BG106577A - Фибринолитично активен полипептид - Google Patents
Фибринолитично активен полипептид Download PDFInfo
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- BG106577A BG106577A BG106577A BG10657702A BG106577A BG 106577 A BG106577 A BG 106577A BG 106577 A BG106577 A BG 106577A BG 10657702 A BG10657702 A BG 10657702A BG 106577 A BG106577 A BG 106577A
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- polypeptide
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Classifications
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
-
- 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
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/64—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6421—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
- C12N9/6489—Metalloendopeptidases (3.4.24)
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- A61K38/1703—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P7/00—Drugs for disorders of the blood or the extracellular fluid
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P7/00—Drugs for disorders of the blood or the extracellular fluid
- A61P7/02—Antithrombotic agents; Anticoagulants; Platelet aggregation inhibitors
-
- 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
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/64—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6402—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from non-mammals
- C12N9/6418—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from non-mammals from snakes
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Organic Chemistry (AREA)
- Zoology (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Wood Science & Technology (AREA)
- Biomedical Technology (AREA)
- Biochemistry (AREA)
- Molecular Biology (AREA)
- Microbiology (AREA)
- Pharmacology & Pharmacy (AREA)
- Veterinary Medicine (AREA)
- General Engineering & Computer Science (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Biotechnology (AREA)
- Gastroenterology & Hepatology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Marine Sciences & Fisheries (AREA)
- Epidemiology (AREA)
- General Chemical & Material Sciences (AREA)
- Immunology (AREA)
- Hematology (AREA)
- Diabetes (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Biophysics (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Enzymes And Modification Thereof (AREA)
- Peptides Or Proteins (AREA)
- Materials For Medical Uses (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US09/411,329 US6261820B1 (en) | 1999-10-01 | 1999-10-01 | Fibronolytically active polypeptide |
| PCT/US2000/027029 WO2001025445A1 (en) | 1999-10-01 | 2000-09-29 | Fibrinolytically active polypeptide |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| BG106577A true BG106577A (bg) | 2003-04-30 |
Family
ID=23628486
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| BG106577A BG106577A (bg) | 1999-10-01 | 2002-04-04 | Фибринолитично активен полипептид |
Country Status (29)
| Country | Link |
|---|---|
| US (4) | US6261820B1 (cs) |
| EP (2) | EP1605049A3 (cs) |
| JP (1) | JP2003511034A (cs) |
| KR (2) | KR100700753B1 (cs) |
| CN (2) | CN101230340A (cs) |
| AT (1) | ATE292180T1 (cs) |
| AU (1) | AU767827B2 (cs) |
| BG (1) | BG106577A (cs) |
| BR (1) | BR0014414A (cs) |
| CA (1) | CA2386185A1 (cs) |
| CZ (1) | CZ298502B6 (cs) |
| DE (1) | DE60019147T2 (cs) |
| DK (1) | DK1224298T3 (cs) |
| EA (2) | EA006487B1 (cs) |
| ES (1) | ES2240167T3 (cs) |
| HK (1) | HK1049351B (cs) |
| HU (1) | HUP0202650A3 (cs) |
| IL (1) | IL148787A0 (cs) |
| MX (1) | MXPA02003126A (cs) |
| NO (1) | NO20021501L (cs) |
| NZ (1) | NZ517951A (cs) |
| PL (1) | PL355017A1 (cs) |
| PT (1) | PT1224298E (cs) |
| RS (1) | RS20060033A (cs) |
| SG (1) | SG127720A1 (cs) |
| SK (1) | SK4232002A3 (cs) |
| WO (1) | WO2001025445A1 (cs) |
| YU (2) | YU59604A (cs) |
| ZA (1) | ZA200202206B (cs) |
