KR910001807B1 - 스태필로키나아제를 생산하는 유전자를 함유하는 새로운 대장균 및 스태필로키나아제의 제조법 - Google Patents
스태필로키나아제를 생산하는 유전자를 함유하는 새로운 대장균 및 스태필로키나아제의 제조법 Download PDFInfo
- Publication number
- KR910001807B1 KR910001807B1 KR8204582A KR820004582A KR910001807B1 KR 910001807 B1 KR910001807 B1 KR 910001807B1 KR 8204582 A KR8204582 A KR 8204582A KR 820004582 A KR820004582 A KR 820004582A KR 910001807 B1 KR910001807 B1 KR 910001807B1
- Authority
- KR
- South Korea
- Prior art keywords
- dna
- coli
- production
- sak
- staphylokinase
- 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.)
- Expired
Links
- 238000004519 manufacturing process Methods 0.000 title claims description 40
- 101710145796 Staphylokinase Proteins 0.000 title claims description 8
- 108090000623 proteins and genes Proteins 0.000 title description 6
- 102000004169 proteins and genes Human genes 0.000 title description 3
- 108020004511 Recombinant DNA Proteins 0.000 title description 2
- 241000193830 Bacillus <bacterium> Species 0.000 title 1
- 241000588724 Escherichia coli Species 0.000 claims description 54
- 238000000034 method Methods 0.000 claims description 29
- 239000013598 vector Substances 0.000 claims description 20
- 230000002068 genetic effect Effects 0.000 claims description 9
- 230000007774 longterm Effects 0.000 claims description 3
- 241000191940 Staphylococcus Species 0.000 claims 2
- 230000001131 transforming effect Effects 0.000 claims 1
- 108020004414 DNA Proteins 0.000 description 65
- 239000012634 fragment Substances 0.000 description 23
- 238000006243 chemical reaction Methods 0.000 description 17
- 108091008146 restriction endonucleases Proteins 0.000 description 17
- 239000000243 solution Substances 0.000 description 15
- 238000003776 cleavage reaction Methods 0.000 description 14
- 230000007017 scission Effects 0.000 description 14
- FAPWRFPIFSIZLT-UHFFFAOYSA-M sodium chloride Inorganic materials [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 13
- 239000013612 plasmid Substances 0.000 description 12
- 238000001816 cooling Methods 0.000 description 10
- 241000894006 Bacteria Species 0.000 description 9
- 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 9
- 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 8
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 8
- 239000000872 buffer Substances 0.000 description 7
- 239000011780 sodium chloride Substances 0.000 description 7
- 210000001322 periplasm Anatomy 0.000 description 6
- 230000006798 recombination Effects 0.000 description 6
- 238000005215 recombination Methods 0.000 description 6
- 210000004027 cell Anatomy 0.000 description 5
- 230000000694 effects Effects 0.000 description 5
- 238000000855 fermentation Methods 0.000 description 5
- 229920001817 Agar Polymers 0.000 description 4
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 4
- 102000009123 Fibrin Human genes 0.000 description 4
- 108010073385 Fibrin Proteins 0.000 description 4
- BWGVNKXGVNDBDI-UHFFFAOYSA-N Fibrin monomer Chemical compound CNC(=O)CNC(=O)CN BWGVNKXGVNDBDI-UHFFFAOYSA-N 0.000 description 4
- 239000008272 agar Substances 0.000 description 4
- 238000012258 culturing Methods 0.000 description 4
- 229950003499 fibrin Drugs 0.000 description 4
- 239000005457 ice water Substances 0.000 description 4
- 239000002244 precipitate Substances 0.000 description 4
- 238000000746 purification Methods 0.000 description 4
- 229920000936 Agarose Polymers 0.000 description 3
- 239000007984 Tris EDTA buffer Substances 0.000 description 3
- 238000000246 agarose gel electrophoresis Methods 0.000 description 3
- 229960000723 ampicillin Drugs 0.000 description 3
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 3
- 230000000721 bacterilogical effect Effects 0.000 description 3
- 230000008901 benefit Effects 0.000 description 3
- 238000000605 extraction Methods 0.000 description 3
- 239000001509 sodium citrate Substances 0.000 description 3
- NLJMYIDDQXHKNR-UHFFFAOYSA-K sodium citrate Chemical compound O.O.[Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NLJMYIDDQXHKNR-UHFFFAOYSA-K 0.000 description 3
- 239000006228 supernatant Substances 0.000 description 3
- 238000012360 testing method Methods 0.000 description 3
- 102000016928 DNA-directed DNA polymerase Human genes 0.000 description 2
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 description 2
- 241000588722 Escherichia Species 0.000 description 2
- 241001646716 Escherichia coli K-12 Species 0.000 description 2
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 2
- 102000003960 Ligases Human genes 0.000 description 2
- 108090000364 Ligases Proteins 0.000 description 2
