NO902405L - Vevplasminogenaktivatorderivat, dna-sekvens og ekspresjonsplasmid, samt fremgangsmaate for fremstilling av plasmidet. - Google Patents
Vevplasminogenaktivatorderivat, dna-sekvens og ekspresjonsplasmid, samt fremgangsmaate for fremstilling av plasmidet.Info
- Publication number
- NO902405L NO902405L NO90902405A NO902405A NO902405L NO 902405 L NO902405 L NO 902405L NO 90902405 A NO90902405 A NO 90902405A NO 902405 A NO902405 A NO 902405A NO 902405 L NO902405 L NO 902405L
- Authority
- NO
- Norway
- Prior art keywords
- plasmid
- derivative
- dna sequence
- protein
- mmol
- Prior art date
Links
- 102000003978 Tissue Plasminogen Activator Human genes 0.000 title claims abstract description 69
- 108090000373 Tissue Plasminogen Activator Proteins 0.000 title claims abstract description 69
- 229960000187 tissue plasminogen activator Drugs 0.000 title claims abstract description 11
- 239000013612 plasmid Substances 0.000 title claims description 34
- 108091028043 Nucleic acid sequence Proteins 0.000 title claims description 17
- 238000000034 method Methods 0.000 title claims description 14
- 239000013613 expression plasmid Substances 0.000 title claims description 10
- 108090000623 proteins and genes Proteins 0.000 claims description 12
- 239000000203 mixture Substances 0.000 claims description 11
- 235000018102 proteins Nutrition 0.000 claims description 11
- 102000004169 proteins and genes Human genes 0.000 claims description 11
- 241000588724 Escherichia coli Species 0.000 claims description 10
- 210000004027 cell Anatomy 0.000 claims description 10
- 210000003000 inclusion body Anatomy 0.000 claims description 10
- 238000004519 manufacturing process Methods 0.000 claims description 10
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Natural products OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 claims description 9
- 238000001179 sorption measurement Methods 0.000 claims description 6
- ODKSFYDXXFIFQN-BYPYZUCNSA-N L-arginine Chemical compound OC(=O)[C@@H](N)CCCN=C(N)N ODKSFYDXXFIFQN-BYPYZUCNSA-N 0.000 claims description 5
- 229930064664 L-arginine Natural products 0.000 claims description 5
- 235000014852 L-arginine Nutrition 0.000 claims description 5
- 150000001413 amino acids Chemical group 0.000 claims description 5
- 238000010828 elution Methods 0.000 claims description 5
- 229960003180 glutathione Drugs 0.000 claims description 5
- PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 claims description 5
- 238000002703 mutagenesis Methods 0.000 claims description 5
- 231100000350 mutagenesis Toxicity 0.000 claims description 5
- 102000035195 Peptidases Human genes 0.000 claims description 4
- 108091005804 Peptidases Proteins 0.000 claims description 4
- 239000004365 Protease Substances 0.000 claims description 4
- 239000001963 growth medium Substances 0.000 claims description 3
- 229960000789 guanidine hydrochloride Drugs 0.000 claims description 3
- 108010053070 Glutathione Disulfide Proteins 0.000 claims description 2
- 235000001014 amino acid Nutrition 0.000 claims description 2
- 230000029087 digestion Effects 0.000 claims description 2
- 230000002068 genetic effect Effects 0.000 claims description 2
- YPZRWBKMTBYPTK-BJDJZHNGSA-N glutathione disulfide Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@H](C(=O)NCC(O)=O)CSSC[C@@H](C(=O)NCC(O)=O)NC(=O)CC[C@H](N)C(O)=O YPZRWBKMTBYPTK-BJDJZHNGSA-N 0.000 claims description 2
- 210000001236 prokaryotic cell Anatomy 0.000 claims description 2
- 238000011097 chromatography purification Methods 0.000 claims 3
- 239000012141 concentrate Substances 0.000 claims 2
- 108091028026 C-DNA Proteins 0.000 claims 1
- 208000007536 Thrombosis Diseases 0.000 claims 1
- 230000007850 degeneration Effects 0.000 claims 1
- YPZRWBKMTBYPTK-UHFFFAOYSA-N oxidized gamma-L-glutamyl-L-cysteinylglycine Natural products OC(=O)C(N)CCC(=O)NC(C(=O)NCC(O)=O)CSSCC(C(=O)NCC(O)=O)NC(=O)CCC(N)C(O)=O YPZRWBKMTBYPTK-UHFFFAOYSA-N 0.000 claims 1
- 230000007420 reactivation Effects 0.000 claims 1
- 125000003275 alpha amino acid group Chemical group 0.000 abstract 1
- 230000000694 effects Effects 0.000 description 15
