JPS60501239A - ウロキナ−ゼ誘導体 - Google Patents
ウロキナ−ゼ誘導体Info
- Publication number
- JPS60501239A JPS60501239A JP59501243A JP50124384A JPS60501239A JP S60501239 A JPS60501239 A JP S60501239A JP 59501243 A JP59501243 A JP 59501243A JP 50124384 A JP50124384 A JP 50124384A JP S60501239 A JPS60501239 A JP S60501239A
- Authority
- JP
- Japan
- Prior art keywords
- urokinase
- compound
- derivative
- hours
- solution
- Prior art date
- Legal status (The legal status 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 status listed.)
- Granted
Links
- 102000003990 Urokinase-type plasminogen activator Human genes 0.000 title claims description 87
- 108090000435 Urokinase-type plasminogen activator Proteins 0.000 title claims description 87
- 229960005356 urokinase Drugs 0.000 title claims description 85
- 108010049003 Fibrinogen Proteins 0.000 claims description 14
- 102000008946 Fibrinogen Human genes 0.000 claims description 14
- 229940012952 fibrinogen Drugs 0.000 claims description 14
- 230000003197 catalytic effect Effects 0.000 claims description 12
- 108090000371 Esterases Proteins 0.000 claims description 9
- 150000004985 diamines Chemical class 0.000 claims description 9
- 125000001931 aliphatic group Chemical group 0.000 claims 1
- 102000004190 Enzymes Human genes 0.000 description 20
- 108090000790 Enzymes Proteins 0.000 description 20
- 229940088598 enzyme Drugs 0.000 description 19
- 230000002537 thrombolytic effect Effects 0.000 description 15
- 150000001875 compounds Chemical class 0.000 description 14
- BWGVNKXGVNDBDI-UHFFFAOYSA-N Fibrin monomer Chemical compound CNC(=O)CNC(=O)CN BWGVNKXGVNDBDI-UHFFFAOYSA-N 0.000 description 13
- 102000009123 Fibrin Human genes 0.000 description 12
- 108010073385 Fibrin Proteins 0.000 description 12
- 230000000694 effects Effects 0.000 description 12
- 229950003499 fibrin Drugs 0.000 description 12
- 238000000034 method Methods 0.000 description 11
- 239000000203 mixture Substances 0.000 description 10
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 10
- 239000008363 phosphate buffer Substances 0.000 description 9
- 238000002360 preparation method Methods 0.000 description 9
- 229940125904 compound 1 Drugs 0.000 description 8
- 229940125898 compound 5 Drugs 0.000 description 8
- 239000012153 distilled water Substances 0.000 description 8
- -1 aliphatic diamine Chemical class 0.000 description 7
- 238000002474 experimental method Methods 0.000 description 7
- 150000001718 carbodiimides Chemical class 0.000 description 6
- 230000000717 retained effect Effects 0.000 description 6
- 208000007536 Thrombosis Diseases 0.000 description 5
- 229940126214 compound 3 Drugs 0.000 description 5
- 238000012986 modification Methods 0.000 description 5
- 230000004913 activation Effects 0.000 description 4
- 229940125782 compound 2 Drugs 0.000 description 4
- 239000003431 cross linking reagent Substances 0.000 description 4
- 238000004090 dissolution Methods 0.000 description 4
- 239000011159 matrix material Substances 0.000 description 4
- 230000004048 modification Effects 0.000 description 4
- 230000008569 process Effects 0.000 description 4
- 238000009739 binding Methods 0.000 description 3
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 3
- QFTYSVGGYOXFRQ-UHFFFAOYSA-N dodecane-1,12-diamine Chemical compound NCCCCCCCCCCCCN QFTYSVGGYOXFRQ-UHFFFAOYSA-N 0.000 description 3
- 230000003480 fibrinolytic effect Effects 0.000 description 3
- RTWNYYOXLSILQN-UHFFFAOYSA-N methanediamine Chemical compound NCN RTWNYYOXLSILQN-UHFFFAOYSA-N 0.000 description 3
