SE442022B - Urokinasderivat bestaende av urokinas bundet till fibrinogen - Google Patents
Urokinasderivat bestaende av urokinas bundet till fibrinogenInfo
- Publication number
- SE442022B SE442022B SE8500093A SE8500093A SE442022B SE 442022 B SE442022 B SE 442022B SE 8500093 A SE8500093 A SE 8500093A SE 8500093 A SE8500093 A SE 8500093A SE 442022 B SE442022 B SE 442022B
- Authority
- SE
- Sweden
- Prior art keywords
- urokinase
- fibrinogen
- derivatives
- compound
- bound
- Prior art date
Links
- 229940012952 fibrinogen Drugs 0.000 title claims description 46
- 108010049003 Fibrinogen Proteins 0.000 title claims description 44
- 102000008946 Fibrinogen Human genes 0.000 title claims description 44
- FBPFZTCFMRRESA-ZXXMMSQZSA-N D-iditol Chemical compound OC[C@@H](O)[C@H](O)[C@@H](O)[C@H](O)CO FBPFZTCFMRRESA-ZXXMMSQZSA-N 0.000 title 1
- 102000003990 Urokinase-type plasminogen activator Human genes 0.000 claims description 84
- 108090000435 Urokinase-type plasminogen activator Proteins 0.000 claims description 84
- 229960005356 urokinase Drugs 0.000 claims description 83
- 230000000694 effects Effects 0.000 claims description 18
- 230000003197 catalytic effect Effects 0.000 claims description 14
- QCVGEOXPDFCNHA-UHFFFAOYSA-N 5,5-dimethyl-2,4-dioxo-1,3-oxazolidine-3-carboxamide Chemical compound CC1(C)OC(=O)N(C(N)=O)C1=O QCVGEOXPDFCNHA-UHFFFAOYSA-N 0.000 claims description 10
- 102000002322 Egg Proteins Human genes 0.000 claims description 10
- 108010000912 Egg Proteins Proteins 0.000 claims description 10
- 235000014103 egg white Nutrition 0.000 claims description 10
- 210000000969 egg white Anatomy 0.000 claims description 10
- 108090000371 Esterases Proteins 0.000 claims description 8
- -1 aliphatic diamine Chemical class 0.000 claims description 8
- 150000001875 compounds Chemical class 0.000 description 20
- 239000000243 solution Substances 0.000 description 19
- 102000004190 Enzymes Human genes 0.000 description 18
- 108090000790 Enzymes Proteins 0.000 description 18
- 108010073385 Fibrin Proteins 0.000 description 18
- 229940088598 enzyme Drugs 0.000 description 17
- 102000009123 Fibrin Human genes 0.000 description 16
- BWGVNKXGVNDBDI-UHFFFAOYSA-N Fibrin monomer Chemical compound CNC(=O)CNC(=O)CN BWGVNKXGVNDBDI-UHFFFAOYSA-N 0.000 description 16
- 229950003499 fibrin Drugs 0.000 description 16
- 238000000034 method Methods 0.000 description 15
- 238000002360 preparation method Methods 0.000 description 15
- 230000002537 thrombolytic effect Effects 0.000 description 12
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 12
- 239000000203 mixture Substances 0.000 description 11
- 239000008055 phosphate buffer solution Substances 0.000 description 9
- 150000001718 carbodiimides Chemical class 0.000 description 7
- 239000012876 carrier material Substances 0.000 description 7
- 229940125898 compound 5 Drugs 0.000 description 7
- 239000012153 distilled water Substances 0.000 description 7
- 230000003480 fibrinolytic effect Effects 0.000 description 7
- 239000011159 matrix material Substances 0.000 description 7
- 208000007536 Thrombosis Diseases 0.000 description 6
- 238000004090 dissolution Methods 0.000 description 6
- 238000002474 experimental method Methods 0.000 description 6
- 238000009739 binding Methods 0.000 description 5
- 210000000988 bone and bone Anatomy 0.000 description 5
- 229940125904 compound 1 Drugs 0.000 description 5
- 229940126214 compound 3 Drugs 0.000 description 5
- 230000008569 process Effects 0.000 description 5
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 4
- 229940125782 compound 2 Drugs 0.000 description 4
- 239000003431 cross linking reagent Substances 0.000 description 4
- YQLZOAVZWJBZSY-UHFFFAOYSA-N decane-1,10-diamine Chemical compound NCCCCCCCCCCN YQLZOAVZWJBZSY-UHFFFAOYSA-N 0.000 description 4
- 150000004985 diamines Chemical class 0.000 description 4