- 239000012634 fragment Substances 0.000 description 12
- 102000009123 Fibrin Human genes 0.000 description 11
- 108010073385 Fibrin Proteins 0.000 description 11
- BWGVNKXGVNDBDI-UHFFFAOYSA-N Fibrin monomer Chemical compound CNC(=O)CNC(=O)CN BWGVNKXGVNDBDI-UHFFFAOYSA-N 0.000 description 11
- 229950003499 fibrin Drugs 0.000 description 11
- 102000008946 Fibrinogen Human genes 0.000 description 8
- 108010049003 Fibrinogen Proteins 0.000 description 8
- 229940012952 fibrinogen Drugs 0.000 description 8
- 230000002537 thrombolytic effect Effects 0.000 description 7
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 6
- 125000002059 L-arginyl group Chemical group O=C([*])[C@](N([H])[H])([H])C([H])([H])C([H])([H])C([H])([H])N([H])C(=N[H])N([H])[H] 0.000 description 6
- DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 6
- 238000002360 preparation method Methods 0.000 description 6
- 239000004475 Arginine Substances 0.000 description 5
- 235000009697 arginine Nutrition 0.000 description 5
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 5
- 229960003121 arginine Drugs 0.000 description 5
- 239000000872 buffer Substances 0.000 description 5
- 238000003776 cleavage reaction Methods 0.000 description 5
- 230000007017 scission Effects 0.000 description 5
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 4
- 229920002684 Sepharose Polymers 0.000 description 4
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 4
- 230000015271 coagulation Effects 0.000 description 4
- 238000005345 coagulation Methods 0.000 description 4
- 210000002381 plasma Anatomy 0.000 description 4
- 239000000047 product Substances 0.000 description 4
- 238000000746 purification Methods 0.000 description 4
- 238000004007 reversed phase HPLC Methods 0.000 description 4
- 238000012360 testing method Methods 0.000 description 4
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 3
- 108010024636 Glutathione Proteins 0.000 description 3
- 241001465754 Metazoa Species 0.000 description 3
- 102000013566 Plasminogen Human genes 0.000 description 3
- 108010051456 Plasminogen Proteins 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 238000001042 affinity chromatography Methods 0.000 description 3
- 238000004458 analytical method Methods 0.000 description 3
- 210000004369 blood Anatomy 0.000 description 3
- 239000008280 blood Substances 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
- 238000000354 decomposition reaction Methods 0.000 description 3
- 230000003480 fibrinolytic effect Effects 0.000 description 3
- 229960004198 guanidine Drugs 0.000 description 3
- 238000000338 in vitro Methods 0.000 description 3
- 238000002347 injection Methods 0.000 description 3
- 239000007924 injection Substances 0.000 description 3
- 239000000463 material Substances 0.000 description 3
- 229940012957 plasmin Drugs 0.000 description 3
- 230000010076 replication Effects 0.000 description 3
- 238000000926 separation method Methods 0.000 description 3
- 239000000243 solution Substances 0.000 description 3
- ZRALSGWEFCBTJO-UHFFFAOYSA-N Guanidine Chemical compound NC(N)=N ZRALSGWEFCBTJO-UHFFFAOYSA-N 0.000 description 2
- 206010023237 Jugular vein thrombosis Diseases 0.000 description 2
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 2
- 108091034117 Oligonucleotide Proteins 0.000 description 2
- 241000283973 Oryctolagus cuniculus Species 0.000 description 2
- 239000007983 Tris buffer Substances 0.000 description 2
- 230000004913 activation Effects 0.000 description 2
- 230000008901 benefit Effects 0.000 description 2
- 230000003197 catalytic effect Effects 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 238000012512 characterization method Methods 0.000 description 2
- 239000003795 chemical substances by application Substances 0.000 description 2
- 239000007857 degradation product Substances 0.000 description 2
- 238000012217 deletion Methods 0.000 description 2
- 230000037430 deletion Effects 0.000 description 2
- 238000000502 dialysis Methods 0.000 description 2
- 230000008030 elimination Effects 0.000 description 2
- 238000003379 elimination reaction Methods 0.000 description 2