- 230000004899 motility Effects 0.000 description 3
- 230000003287 optical effect Effects 0.000 description 3
- 102000004169 proteins and genes Human genes 0.000 description 3
- 108090000623 proteins and genes Proteins 0.000 description 3
- 230000001732 thrombotic effect Effects 0.000 description 3
- 238000000108 ultra-filtration Methods 0.000 description 3
- 238000005406 washing Methods 0.000 description 3
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 2
- 108091000080 Phosphotransferase Proteins 0.000 description 2
- 239000003146 anticoagulant agent Substances 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- 239000008280 blood Substances 0.000 description 2
- 210000004369 blood Anatomy 0.000 description 2
- 239000000872 buffer Substances 0.000 description 2
- 230000015556 catabolic process Effects 0.000 description 2
- 230000008859 change Effects 0.000 description 2
- 238000007796 conventional method Methods 0.000 description 2
- 238000006731 degradation reaction Methods 0.000 description 2
- 239000003814 drug Substances 0.000 description 2
- 238000001914 filtration Methods 0.000 description 2
- 230000007062 hydrolysis Effects 0.000 description 2
- 238000006460 hydrolysis reaction Methods 0.000 description 2
- 238000011534 incubation Methods 0.000 description 2
- 230000003993 interaction Effects 0.000 description 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 238000005259 measurement Methods 0.000 description 2
- 125000001570 methylene group Chemical group [H]C([H])([*:1])[*:2] 0.000 description 2
- 102000020233 phosphotransferase Human genes 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- ISCMYZGMRHODRP-UHFFFAOYSA-N 3-(iminomethylideneamino)-n,n-dimethylpropan-1-amine Chemical compound CN(C)CCCN=C=N ISCMYZGMRHODRP-UHFFFAOYSA-N 0.000 description 1
- 241000511343 Chondrostoma nasus Species 0.000 description 1
- 206010011091 Coronary artery thrombosis Diseases 0.000 description 1
- 229920002307 Dextran Polymers 0.000 description 1
- LCGLNKUTAGEVQW-UHFFFAOYSA-N Dimethyl ether Chemical compound COC LCGLNKUTAGEVQW-UHFFFAOYSA-N 0.000 description 1
- 102000010911 Enzyme Precursors Human genes 0.000 description 1
- 108010062466 Enzyme Precursors Proteins 0.000 description 1
- 239000005977 Ethylene Substances 0.000 description 1
- HTTJABKRGRZYRN-UHFFFAOYSA-N Heparin Chemical compound OC1C(NC(=O)C)C(O)OC(COS(O)(=O)=O)C1OC1C(OS(O)(=O)=O)C(O)C(OC2C(C(OS(O)(=O)=O)C(OC3C(C(O)C(O)C(O3)C(O)=O)OS(O)(=O)=O)C(CO)O2)NS(O)(=O)=O)C(C(O)=O)O1 HTTJABKRGRZYRN-UHFFFAOYSA-N 0.000 description 1
- 238000012404 In vitro experiment Methods 0.000 description 1
- LFVLUOAHQIVABZ-UHFFFAOYSA-N Iodofenphos Chemical compound COP(=S)(OC)OC1=CC(Cl)=C(I)C=C1Cl LFVLUOAHQIVABZ-UHFFFAOYSA-N 0.000 description 1
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- 102000013566 Plasminogen Human genes 0.000 description 1
- 108010051456 Plasminogen Proteins 0.000 description 1
- 208000010378 Pulmonary Embolism Diseases 0.000 description 1
- QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 1
- 108090000190 Thrombin Proteins 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 229910000147 aluminium phosphate Inorganic materials 0.000 description 1
- 150000001412 amines Chemical class 0.000 description 1
- 150000001413 amino acids Chemical class 0.000 description 1
- 230000003110 anti-inflammatory effect Effects 0.000 description 1
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 1
- 239000011942 biocatalyst Substances 0.000 description 1