- 238000011534 incubation Methods 0.000 description 4
- 239000000463 material Substances 0.000 description 4
- 230000000717 retained effect Effects 0.000 description 4
- 238000000108 ultra-filtration Methods 0.000 description 4
- 102000013566 Plasminogen Human genes 0.000 description 3
- 108010051456 Plasminogen Proteins 0.000 description 3
- 239000003146 anticoagulant agent Substances 0.000 description 3
- 239000007853 buffer solution Substances 0.000 description 3
- 230000008859 change Effects 0.000 description 3
- 239000003153 chemical reaction reagent Substances 0.000 description 3
- PWSKHLMYTZNYKO-UHFFFAOYSA-N heptane-1,7-diamine Chemical compound NCCCCCCCN PWSKHLMYTZNYKO-UHFFFAOYSA-N 0.000 description 3
- 125000001570 methylene group Chemical group [H]C([H])([*:1])[*:2] 0.000 description 3
- 230000003287 optical effect Effects 0.000 description 3
- KIDHWZJUCRJVML-UHFFFAOYSA-N putrescine Chemical compound NCCCCN KIDHWZJUCRJVML-UHFFFAOYSA-N 0.000 description 3
- 239000012487 rinsing solution Substances 0.000 description 3
- WCUXLLCKKVVCTQ-UHFFFAOYSA-M Potassium chloride Chemical compound [Cl-].[K+] WCUXLLCKKVVCTQ-UHFFFAOYSA-M 0.000 description 2
- 108090000190 Thrombin Proteins 0.000 description 2
- 230000004913 activation Effects 0.000 description 2
- 230000009089 cytolysis Effects 0.000 description 2
- ZBCBWPMODOFKDW-UHFFFAOYSA-N diethanolamine Chemical compound OCCNCCO ZBCBWPMODOFKDW-UHFFFAOYSA-N 0.000 description 2
- 150000002148 esters Chemical class 0.000 description 2
- 230000020764 fibrinolysis Effects 0.000 description 2
- 238000005227 gel permeation chromatography Methods 0.000 description 2
- 230000007062 hydrolysis Effects 0.000 description 2
- 238000006460 hydrolysis reaction Methods 0.000 description 2
- 238000002955 isolation Methods 0.000 description 2
- 238000002156 mixing Methods 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 230000002035 prolonged effect Effects 0.000 description 2
- 239000011541 reaction mixture Substances 0.000 description 2
- 229960004072 thrombin Drugs 0.000 description 2
- 206010008138 Cerebral venous thrombosis Diseases 0.000 description 1
- 206010011091 Coronary artery thrombosis Diseases 0.000 description 1
- 206010051055 Deep vein thrombosis Diseases 0.000 description 1
- LCGLNKUTAGEVQW-UHFFFAOYSA-N Dimethyl ether Chemical compound COC LCGLNKUTAGEVQW-UHFFFAOYSA-N 0.000 description 1
- 101000605403 Homo sapiens Plasminogen Proteins 0.000 description 1
- 238000012404 In vitro experiment Methods 0.000 description 1
- 108091000080 Phosphotransferase Proteins 0.000 description 1
- 102000001253 Protein Kinase Human genes 0.000 description 1
- 229920005654 Sephadex Polymers 0.000 description 1
- 239000012507 Sephadex™ Substances 0.000 description 1
- 206010047249 Venous thrombosis Diseases 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 230000002411 adverse Effects 0.000 description 1
- 239000011942 biocatalyst Substances 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 210000004204 blood vessel Anatomy 0.000 description 1
- 239000012928 buffer substance Substances 0.000 description 1
- 230000002490 cerebral effect Effects 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 229940125773 compound 10 Drugs 0.000 description 1
- 239000000356 contaminant Substances 0.000 description 1
- 208000002528 coronary thrombosis Diseases 0.000 description 1
- 238000004132 cross linking Methods 0.000 description 1
- 230000006378 damage Effects 0.000 description 1
- 238000000354 decomposition reaction Methods 0.000 description 1
- 230000007423 decrease Effects 0.000 description 1
- QFTYSVGGYOXFRQ-UHFFFAOYSA-N dodecane-1,12-diamine Chemical compound NCCCCCCCCCCCCN QFTYSVGGYOXFRQ-UHFFFAOYSA-N 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 230000002349 favourable effect Effects 0.000 description 1