- 238000001727 in vivo Methods 0.000 description 2
- 238000001990 intravenous administration Methods 0.000 description 2
- 239000011159 matrix material Substances 0.000 description 2
- 108090000765 processed proteins & peptides Proteins 0.000 description 2
- 102000004196 processed proteins & peptides Human genes 0.000 description 2
- 238000011555 rabbit model Methods 0.000 description 2
- 238000004153 renaturation Methods 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 2
- 239000002904 solvent Substances 0.000 description 2
- 239000013598 vector Substances 0.000 description 2
- 241000894006 Bacteria Species 0.000 description 1
- 108091026890 Coding region Proteins 0.000 description 1
- 108090000204 Dipeptidase 1 Proteins 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 108010043984 Erythrina caffra trypsin inhibitor Proteins 0.000 description 1
- 241000206602 Eukaryota Species 0.000 description 1
- 108091027305 Heteroduplex Proteins 0.000 description 1
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 1
- 102000016943 Muramidase Human genes 0.000 description 1
- 108010014251 Muramidase Proteins 0.000 description 1
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
- CHJJGSNFBQVOTG-UHFFFAOYSA-N N-methyl-guanidine Natural products CNC(N)=N CHJJGSNFBQVOTG-UHFFFAOYSA-N 0.000 description 1
- 102000001938 Plasminogen Activators Human genes 0.000 description 1
- 108010001014 Plasminogen Activators Proteins 0.000 description 1
- 108010023197 Streptokinase Proteins 0.000 description 1
- 229920004890 Triton X-100 Polymers 0.000 description 1
- 101710162629 Trypsin inhibitor Proteins 0.000 description 1
- 229940122618 Trypsin inhibitor Drugs 0.000 description 1
- 102000003990 Urokinase-type plasminogen activator Human genes 0.000 description 1
- 108090000435 Urokinase-type plasminogen activator Proteins 0.000 description 1
- BUBBEHCXSMCYNY-CVEARBPZSA-N [3-hydroxy-5-methyl-4-[(2S,3R)-2,3,4-trihydroxybutoxy]carbonylphenyl] 2,4-dihydroxy-6-methylbenzoate Chemical compound CC1=CC(O)=CC(O)=C1C(=O)OC1=CC(C)=C(C(=O)OC[C@H](O)[C@H](O)CO)C(O)=C1 BUBBEHCXSMCYNY-CVEARBPZSA-N 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 230000003213 activating effect Effects 0.000 description 1
- 239000003463 adsorbent Substances 0.000 description 1
- 230000002776 aggregation Effects 0.000 description 1
- 238000004220 aggregation Methods 0.000 description 1
- 235000004279 alanine Nutrition 0.000 description 1
- 102000003801 alpha-2-Antiplasmin Human genes 0.000 description 1
- 108090000183 alpha-2-Antiplasmin Proteins 0.000 description 1
- 229940024606 amino acid Drugs 0.000 description 1
- 239000003146 anticoagulant agent Substances 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 230000000740 bleeding effect Effects 0.000 description 1
- 230000000903 blocking effect Effects 0.000 description 1
- 230000023555 blood coagulation Effects 0.000 description 1
- 230000037396 body weight Effects 0.000 description 1
- 238000004364 calculation method Methods 0.000 description 1
- 239000012876 carrier material Substances 0.000 description 1
- 230000006037 cell lysis Effects 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 238000007385 chemical modification Methods 0.000 description 1
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 238000004590 computer program Methods 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 230000009089 cytolysis Effects 0.000 description 1
- 238000004925 denaturation Methods 0.000 description 1
- 230000036425 denaturation Effects 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 238000001212 derivatisation Methods 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- SWSQBOPZIKWTGO-UHFFFAOYSA-N dimethylaminoamidine Natural products CN(C)C(N)=N SWSQBOPZIKWTGO-UHFFFAOYSA-N 0.000 description 1
- 239000006185 dispersion Substances 0.000 description 1
- 238000006073 displacement reaction Methods 0.000 description 1
- 238000004090 dissolution Methods 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 229940088598 enzyme Drugs 0.000 description 1