Families Citing this family (21)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6440414B1 (en) | 1999-10-01 | 2002-08-27 | Amgen Inc. | Pharmaceutical compositions of fibrinolytic agent |
| US6261820B1 (en) | 1999-10-01 | 2001-07-17 | Amgen Inc. | Fibronolytically active polypeptide |
| US7033776B2 (en) * | 1999-12-17 | 2006-04-25 | Amgen Inc. | Method for treatment of indwelling catheter occlusion using fibrinolytic metalloproteinases |
| US6455269B1 (en) * | 1999-12-17 | 2002-09-24 | Amgen, Inc. | Method for localized administration of fibrinolytic metalloproteinases |
| US6523647B2 (en) * | 2001-05-21 | 2003-02-25 | Hydro Mobile Inc. | Elevating platform assembly |
| EP1482882B1 (en) * | 2002-02-11 | 2011-09-14 | Gold-T Tech, Inc. | Implantable device for preventing thrombus formation |
| US7016409B2 (en) * | 2003-11-12 | 2006-03-21 | Sony Corporation | Apparatus and method for use in providing dynamic bit rate encoding |
| ES2239532B1 (es) * | 2004-02-06 | 2006-11-01 | Proyecto De Biomedicina Cima S.L. | Metodo para evaluar el riesgo y la predisposicion a desarrollar una patologia relacionada con la presencia de autoanticuerpos frente a epcr. |
| US20070141625A1 (en) * | 2005-02-03 | 2007-06-21 | Santos Jose H | Method for assessing risk of and predisposition to development of a pathology related to the presence of anti-epcr autoantibodies |
| EP1986568B1 (en) | 2006-02-03 | 2017-04-05 | Covidien LP | Methods and devices for restoring blood flow within blocked vasculature |
| WO2010102307A1 (en) | 2009-03-06 | 2010-09-10 | Lazarus Effect, Inc. | Retrieval systems and methods for use thereof |
| US10207240B2 (en) | 2009-11-03 | 2019-02-19 | Gen9, Inc. | Methods and microfluidic devices for the manipulation of droplets in high fidelity polynucleotide assembly |
| WO2012129363A2 (en) | 2011-03-24 | 2012-09-27 | President And Fellows Of Harvard College | Single cell nucleic acid detection and analysis |
| CN107873054B (zh) | 2014-09-09 | 2022-07-12 | 博德研究所 | 用于复合单细胞核酸分析的基于微滴的方法和设备 |
| US10456560B2 (en) | 2015-02-11 | 2019-10-29 | Covidien Lp | Expandable tip medical devices and methods |
| US11873483B2 (en) | 2015-03-11 | 2024-01-16 | The Broad Institute, Inc. | Proteomic analysis with nucleic acid identifiers |
| US11092607B2 (en) | 2015-10-28 | 2021-08-17 | The Board Institute, Inc. | Multiplex analysis of single cell constituents |
| WO2017075297A1 (en) | 2015-10-28 | 2017-05-04 | The Broad Institute Inc. | High-throughput dynamic reagent delivery system |
| US12071663B2 (en) | 2016-01-15 | 2024-08-27 | Massachusetts Institute Of Technology | Semi-permeable arrays for analyzing biological systems and methods of using same |
| US11072816B2 (en) | 2017-05-03 | 2021-07-27 | The Broad Institute, Inc. | Single-cell proteomic assay using aptamers |
| WO2022182799A1 (en) * | 2021-02-23 | 2022-09-01 | Clara Foods Co. | Compositions for preparing animal-free egg-like products |
Family Cites Families (35)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| FR2310133A2 (fr) * | 1975-05-05 | 1976-12-03 | Fabre Sa Pierre | Nouveau medicament comportant un activateur du plasminogene perfectionne |
| US4447236A (en) * | 1982-02-05 | 1984-05-08 | Cordis Corporation | Infusion catheter system |
| DE3330699A1 (de) * | 1983-08-25 | 1985-03-07 | Boehringer Mannheim Gmbh, 6800 Mannheim | Verfahren zur gleichzeitigen bestimmung von fibrinogen und fibrinogen-spaltprodukten im plasma |
| US4610879A (en) | 1984-01-06 | 1986-09-09 | University Of Southern California | Fibrinolytic enzyme from snake vernom |
| CA1237482A (en) * | 1984-03-09 | 1988-05-31 | Frank B. Stiles | Catheter for effecting removal of obstructions from a biological duct |
| US4755167A (en) * | 1984-04-10 | 1988-07-05 | Research Corporation | In vivo method for distribution and stirring of therapeutic agents |
| US4885242A (en) * | 1984-10-30 | 1989-12-05 | Phillips Petroleum Company | Genes from pichia histidine pathway and uses thereof |