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 239000012634 fragment Substances 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 230000003100 immobilizing effect Effects 0.000 description 1
- ZLVXBBHTMQJRSX-VMGNSXQWSA-N jdtic Chemical compound C1([C@]2(C)CCN(C[C@@H]2C)C[C@H](C(C)C)NC(=O)[C@@H]2NCC3=CC(O)=CC=C3C2)=CC=CC(O)=C1 ZLVXBBHTMQJRSX-VMGNSXQWSA-N 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- RTWNYYOXLSILQN-UHFFFAOYSA-N methanediamine Chemical compound NCN RTWNYYOXLSILQN-UHFFFAOYSA-N 0.000 description 1
- 208000010125 myocardial infarction Diseases 0.000 description 1
- 102000020233 phosphotransferase Human genes 0.000 description 1
- 229940012957 plasmin Drugs 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 235000011164 potassium chloride Nutrition 0.000 description 1
- 239000001103 potassium chloride Substances 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 108060006633 protein kinase Proteins 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 239000012088 reference solution Substances 0.000 description 1
- 239000013558 reference substance Substances 0.000 description 1
- 238000002798 spectrophotometry method Methods 0.000 description 1
- 230000000087 stabilizing effect Effects 0.000 description 1
- 230000003335 steric effect Effects 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 230000009885 systemic effect Effects 0.000 description 1
- 229940124597 therapeutic agent Drugs 0.000 description 1
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
- C12N9/14—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
- C12N9/6424—Serine endopeptidases (3.4.21)
- C12N9/6456—Plasminogen activators
- C12N9/6462—Plasminogen activators u-Plasminogen activator (3.4.21.73), i.e. urokinase
-
- 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
- A61K47/62—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 a protein, peptide or polyamino acid
-
- 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
- C12N9/96—Stabilising an enzyme by forming an adduct or a composition; Forming enzyme conjugates
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y304/00—Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
- C12Y304/21—Serine endopeptidases (3.4.21)
- C12Y304/21073—Serine endopeptidases (3.4.21) u-Plasminogen activator (3.4.21.73), i.e. urokinase
-
- 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)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Organic Chemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Genetics & Genomics (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- General Engineering & Computer Science (AREA)
- Biochemistry (AREA)
- Biomedical Technology (AREA)
- Microbiology (AREA)
- Molecular Biology (AREA)
- Biotechnology (AREA)
- Pharmacology & Pharmacy (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Epidemiology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Hematology (AREA)
- Diabetes (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Enzymes And Modification Thereof (AREA)
- Immobilizing And Processing Of Enzymes And Microorganisms (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| SU833590957A SU1128601A1 (ru) | 1983-05-10 | 1983-05-10 | Урокиназа,иммобилизированна на фибриногене |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| SE8500093L SE8500093L (sv) | 1985-01-09 |
| SE8500093D0 SE8500093D0 (sv) | 1985-01-09 |
| SE442022B true SE442022B (sv) | 1985-11-25 |
Family
ID=21063322
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| SE8500093A SE442022B (sv) | 1983-05-10 | 1985-01-09 | Urokinasderivat bestaende av urokinas bundet till fibrinogen |
Country Status (8)
| Country | Link |
|---|---|
| US (1) | US4564596A (en, 2012) |
| JP (1) | JPS60501239A (en, 2012) |
| DE (1) | DE3490222T1 (en, 2012) |
| GB (1) | GB2150576B (en, 2012) |
| IT (1) | IT1199522B (en, 2012) |
| SE (1) | SE442022B (en, 2012) |
| SU (1) | SU1128601A1 (en, 2012) |
| WO (1) | WO1984004536A1 (en, 2012) |
