NO300505B1 - hGPIIb kryptisk determinant polypeptidanalog og antistoffer som inhiberer blodplateadhesjon, samt hybridomer som produserer antistoffene, diagnostisk system i settform og anvendelser av antistoffene - Google Patents
hGPIIb kryptisk determinant polypeptidanalog og antistoffer som inhiberer blodplateadhesjon, samt hybridomer som produserer antistoffene, diagnostisk system i settform og anvendelser av antistoffene Download PDFInfo
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- NO300505B1 NO300505B1 NO890981A NO890981A NO300505B1 NO 300505 B1 NO300505 B1 NO 300505B1 NO 890981 A NO890981 A NO 890981A NO 890981 A NO890981 A NO 890981A NO 300505 B1 NO300505 B1 NO 300505B1
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- gpiib
- polypeptide
- iiia
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Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
- C07K16/2839—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against the integrin superfamily
-
- 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
- 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
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
- C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
- C07K14/4702—Regulators; Modulating activity
- C07K14/4703—Inhibitors; Suppressors
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
- G01N33/566—Immunoassay; Biospecific binding assay; Materials therefor using specific carrier or receptor proteins as ligand binding reagents where possible specific carrier or receptor proteins are classified with their target compounds
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
- G01N33/569—Immunoassay; Biospecific binding assay; Materials therefor for microorganisms, e.g. protozoa, bacteria, viruses
- G01N33/56966—Animal cells
- G01N33/56972—White blood cells
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
- C07K2317/34—Identification of a linear epitope shorter than 20 amino acid residues or of a conformational epitope defined by amino acid residues
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S436/00—Chemistry: analytical and immunological testing
- Y10S436/811—Test for named disease, body condition or organ function
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Immunology (AREA)
- Molecular Biology (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Hematology (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Cell Biology (AREA)
- Biomedical Technology (AREA)
- Urology & Nephrology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Analytical Chemistry (AREA)
- Biotechnology (AREA)
- Pathology (AREA)
- General Physics & Mathematics (AREA)
- Physics & Mathematics (AREA)
- Food Science & Technology (AREA)
- Microbiology (AREA)
- Zoology (AREA)
- Toxicology (AREA)
- Virology (AREA)
- Gastroenterology & Hepatology (AREA)
- Tropical Medicine & Parasitology (AREA)
- Animal Behavior & Ethology (AREA)
- Veterinary Medicine (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Pharmacology & Pharmacy (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Chemical & Material Sciences (AREA)
- Public Health (AREA)
- Diabetes (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Applications Claiming Priority (3)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US7095387A | 1987-07-08 | 1987-07-08 | |
US07/175,342 US5114842A (en) | 1987-07-08 | 1988-03-31 | Peptides and antibodies that inhibit platelet adhesion |
PCT/US1988/002312 WO1989000200A1 (en) | 1987-07-08 | 1988-07-08 | Peptides and antibodies that inhibit platelet adhesion |
