-coli-stämme |
| SE468881B (sv) * | 1991-01-09 | 1993-04-05 | Kabi Pharmacia Ab | Anvaendning av vissa foereningar foer framstaellning av laekemedel foer behandling av endotoxininducerade effekter samt saett att avlaegsna endotoxiner ur diverse loesningar |
| WO1993000443A1 (en) * | 1991-06-26 | 1993-01-07 | Bio-Technology General Corp. | Purification of recombinant apolipoprotein e from bacteria |
| SE9103701D0 (sv) * | 1991-12-13 | 1991-12-13 | Kabi Pharmacia Ab | Apolipoprotein |
| WO1993025581A1 (en) * | 1992-06-12 | 1993-12-23 | N.V. Innogenetics S.A. | New peptides and proteins, process for their preparation and their use as cholesterol acceptors |
| SE9203753D0 (sv) * | 1992-12-11 | 1992-12-11 | Kabi Pharmacia Ab | Expression system for producing apolipoprotein ai-m |
| JP3491917B2 (ja) * | 1993-02-05 | 2004-02-03 | メビオール株式会社 | 熱可逆性ハイドロゲル材料 |
| US5643757A (en) * | 1994-03-21 | 1997-07-01 | American Cyanamid Company | High yield production of human apolipoprotein A1 in E. coli. |
| JP3514514B2 (ja) * | 1994-06-14 | 2004-03-31 | 財団法人化学及血清療法研究所 | ヒト血漿からのアポリポ蛋白a−1の製造方法 |
| SE9500724D0 (sv) * | 1994-06-23 | 1995-02-24 | Pharmacia Ab | Filtrering |
| WO1996004556A1 (en) * | 1994-08-01 | 1996-02-15 | Hsu James T | Lipoprotein cholesterol assays |
| SE9500778D0 (sv) * | 1995-03-03 | 1995-03-03 | Pharmacia Ab | Process for producing a protein |
| US5672685A (en) * | 1995-10-04 | 1997-09-30 | Duke University | Source of apolipoprotein E and method of isolating apolipoprotein E |
| SE9603068D0 (sv) * | 1996-08-23 | 1996-08-23 | Pharmacia & Upjohn Ab | Process for purifying a protein |
-
1995
- 1995-03-03 SE SE9500778A patent/SE9500778D0/xx unknown
-
1996
- 1996-02-29 IL IL11732096A patent/IL117320A/en not_active IP Right Cessation
- 1996-03-01 JP JP8526799A patent/JPH11501046A/ja active Pending
- 1996-03-01 AU AU49607/96A patent/AU694623B2/en not_active Ceased
- 1996-03-01 DE DE69628148T patent/DE69628148T2/de not_active Expired - Fee Related
- 1996-03-01 PT PT96906136T patent/PT813541E/pt unknown
- 1996-03-01 EP EP96906136A patent/EP0813541B1/de not_active Expired - Lifetime
- 1996-03-01 CA CA002212125A patent/CA2212125A1/en not_active Abandoned
- 1996-03-01 DK DK96906136T patent/DK0813541T3/da active
- 1996-03-01 US US08/875,125 patent/US5834596A/en not_active Expired - Lifetime
- 1996-03-01 WO PCT/SE1996/000271 patent/WO1996027608A1/en not_active Ceased
- 1996-03-01 AT AT96906136T patent/ATE240348T1/de not_active IP Right Cessation
- 1996-03-01 NZ NZ303325A patent/NZ303325A/xx unknown
- 1996-03-01 ZA ZA961679A patent/ZA961679B/xx unknown
- 1996-03-01 ES ES96906136T patent/ES2199284T3/es not_active Expired - Lifetime
-
1998
- 1998-08-05 US US09/129,720 patent/US5990081A/en not_active Expired - Lifetime
-
1999
- 1999-11-22 US US09/444,816 patent/US6506879B1/en not_active Expired - Fee Related
Also Published As
| Publication number | Publication date |
|---|---|
| IL117320A0 (en) | 1996-06-18 |
| SE9500778D0 (sv) | 1995-03-03 |
| DE69628148T2 (de) | 2004-01-08 |
| ES2199284T3 (es) | 2004-02-16 |
| EP0813541B1 (de) | 2003-05-14 |
| DK0813541T3 (da) | 2003-09-15 |
| EP0813541A1 (de) | 1997-12-29 |
| ZA961679B (en) | 1996-10-07 |
| NZ303325A (en) | 1998-12-23 |
| CA2212125A1 (en) | 1996-09-12 |
| US5834596A (en) | 1998-11-10 |
| WO1996027608A1 (en) | 1996-09-12 |
| US6506879B1 (en) | 2003-01-14 |
| PT813541E (pt) | 2003-09-30 |
| AU694623B2 (en) | 1998-07-23 |
| JPH11501046A (ja) | 1999-01-26 |
| DE69628148D1 (de) | 2003-06-18 |
| ATE240348T1 (de) | 2003-05-15 |
| US5990081A (en) | 1999-11-23 |
| AU4960796A (en) | 1996-09-23 |
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Legal Events
| Date | Code | Title | Description |
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| FF | Patent granted | ||
| KB | Patent renewed | ||
| KB | Patent renewed | ||
| KB | Patent renewed | ||
| MM9K | Patent not in force due to non-payment of renewal fees |