Families Citing this family (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB8400653D0 (en) * | 1984-01-11 | 1984-02-15 | Beecham Group Plc | Conjugates |
| US4783330A (en) * | 1984-11-15 | 1988-11-08 | New England Medical Center Hospitals, Inc. | Monoclonal antibodies to activated platelets |
| CA1335361C (en) * | 1989-05-24 | 1995-04-25 | Andrei Z. Budzynski | Thrombus-targeted complexes of plasminogen activator and fibrin fragments |
| US5632986A (en) * | 1991-05-09 | 1997-05-27 | The University Of Washington | Phospholipid-targeted thrombolytic agents |
| CA2091544A1 (en) * | 1992-03-26 | 1993-09-27 | Shing F. Kwan | Stabilization of functional proteins |
| US10127295B2 (en) * | 2009-06-05 | 2018-11-13 | Microsoft Technolofy Licensing, Llc | Geographic co-location service for cloud computing |
| US8577892B2 (en) * | 2009-06-05 | 2013-11-05 | Microsoft Corporation | Utilizing affinity groups to allocate data items and computing resources |
| RU2674032C1 (ru) * | 2018-06-05 | 2018-12-04 | федеральное государственное автономное образовательное учреждение высшего образования "Санкт-Петербургский национальный исследовательский университет информационных технологий, механики и оптики" (Университет ИТМО) | Способ получения урокиназы, энтрапированной в коллоидный магнитный керамический нанокомпозитный материал |
Family Cites Families (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US3544427A (en) * | 1968-04-18 | 1970-12-01 | Century Lab Inc | Method of production of urokinase |
| US4029767A (en) * | 1971-09-24 | 1977-06-14 | Choay S.A. | Pharmaceutical compositions of stable urokinase-heparin complexes and methods for use thereof |
| DE2431342C3 (de) * | 1973-07-27 | 1978-10-26 | Behringwerke Ag, 3550 Marburg | Verfahren zur Messung des Plasminogengehaltes durch Bestimmung der Bildung von Fibrin in einer Probe |
| JPS6043116B2 (ja) * | 1978-02-21 | 1985-09-26 | 株式会社ミドリ十字 | ウロキナ−ゼ誘導体 |
| JPS54147916A (en) * | 1978-05-12 | 1979-11-19 | Sumitomo Chem Co Ltd | Preparation of urokinase injection |
| GB2038337B (en) * | 1978-12-21 | 1983-01-19 | Green Cross Corp | Process which comprises separation of urokinases having different molecular weights |
| SU1022988A1 (ru) * | 1979-09-28 | 1983-06-15 | Всесоюзный кардиологический научный центр АМН СССР | Стабилизированна урокиназа,обладающа тромболитической активностью,и способ ее получени |
| US4381346A (en) * | 1979-11-13 | 1983-04-26 | Huasin Syed S | Isolation of plasminogen activators useful as therapeutic and diagnostic agents |
-
1983
- 1983-05-10 SU SU833590957A patent/SU1128601A1/ru active
-
1984
- 1984-03-01 US US06/705,343 patent/US4564596A/en not_active Expired - Fee Related
- 1984-03-01 DE DE19843490222 patent/DE3490222T1/de not_active Withdrawn
- 1984-03-01 WO PCT/SU1984/000008 patent/WO1984004536A1/ru active Application Filing
- 1984-03-01 JP JP59501243A patent/JPS60501239A/ja active Granted
- 1984-03-01 GB GB08500165A patent/GB2150576B/en not_active Expired
- 1984-05-09 IT IT41570/84A patent/IT1199522B/it active
-
1985
- 1985-01-09 SE SE8500093A patent/SE442022B/sv not_active IP Right Cessation
Also Published As
| Publication number | Publication date |
|---|---|
| IT1199522B (it) | 1988-12-30 |
| GB2150576B (en) | 1987-02-25 |
| WO1984004536A1 (en) | 1984-11-22 |
| GB2150576A (en) | 1985-07-03 |
| DE3490222T1 (de) | 1985-05-02 |
| JPS60501239A (ja) | 1985-08-08 |
| SE8500093L (sv) | 1985-01-09 |
| IT8441570A0 (it) | 1984-05-09 |
| IT8441570A1 (it) | 1985-11-09 |
| GB8500165D0 (en) | 1985-02-13 |
| SU1128601A1 (ru) | 1985-07-15 |
| JPH026513B2 (en, 2012) | 1990-02-09 |
| US4564596A (en) | 1986-01-14 |
| SE8500093D0 (sv) | 1985-01-09 |
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Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| NUG | Patent has lapsed |
Ref document number: 8500093-3 Effective date: 19910117 Format of ref document f/p: F |