Publications (3)
Publication Number | Publication Date |
---|---|
NO890981D0 NO890981D0 (no) | 1989-03-07 |
NO890981L NO890981L (no) | 1989-05-05 |
NO300505B1 true NO300505B1 (no) | 1997-06-09 |
Family
ID=26751678
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
NO890981A NO300505B1 (no) | 1987-07-08 | 1989-03-07 | hGPIIb kryptisk determinant polypeptidanalog og antistoffer som inhiberer blodplateadhesjon, samt hybridomer som produserer antistoffene, diagnostisk system i settform og anvendelser av antistoffene |
Country Status (9)
Country | Link |
---|---|
US (4) | US5114842A (de) |
EP (1) | EP0326595B1 (de) |
JP (3) | JP3184878B2 (de) |
AT (1) | ATE128183T1 (de) |
DE (1) | DE3854496T2 (de) |
DK (1) | DK175655B1 (de) |
FI (1) | FI105276B (de) |
NO (1) | NO300505B1 (de) |
WO (1) | WO1989000200A1 (de) |
Families Citing this family (70)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US5800815A (en) * | 1903-05-05 | 1998-09-01 | Cytel Corporation | Antibodies to P-selectin and their uses |
US5114842A (en) * | 1987-07-08 | 1992-05-19 | The Scripps Research Institute | Peptides and antibodies that inhibit platelet adhesion |
US5306620A (en) * | 1987-07-08 | 1994-04-26 | The Scripps Research Institute | Antibodies that bind to a ligand-induced binding site on integrin and induce integrin activation |
US5827821A (en) * | 1987-12-10 | 1998-10-27 | The Burnham Institute | Conformationally stabilized cell adhesion peptides |
AU639409B2 (en) * | 1987-12-10 | 1993-07-29 | La Jolla Cancer Research Foundation | Conformationally stabilized cell adhesion peptides |
US5770198A (en) * | 1988-05-18 | 1998-06-23 | The Research Foundation Of The State Of New York | Platelet-specific chimeric 7E3 immunoglobulin |
US5877275A (en) * | 1988-06-28 | 1999-03-02 | The General Hospital Corporation | Controlling cellular immune/inflammatory responses with β2 integrins |
US5204445A (en) * | 1988-10-03 | 1993-04-20 | The Scripps Research Institute | Peptides and antibodies that inhibit integrin-ligand binding |
ES2176174T3 (es) * | 1988-12-22 | 2002-12-01 | Genentech Inc | Procedimiento de preparacion de polipeptidos solubles en agua. |
US5378464A (en) * | 1989-03-08 | 1995-01-03 | Board Of Regents Of The University Of Oklahoma | Modulation of inflammatory responses by administration of GMP-140 or antibody to GMP-140 |
US5464778A (en) * | 1989-03-08 | 1995-11-07 | Board Of Regents Of The University Of Oklahoma | Glycoprotein ligand for P-selectin and methods of use thereof |
US5498694A (en) * | 1989-05-25 | 1996-03-12 | La Jolla Cancer Research Foundation | Peptides of the cytoplasmic domain of integrin |
US5384309A (en) * | 1989-07-17 | 1995-01-24 | Genentech, Inc. | Cyclized peptides and their use as platelet aggregation inhibitors |
WO1991001380A1 (fr) * | 1989-07-25 | 1991-02-07 | Institut National De La Sante Et De La Recherche Medicale | Anticorps monoclonaux diriges contre des proteines impliquees dans les fonctions plaquettaires, leur application en tant qu'agent diagnostique et therapeutique |
FR2650186B1 (fr) * | 1989-07-25 | 1992-02-28 | Inst Nat Sante Rech Med | Anticorps monoclonaux diriges contre des proteines impliquees dans les fonctions plaquettaires. leur application en tant qu'agent diagnostique et therapeutique |
US5196511A (en) * | 1989-12-01 | 1993-03-23 | The Scripps Research Institute | Peptides and antibodies that inhibit integrin-ligand binding |
US5780303A (en) * | 1990-04-06 | 1998-07-14 | La Jolla Cancer Research Foundation | Method and composition for treating thrombosis |