- 230000017531 blood circulation Effects 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 239000003054 catalyst Substances 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 238000004140 cleaning Methods 0.000 description 1
- 230000001010 compromised effect Effects 0.000 description 1
- 239000004020 conductor Substances 0.000 description 1
- 208000002528 coronary thrombosis Diseases 0.000 description 1
- 230000009089 cytolysis Effects 0.000 description 1
- 230000006378 damage Effects 0.000 description 1
- YQLZOAVZWJBZSY-UHFFFAOYSA-N decane-1,10-diamine Chemical compound NCCCCCCCCCCN YQLZOAVZWJBZSY-UHFFFAOYSA-N 0.000 description 1
- 230000007423 decrease Effects 0.000 description 1
- 230000000593 degrading effect Effects 0.000 description 1
- ZBCBWPMODOFKDW-UHFFFAOYSA-N diethanolamine Chemical compound OCCNCCO ZBCBWPMODOFKDW-UHFFFAOYSA-N 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 230000007071 enzymatic hydrolysis Effects 0.000 description 1
- 238000006047 enzymatic hydrolysis reaction Methods 0.000 description 1
- 239000003925 fat Substances 0.000 description 1
- 230000002349 favourable effect Effects 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- 239000012634 fragment Substances 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 229960002897 heparin Drugs 0.000 description 1
- 229920000669 heparin Polymers 0.000 description 1
- 150000003949 imides Chemical class 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 230000002779 inactivation Effects 0.000 description 1
- 239000000411 inducer Substances 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 239000003999 initiator Substances 0.000 description 1
- 230000005923 long-lasting effect Effects 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 238000009740 moulding (composite fabrication) Methods 0.000 description 1
- 208000010125 myocardial infarction Diseases 0.000 description 1
- 229910052760 oxygen Inorganic materials 0.000 description 1
- 239000001301 oxygen Substances 0.000 description 1
- 230000000704 physical effect Effects 0.000 description 1
- 229940012957 plasmin Drugs 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 230000008092 positive effect Effects 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 230000002035 prolonged effect Effects 0.000 description 1
- KIDHWZJUCRJVML-UHFFFAOYSA-N putrescine Chemical compound NCCCCN KIDHWZJUCRJVML-UHFFFAOYSA-N 0.000 description 1
- 239000011541 reaction mixture Substances 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 238000004904 shortening Methods 0.000 description 1
- 230000000087 stabilizing effect Effects 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 230000009885 systemic effect Effects 0.000 description 1
- 230000002123 temporal effect Effects 0.000 description 1
- 229960004072 thrombin Drugs 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 230000010415 tropism Effects 0.000 description 1
- 210000003462 vein Anatomy 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)
- Bioinformatics & Cheminformatics (AREA)
- Organic Chemistry (AREA)
- Genetics & Genomics (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Biomedical Technology (AREA)
- General Engineering & Computer Science (AREA)
- Biochemistry (AREA)
- Biotechnology (AREA)
- Molecular Biology (AREA)
- Microbiology (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 (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| SU833590957A SU1128601A1 (ru) | 1983-05-10 | 1983-05-10 | Урокиназа,иммобилизированна на фибриногене |
| SU3590957/28 | 1983-05-10 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPS60501239A true JPS60501239A (ja) | 1985-08-08 |