- BUBBEHCXSMCYNY-UHFFFAOYSA-N erythrin Natural products CC1=CC(O)=CC(O)=C1C(=O)OC1=CC(C)=C(C(=O)OCC(O)C(O)CO)C(O)=C1 BUBBEHCXSMCYNY-UHFFFAOYSA-N 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 239000003527 fibrinolytic agent Substances 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 230000023597 hemostasis Effects 0.000 description 1
- 238000009396 hybridization Methods 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 208000015181 infectious disease Diseases 0.000 description 1
- 230000010354 integration Effects 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 238000012417 linear regression Methods 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 239000006166 lysate Substances 0.000 description 1
- 229960000274 lysozyme Drugs 0.000 description 1
- 239000004325 lysozyme Substances 0.000 description 1
- 235000010335 lysozyme Nutrition 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 230000010534 mechanism of action Effects 0.000 description 1
- 208000010125 myocardial infarction Diseases 0.000 description 1
- 238000011587 new zealand white rabbit Methods 0.000 description 1
- 230000020477 pH reduction Effects 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 230000001575 pathological effect Effects 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- 230000003285 pharmacodynamic effect Effects 0.000 description 1
- 230000004962 physiological condition Effects 0.000 description 1
- 230000036470 plasma concentration Effects 0.000 description 1
- 229940127126 plasminogen activator Drugs 0.000 description 1
- 239000013014 purified material Substances 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 238000010405 reoxidation reaction Methods 0.000 description 1
- 230000003362 replicative effect Effects 0.000 description 1
- 108091008146 restriction endonucleases Proteins 0.000 description 1
- 238000002741 site-directed mutagenesis Methods 0.000 description 1
- 229960005202 streptokinase Drugs 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000002753 trypsin inhibitor Substances 0.000 description 1
- 229960005356 urokinase Drugs 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
- C12N9/6459—Plasminogen activators t-plasminogen activator (3.4.21.68), i.e. tPA
-
- 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
- C12N9/6421—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
-
- 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)
- C12Y304/21069—Protein C activated (3.4.21.69)
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth 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)
- Biomedical Technology (AREA)
- General Engineering & Computer Science (AREA)
- Biochemistry (AREA)
- Medicinal Chemistry (AREA)
- Microbiology (AREA)
- Biotechnology (AREA)
- Molecular Biology (AREA)
- Veterinary Medicine (AREA)
- Hematology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Diabetes (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Enzymes And Modification Thereof (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Saccharide Compounds (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Luminescent Compositions (AREA)
- Organic Low-Molecular-Weight Compounds And Preparation Thereof (AREA)
- Nitrogen Condensed Heterocyclic Rings (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DE3917781 | 1989-05-31 | ||
| DE3923339A DE3923339A1 (de) | 1989-05-31 | 1989-07-14 | Gewebs-plasminogen-aktivator-derivat |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| NO902405D0 NO902405D0 (no) | 1990-05-30 |
| NO902405L true NO902405L (no) | 1990-12-03 |
Family
ID=25881452
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| NO90902405A NO902405L (no) | 1989-05-31 | 1990-05-30 | Vevplasminogenaktivatorderivat, dna-sekvens og ekspresjonsplasmid, samt fremgangsmaate for fremstilling av plasmidet. |
Country Status (17)
| Country | Link |
|---|---|
| EP (1) | EP0400545B1 (cs) |
| JP (1) | JPH0327286A (cs) |
| AT (1) | ATE119940T1 (cs) |
| AU (1) | AU623781B2 (cs) |
| CA (1) | CA2017636C (cs) |
| CZ (1) | CZ267690A3 (cs) |
| DD (1) | DD300109A5 (cs) |
| DE (2) | DE3923339A1 (cs) |
| ES (1) | ES2070210T3 (cs) |
| FI (1) | FI101475B1 (cs) |
| HU (1) | HU216870B (cs) |
| IE (1) | IE66006B1 (cs) |