US5612311A (en) * | 1990-04-06 | 1997-03-18 | La Jolla Cancer Research Foundation | Method and composition for treating thrombosis |
US6521594B1 (en) | 1990-04-06 | 2003-02-18 | La Jolla Cancer Research Foundation | Method and composition for treating thrombosis |
US5648330A (en) * | 1990-04-06 | 1997-07-15 | La Jolla Cancer Research Foundation | Method and composition for treating vascular graft occlusion |
US5672585A (en) * | 1990-04-06 | 1997-09-30 | La Jolla Cancer Research Foundation | Method and composition for treating thrombosis |
AU660926B2 (en) * | 1990-04-06 | 1995-07-13 | La Jolla Cancer Research Foundation | Method and composition for treating thrombosis |
US5196309A (en) * | 1990-11-15 | 1993-03-23 | The Scripps Research Institute | Characterization of platelet aggregation disorders |
US6124267A (en) * | 1991-02-05 | 2000-09-26 | Southpac Trust Internationals, Inc. | O-glycan inhibitors of selectin mediated inflammation derived from PSGL-1 |
US6309639B1 (en) | 1991-02-05 | 2001-10-30 | The Board Of Regents Of The University Of Oklahoma | Method for inhibiting an inflammatory response using antibodies to P-selectin glycoprotein ligand |
US5645815A (en) * | 1991-02-08 | 1997-07-08 | Diatide, Inc. | Radiolabled compounds for thrombus imaging |
AU666853B2 (en) * | 1991-04-05 | 1996-02-29 | Genentech Inc. | Platelet aggregation inhibitors having high specificity for GP IIbIIIa |
CA2102115C (en) * | 1991-04-30 | 2009-04-07 | Mark H. Ginsberg | In vitro methods for determining in vivo thrombotic events |
US6033667A (en) * | 1992-05-05 | 2000-03-07 | Cytel Corporation | Method for detecting the presence of P-selectin |
US5681699A (en) * | 1994-02-11 | 1997-10-28 | Cedars-Sinai Medical Center | Methods of diagnosing ulcerative colitis and Crohn's disease |
US6884590B1 (en) | 1994-02-11 | 2005-04-26 | Cedars-Sinai Medical Center | Methods of screening for ulcerative colitis and crohn's disease |
US5763199A (en) * | 1994-09-29 | 1998-06-09 | Mount Sinai School Of Medicine Of The City University Of New York | Platelet blockade assay |
US5817748A (en) * | 1995-03-17 | 1998-10-06 | The Research Foundation Of State University Of New York | Mimotopes of human Platelet glycoprotein Ib/IX |
US5877155A (en) * | 1995-03-17 | 1999-03-02 | The Research Foundation Of State University Of New York | Mimotopes and anti-mimotopes of human platelet glycoprotein Ib/IX |
US7074888B1 (en) | 1995-03-17 | 2006-07-11 | The Research Foundation Of State University Of New York | Mimotopes and anti-mimotopes of human platelet glycoprotein Ib/IX |
US5817768A (en) * | 1995-06-07 | 1998-10-06 | The New York Blood Center, Inc. | Monospecific antibodies against a subunit of fibrinogen |
AU4815397A (en) * | 1996-10-15 | 1998-05-11 | Vanderbilt University | Method of disrupting cellular adhesion |
US5922551A (en) * | 1997-03-20 | 1999-07-13 | Accumetrics, Inc. | Agglutrimetric platelet binding assays in blood |
FR2764388B1 (fr) * | 1997-06-06 | 1999-08-27 | Biocytex | Nouvelle methode d'analyse des recepteurs plaquettaires gpiib/iiia |
US6184206B1 (en) * | 1997-09-03 | 2001-02-06 | The Burnham Institute | Integrin ligand dissociators |
US6210904B1 (en) | 1997-10-14 | 2001-04-03 | Merck & Co., Inc. | Anticoagulant test |
AU1082699A (en) * | 1997-10-14 | 1999-05-03 | Merck & Co., Inc. | Anticoagulant test |
US6623981B2 (en) | 1998-01-27 | 2003-09-23 | Bristol-Myers Squibb Company | Detection of patients at risk for developing integrin antagonist/agonist mediated disease states |