| JPH026513B2 JPH026513B2 (forum.php) | 1990-02-09 |
Family
ID=21063322
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP59501243A Granted JPS60501239A (ja) | 1983-05-10 | 1984-03-01 | ウロキナ−ゼ誘導体 |
Country Status (8)
| Country | Link |
|---|---|
| US (1) | US4564596A (forum.php) |
| JP (1) | JPS60501239A (forum.php) |
| DE (1) | DE3490222T1 (forum.php) |
| GB (1) | GB2150576B (forum.php) |
| IT (1) | IT1199522B (forum.php) |
| SE (1) | SE442022B (forum.php) |
| SU (1) | SU1128601A1 (forum.php) |
| WO (1) | WO1984004536A1 (forum.php) |
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 |
| US8577892B2 (en) * | 2009-06-05 | 2013-11-05 | Microsoft Corporation | Utilizing affinity groups to allocate data items and computing resources |
| US10127295B2 (en) * | 2009-06-05 | 2018-11-13 | Microsoft Technolofy Licensing, Llc | Geographic co-location service for cloud computing |
| 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 JP JP59501243A patent/JPS60501239A/ja active Granted
- 1984-03-01 WO PCT/SU1984/000008 patent/WO1984004536A1/ru active Application Filing
- 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 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 |
| JPH026513B2 (forum.php) | 1990-02-09 |
| DE3490222T1 (de) | 1985-05-02 |
| US4564596A (en) | 1986-01-14 |
| GB8500165D0 (en) | 1985-02-13 |
| WO1984004536A1 (en) | 1984-11-22 |
| GB2150576A (en) | 1985-07-03 |
| IT8441570A0 (it) | 1984-05-09 |
| SE8500093L (sv) | 1985-01-09 |
| SU1128601A1 (ru) | 1985-07-15 |
| IT8441570A1 (it) | 1985-11-09 |
| SE442022B (sv) | 1985-11-25 |
| SE8500093D0 (sv) | 1985-01-09 |
| GB2150576B (en) | 1987-02-25 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| Mozhaev et al. | Protein stabilization via hydrophilization: Covalent modification of trypsin and α‐chymotrypsin | |
| Mateo et al. | A new, mild cross‐linking methodology to prepare cross‐linked enzyme aggregates | |
| JPS61249388A (ja) | 安定化ス−パ−オキサイドジスムタ−ゼ | |
| JPH04505326A (ja) | プラスミノーゲン活性化剤とフィブリン断片との血栓ターゲットの錯体 | |
| Thorsen et al. | Reversible and Irreversible Alterations of Human Plasminogen Indicated by Changes in Susceptibility to Plasminogen Activators and in Response to∈-Aminocaproic Acid | |
| JPS60501239A (ja) | ウロキナ−ゼ誘導体 | |
| EP0151308B1 (en) | Urokinase complex adsorbable by fibrin and process for preparing same | |
| US5023078A (en) | Plasminogen activator-heparin conjugates | |
| Maksimenko et al. | Water-soluble urokinase derivatives with increased affinity to the fibrin clot | |
| US4349630A (en) | Heat-resistant water soluble urokinase derivative | |
| Inada et al. | Fibrinolysis by urokinase endowed with magnetic property | |
| CA1336585C (en) | Method of stabilizing urokinase precursor and dry preparation containing said precursor | |
| JPS6296085A (ja) | 高分子量単鎖ウロキナ−ゼとその製法 | |
| JPH1052267A (ja) | プロトロンビンの活性化方法および該方法に基づくトロンビンの製造方法 | |
| JPS6360938A (ja) | 修飾組織型プラスミノ−ゲン活性化因子およびその製造方法 | |
| JPH0218834B2 (forum.php) | ||
| Torchilin et al. | [49] Immobilized enzymes for thrombolytic therapy | |
| Torchilin et al. | Enzyme immobilization on heparin | |
| Velumani | Isolation, screening, characterization and production of fibrinolytic enzyme from marine microorganism | |
| JPS60184026A (ja) | 組織プラスミノ−ゲン・アクチベ−タ−の溶解補助方法 | |
| SU1137760A1 (ru) | Урокиназа,иммобилизованна на гепарине | |
| JP2861655B2 (ja) | ヒト尿性トリプシンインヒビター含有液状製剤及びその製造方法 | |
| JP2714817B2 (ja) | ウロキナーゼ前駆体の製造方法 | |
| JPS61238731A (ja) | ウロキナーゼ前駆体乾燥製剤 | |
| JPH0429350B2 (forum.php) |