| US4855231A (en) * | 1984-10-30 | 1989-08-08 | Phillips Petroleum Company | Regulatory region for heterologous gene expression in yeast |
| US4837148A (en) * | 1984-10-30 | 1989-06-06 | Phillips Petroleum Company | Autonomous replication sequences for yeast strains of the genus pichia |
| US4818700A (en) * | 1985-10-25 | 1989-04-04 | Phillips Petroleum Company | Pichia pastoris argininosuccinate lyase gene and uses thereof |
| US4812405A (en) * | 1986-02-18 | 1989-03-14 | Phillips Petroleum Company | Double auxotrophic mutants of Pichia pastoris and methods for preparation |
| US5000185A (en) * | 1986-02-28 | 1991-03-19 | Cardiovascular Imaging Systems, Inc. | Method for intravascular two-dimensional ultrasonography and recanalization |
| ZA889415B (en) | 1987-12-18 | 1989-09-27 | Chiron Corp | Compositions and method for recombinant production of crotalidus venum fibrolase |
| WO1990007352A1 (en) | 1989-01-04 | 1990-07-12 | Boston Scientific Corporation | Angioplasty catheter |
| US5222941A (en) * | 1990-01-12 | 1993-06-29 | Don Michael T Anthony | Method of dissolving an obstruction in a vessel |
| JPH05184352A (ja) * | 1990-01-16 | 1993-07-27 | Centro De Ing Genetica Y Biotecnol | ピヒア パストリス(Pichia pastoris)酵母中での異種遺伝子の発現方法、発現ベクターおよび形質転換微生物 |
| US5709676A (en) * | 1990-02-14 | 1998-01-20 | Alt; Eckhard | Synergistic treatment of stenosed blood vessels using shock waves and dissolving medication |
| US5250034A (en) * | 1990-09-17 | 1993-10-05 | E-Z-Em, Inc. | Pressure responsive valve catheter |
| US5167628A (en) * | 1991-05-02 | 1992-12-01 | Boyles Paul W | Aortic balloon catheter assembly for indirect infusion of the coronary arteries |
| US5380273A (en) * | 1992-05-19 | 1995-01-10 | Dubrul; Will R. | Vibrating catheter |
| EP0624642B1 (en) | 1993-05-12 | 1999-01-20 | Indian Council For Medical Research | Novel thrombolytic agent, process for preparing same and its use for the preparation of a thrombi dissolving medicament |
| US5370653A (en) * | 1993-07-22 | 1994-12-06 | Micro Therapeutics, Inc. | Thrombectomy method and apparatus |
| EP0689843B1 (en) | 1993-12-17 | 2003-09-10 | Mochida Pharmaceutical Co., Ltd. | Composition containing soluble thrombomodulins |
| US5626564A (en) * | 1995-03-31 | 1997-05-06 | Creighton University | Adjustable sideholes catheter |
| US5830468A (en) * | 1995-05-17 | 1998-11-03 | The New York Blood Center, Inc. | Fibrin(ogen) degradation by fibrinolytic matrix metalloproteinase |
| US6020181A (en) * | 1995-05-17 | 2000-02-01 | New York Blood, Inc. | Inhibition of thrombus formation by medical related apparatus comprising treating with fibrinolytic matrix metalloproteinase |
| US5741779A (en) * | 1996-05-10 | 1998-04-21 | Xoma Corporation | Antithrombotic materials and methods |
| DE69734060T2 (de) * | 1996-05-24 | 2006-06-29 | Angiotech Pharmaceuticals, Inc., Vancouver | Zubereitungen und verfahren zur behandlung oder prävention von krankheiten der körperpassagewege |
| US5951981A (en) * | 1996-12-02 | 1999-09-14 | Diatide, Inc. | Thrombolytic agents with antithrombotic activity |
| US6413760B1 (en) * | 1997-04-15 | 2002-07-02 | Genetics Institute, Inc. | Highly purified mocarhagin cobra venom protease polynucleotides endcoding same and related proteases and therapeutic uses thereof |
| WO1999029838A1 (en) * | 1997-12-09 | 1999-06-17 | Bristol-Myers Squibb Company | Fibrinogen-converting enzyme hybrids |
| US6261820B1 (en) | 1999-10-01 | 2001-07-17 | Amgen Inc. | Fibronolytically active polypeptide |
| US6440414B1 (en) | 1999-10-01 | 2002-08-27 | Amgen Inc. | Pharmaceutical compositions of fibrinolytic agent |
| US6455269B1 (en) * | 1999-12-17 | 2002-09-24 | Amgen, Inc. | Method for localized administration of fibrinolytic metalloproteinases |
| WO2002012283A2 (en) | 2000-08-03 | 2002-02-14 | Zymogenetics, Inc. | Disintegrin homologs, zsnk10, zsnk11, and zsnk12 |
-
1999
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