WO2000024781A1 (en) * | 1998-10-23 | 2000-05-04 | The Brigham And Women's Hospital, Inc. | Conformation-specific anti-von willebrand factor antibodies |
CA2397344C (en) | 1999-12-21 | 2011-03-15 | Bioenergy Inc. | Compositions for the storage of platelets |
WO2002046769A2 (en) * | 2000-12-05 | 2002-06-13 | The Penn State Research Foundation | A monoclonal antibody-based diagnostic assay for gamma fibrinogen |
US20040229205A1 (en) * | 2003-05-16 | 2004-11-18 | Ericson Daniel G. | Compositions for the storage of platelets |
WO2005007868A2 (en) | 2003-07-08 | 2005-01-27 | Accumetrics, Inc. | Controlled platelet activation to monitor therapy of adp antagonists |
US20070243632A1 (en) * | 2003-07-08 | 2007-10-18 | Coller Barry S | Methods for measuring platelet reactivity of patients that have received drug eluting stents |
CN1901795B (zh) | 2003-10-22 | 2014-03-26 | 弗雷德哈钦森癌症研究中心 | 用于在细胞,组织,器官,和有机体中诱导停滞的方法,组合物和装置 |
EP2270512B1 (de) * | 2004-12-08 | 2016-03-23 | Cedars-Sinai Medical Center | Verfahren zur Diagnose von Morbus Crohn |
AU2006236150A1 (en) * | 2005-04-20 | 2006-10-26 | Fred Hutchinson Cancer Research Center | Methods, compositions and articles of manufacture for enhancing survivability of cells, tissues, organs, and organisms |
EP1906990B1 (de) * | 2005-07-05 | 2013-12-11 | Baker Medical Research Institute | Antikoagulationsmittel |
US20080015145A1 (en) * | 2006-07-11 | 2008-01-17 | Maria Gyongyossy-Issa | Mimotope receptors and inhibitors for platelet-platelet and platelet-endothelium interactions |
US20100021917A1 (en) * | 2007-02-14 | 2010-01-28 | Cedars-Sinai Medical Center | Methods of using genes and genetic variants to predict or diagnose inflammatory bowel disease |
US20100190162A1 (en) * | 2007-02-26 | 2010-07-29 | Cedars-Sinai Medical Center | Methods of using single nucleotide polymorphisms in the tl1a gene to predict or diagnose inflammatory bowel disease |
WO2010039931A2 (en) * | 2008-10-01 | 2010-04-08 | Cedars-Sinai Medical Center | Methods of using il17rd and il23-il17 pathway genes to diagnose crohn's disease |
WO2008137762A2 (en) * | 2007-05-04 | 2008-11-13 | Cedars-Sinai Medical Center | Methods of diagnosis and treatment of crohn's disease |
US8486640B2 (en) | 2007-03-21 | 2013-07-16 | Cedars-Sinai Medical Center | Ileal pouch-anal anastomosis (IPAA) factors in the treatment of inflammatory bowel disease |
US20100184050A1 (en) * | 2007-04-26 | 2010-07-22 | Cedars-Sinai Medical Center | Diagnosis and treatment of inflammatory bowel disease in the puerto rican population |
EP2170356A1 (de) | 2007-06-25 | 2010-04-07 | Fred Hutchinson Cancer Research Center | Polychalcogenid-zusammensetzungen betreffende verfahren und zusammensetzungen |
US20110189685A1 (en) * | 2008-10-22 | 2011-08-04 | Cedars-Sinai Medical Center | Methods of using jak3 genetic variants to diagnose and predict crohn's disease |
US20110229471A1 (en) | 2008-11-26 | 2011-09-22 | Cedars-Sinai Medical Center | Methods of determining responsiveness to anti-tnf alpha therapy in inflammatory bowel disease |
WO2010075579A2 (en) | 2008-12-24 | 2010-07-01 | Cedars-Sinai Medical Center | Methods of predicting medically refractive ulcerative colitis (mr-uc) requiring colectomy |
KR20210157418A (ko) | 2013-03-27 | 2021-12-28 | 세다르스-신나이 메디칼 센터 | Tl1a 기능 및 관련된 신호전달 경로의 저해에 의한 섬유증 및 염증의 완화 및 반전 |
EP4105236A1 (de) | 2013-07-19 | 2022-12-21 | Cedars-Sinai Medical Center | Anti-tl1a (tnfsf15) antikörper zur behandlung von entzündlichen darmerkrankungen |