| IL (1) | IL94539A (cs) |
| NO (1) | NO902405L (cs) |
| NZ (1) | NZ233796A (cs) |
| PT (1) | PT94227B (cs) |
| ZA (1) | ZA904089B (cs) |
Families Citing this family (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE3942144A1 (de) * | 1989-12-20 | 1991-06-27 | Boehringer Mannheim Gmbh | Stabilisierung von k1k2p pro |
| US6027888A (en) * | 1996-04-05 | 2000-02-22 | Board Of Regents, The University Of Texas System | Methods for producing soluble, biologically-active disulfide-bond containing eukaryotic proteins in bacterial cells |
Family Cites Families (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| HU200615B (en) * | 1982-05-05 | 1990-07-28 | Genentech Inc | Methods of preparing tissue plasiminogen activator derivative composition |
| FR2594845B1 (fr) * | 1986-02-21 | 1989-12-01 | Genetica | Preparation par voie microbiologique de l'activateur tissulaire humain du plasminogene (t-pa) et conversion de l'enzyme ainsi obtenue en sa forme active |
| DE3643158A1 (de) * | 1986-04-21 | 1987-11-19 | Boehringer Mannheim Gmbh | Gewebs-plasminogen-aktivator(tpa) - derivat und seine herstellung |
| FI100106B (fi) * | 1986-12-05 | 1997-09-30 | Novartis Ag | Menetelmä plasminogeenin yksisäikeisen yhdistelmäaktivaattorin valmist amiseksi |
| IL87276A (en) * | 1987-08-03 | 1995-07-31 | Fujisawa Pharmaceutical Co | Analog of tissue plasminogen activator comprising only the kringle 2 and protease domain dna encoding the same processes for the preparation thereof and pharmaceutical compositions containing the same |
| US5094953A (en) * | 1988-03-21 | 1992-03-10 | Genentech, Inc. | Human tissue plasminogen activator variants |
| DE3903581A1 (de) * | 1989-02-07 | 1990-08-16 | Boehringer Mannheim Gmbh | Gewebs-plasminogenaktivator-derivat |
-
1989
- 1989-07-14 DE DE3923339A patent/DE3923339A1/de not_active Withdrawn
-
1990
- 1990-05-22 IE IE184890A patent/IE66006B1/en not_active IP Right Cessation
- 1990-05-24 NZ NZ233796A patent/NZ233796A/en unknown
- 1990-05-28 EP EP90110096A patent/EP0400545B1/de not_active Expired - Lifetime
- 1990-05-28 CA CA002017636A patent/CA2017636C/en not_active Expired - Fee Related
- 1990-05-28 IL IL9453990A patent/IL94539A/en not_active IP Right Cessation
- 1990-05-28 DE DE59008693T patent/DE59008693D1/de not_active Expired - Fee Related
- 1990-05-28 AT AT90110096T patent/ATE119940T1/de not_active IP Right Cessation
- 1990-05-28 AU AU56009/90A patent/AU623781B2/en not_active Ceased
- 1990-05-28 ES ES90110096T patent/ES2070210T3/es not_active Expired - Lifetime
- 1990-05-29 ZA ZA904089A patent/ZA904089B/xx unknown
- 1990-05-29 JP JP2139539A patent/JPH0327286A/ja active Pending
- 1990-05-30 NO NO90902405A patent/NO902405L/no unknown
- 1990-05-30 CZ CS902676A patent/CZ267690A3/cs not_active IP Right Cessation
- 1990-05-30 HU HU903267A patent/HU216870B/hu not_active IP Right Cessation
- 1990-05-30 DD DD341150A patent/DD300109A5/de unknown
- 1990-05-30 FI FI902700A patent/FI101475B1/fi not_active IP Right Cessation
- 1990-05-31 PT PT94227A patent/PT94227B/pt active IP Right Grant
Also Published As
| Publication number | Publication date |
|---|---|
| PT94227B (pt) | 1997-01-31 |
| HU903267D0 (en) | 1990-10-28 |
| EP0400545B1 (de) | 1995-03-15 |
| FI101475B (fi) | 1998-06-30 |
| EP0400545A1 (de) | 1990-12-05 |
| IL94539A0 (en) | 1991-03-10 |
| ES2070210T3 (es) | 1995-06-01 |
| IE66006B1 (en) | 1995-11-29 |
| AU5600990A (en) | 1990-12-06 |
| NZ233796A (en) | 1992-07-28 |
| CA2017636C (en) | 2000-05-02 |
| HU216870B (hu) | 1999-09-28 |
| ATE119940T1 (de) | 1995-04-15 |
| IE901848L (en) | 1990-11-30 |
| PT94227A (pt) | 1991-02-08 |
| FI902700A0 (fi) | 1990-05-30 |
| NO902405D0 (no) | 1990-05-30 |
| CA2017636A1 (en) | 1990-11-30 |
| DE3923339A1 (de) | 1990-12-06 |
| CZ282035B6 (cs) | 1997-04-16 |
| FI101475B1 (fi) | 1998-06-30 |
| AU623781B2 (en) | 1992-05-21 |
| DE59008693D1 (de) | 1995-04-20 |
| DD300109A5 (de) | 1992-05-21 |
| HUT54734A (en) | 1991-03-28 |
| ZA904089B (en) | 1991-03-27 |
| JPH0327286A (ja) | 1991-02-05 |
| CZ267690A3 (en) | 1997-04-16 |
| IL94539A (en) | 1996-08-04 |
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