EP3430172A4 (de) | 2016-03-17 | 2019-08-21 | Cedars-Sinai Medical Center | Verfahren zur diagnose einer entzündlichen darmerkrankung durch rnaset2 |
WO2018170132A1 (en) | 2017-03-14 | 2018-09-20 | University Of Connecticut | Biodegradable pressure sensor |
US11826495B2 (en) | 2019-03-01 | 2023-11-28 | University Of Connecticut | Biodegradable piezoelectric ultrasonic transducer system |
US11745001B2 (en) | 2020-03-10 | 2023-09-05 | University Of Connecticut | Therapeutic bandage |
Family Cites Families (6)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US4421735A (en) * | 1980-04-17 | 1983-12-20 | The Massachusetts General Hospital | Radiolabeled diagnostic compositions and method for making the same |
US4427646A (en) * | 1981-04-02 | 1984-01-24 | Research Corporation | Use of radiolabeled peptide derived from crosslinked fibrin to locate thrombi in vivo |
DE3364347D1 (en) * | 1982-04-09 | 1986-08-07 | Fujirebio Kk | Anti immune complex antibody and preparation thereof |
US4454106A (en) * | 1982-06-07 | 1984-06-12 | Gansow Otto A | Use of metal chelate conjugated monoclonal antibodies |
CA1297816C (en) * | 1985-06-14 | 1992-03-24 | Barry S. Coller | Platelet function inhibiting monoclonal antibody fragment |
US5114842A (en) * | 1987-07-08 | 1992-05-19 | The Scripps Research Institute | Peptides and antibodies that inhibit platelet adhesion |
-
1988
- 1988-03-31 US US07/175,342 patent/US5114842A/en not_active Expired - Lifetime
- 1988-07-08 JP JP50642788A patent/JP3184878B2/ja not_active Expired - Lifetime
- 1988-07-08 AT AT88906651T patent/ATE128183T1/de not_active IP Right Cessation
- 1988-07-08 DE DE3854496T patent/DE3854496T2/de not_active Expired - Lifetime
- 1988-07-08 EP EP88906651A patent/EP0326595B1/de not_active Expired - Lifetime
- 1988-07-08 WO PCT/US1988/002312 patent/WO1989000200A1/en active IP Right Grant
-
1989
- 1989-03-07 FI FI891078A patent/FI105276B/fi active IP Right Grant
- 1989-03-07 DK DK198901101A patent/DK175655B1/da not_active IP Right Cessation
- 1989-03-07 NO NO890981A patent/NO300505B1/no not_active IP Right Cessation
- 1989-10-05 US US07/417,565 patent/US5284751A/en not_active Expired - Lifetime
-
1992
- 1992-05-15 US US07/883,669 patent/US5498499A/en not_active Expired - Fee Related
-
1993
- 1993-10-04 US US08/131,320 patent/US5470738A/en not_active Expired - Lifetime
-
1998
- 1998-03-04 JP JP05192998A patent/JP3541122B2/ja not_active Expired - Lifetime
-
2000
- 2000-11-16 JP JP2000349824A patent/JP3420747B2/ja not_active Expired - Lifetime
Also Published As
Publication number | Publication date |
---|---|
US5284751A (en) | 1994-02-08 |
WO1989000200A1 (en) | 1989-01-12 |
DK110189A (da) | 1989-05-08 |
DE3854496D1 (de) | 1995-10-26 |
JP3541122B2 (ja) | 2004-07-07 |
US5114842A (en) | 1992-05-19 |
FI891078A (fi) | 1989-03-07 |
FI105276B (fi) | 2000-07-14 |
US5498499A (en) | 1996-03-12 |
NO890981D0 (no) | 1989-03-07 |
EP0326595B1 (de) | 1995-09-20 |
NO890981L (no) | 1989-05-05 |
JP3420747B2 (ja) | 2003-06-30 |
DE3854496T2 (de) | 1996-06-13 |
DK110189D0 (da) | 1989-03-07 |
JP2001190287A (ja) | 2001-07-17 |
DK175655B1 (da) | 2005-01-10 |
ATE128183T1 (de) | 1995-10-15 |
JPH10276778A (ja) | 1998-10-20 |
JP3184878B2 (ja) | 2001-07-09 |
EP0326595A1 (de) | 1989-08-09 |
EP0326595A4 (en) | 1990-09-05 |
JPH02500085A (ja) | 1990-01-18 |
US5470738A (en) | 1995-11-28 |
FI891078A0 (fi) | 1989-03-07 |
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Legal Events
Date | Code | Title | Description |
---|---|---|---|
MK1K | Patent expired |