- 102000016943 Muramidase Human genes 0.000 description 2
- 108010014251 Muramidase Proteins 0.000 description 2
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 2
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 2
- 229930006000 Sucrose Natural products 0.000 description 2
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 2
- 238000004458 analytical method Methods 0.000 description 2
- 229940041514 candida albicans extract Drugs 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 238000007796 conventional method Methods 0.000 description 2
- 238000000432 density-gradient centrifugation Methods 0.000 description 2
- 238000000502 dialysis Methods 0.000 description 2
- 238000001962 electrophoresis Methods 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 239000000499 gel Substances 0.000 description 2
- 239000008103 glucose Substances 0.000 description 2
- 229960000274 lysozyme Drugs 0.000 description 2
- 239000004325 lysozyme Substances 0.000 description 2
- 235000010335 lysozyme Nutrition 0.000 description 2
- 239000000203 mixture Substances 0.000 description 2
- 150000002989 phenols Chemical class 0.000 description 2
- 238000001556 precipitation Methods 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- 229920006395 saturated elastomer Polymers 0.000 description 2
- 238000000926 separation method Methods 0.000 description 2
- 239000001632 sodium acetate Substances 0.000 description 2
- 235000017281 sodium acetate Nutrition 0.000 description 2
- 239000005720 sucrose Substances 0.000 description 2
- 239000000725 suspension Substances 0.000 description 2
- 239000012138 yeast extract Substances 0.000 description 2
- NLMKTBGFQGKQEV-UHFFFAOYSA-N 2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-(2-hexadecoxyethoxy)ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethanol Chemical compound CCCCCCCCCCCCCCCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO NLMKTBGFQGKQEV-UHFFFAOYSA-N 0.000 description 1
- CFKMVGJGLGKFKI-UHFFFAOYSA-N 4-chloro-m-cresol Chemical compound CC1=CC(O)=CC=C1Cl CFKMVGJGLGKFKI-UHFFFAOYSA-N 0.000 description 1
- 241001519451 Abramis brama Species 0.000 description 1
- 102220470114 Aldo-keto reductase family 1 member C2_L42E_mutation Human genes 0.000 description 1
- CPELXLSAUQHCOX-UHFFFAOYSA-M Bromide Chemical compound [Br-] CPELXLSAUQHCOX-UHFFFAOYSA-M 0.000 description 1
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 1
- 229920002134 Carboxymethyl cellulose Polymers 0.000 description 1
- VEXZGXHMUGYJMC-UHFFFAOYSA-M Chloride anion Chemical compound [Cl-] VEXZGXHMUGYJMC-UHFFFAOYSA-M 0.000 description 1
- 102000012410 DNA Ligases Human genes 0.000 description 1
- 108010061982 DNA Ligases Proteins 0.000 description 1
- 108010076804 DNA Restriction Enzymes Proteins 0.000 description 1
- 108010053770 Deoxyribonucleases Proteins 0.000 description 1
- 102000016911 Deoxyribonucleases Human genes 0.000 description 1
- 241000701959 Escherichia virus Lambda Species 0.000 description 1
- OTMSDBZUPAUEDD-UHFFFAOYSA-N Ethane Chemical compound CC OTMSDBZUPAUEDD-UHFFFAOYSA-N 0.000 description 1
- 101710196208 Fibrinolytic enzyme Proteins 0.000 description 1
- 108010010803 Gelatin Proteins 0.000 description 1
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 1
- 239000002202 Polyethylene glycol Substances 0.000 description 1
- 108010083644 Ribonucleases Proteins 0.000 description 1
- 102000006382 Ribonucleases Human genes 0.000 description 1
- 101150076271 SAK gene Proteins 0.000 description 1
- 241000191967 Staphylococcus aureus Species 0.000 description 1
- 241000194017 Streptococcus Species 0.000 description 1
- 108010023197 Streptokinase Proteins 0.000 description 1
- 108090000435 Urokinase-type plasminogen activator Proteins 0.000 description 1
- 102000003990 Urokinase-type plasminogen activator Human genes 0.000 description 1
- OSFRXFWEODRNCZ-UHFFFAOYSA-M [Cl-].Br.[Cs+] Chemical compound [Cl-].Br.[Cs+] OSFRXFWEODRNCZ-UHFFFAOYSA-M 0.000 description 1
- VJHCJDRQFCCTHL-UHFFFAOYSA-N acetic acid 2,3,4,5,6-pentahydroxyhexanal Chemical compound CC(O)=O.OCC(O)C(O)C(O)C(O)C=O VJHCJDRQFCCTHL-UHFFFAOYSA-N 0.000 description 1
- 238000005377 adsorption chromatography Methods 0.000 description 1
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 1
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 1
- 235000011130 ammonium sulphate Nutrition 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 244000052616 bacterial pathogen Species 0.000 description 1
- 244000309464 bull Species 0.000 description 1
- 239000001110 calcium chloride Substances 0.000 description 1
- 235000011148 calcium chloride Nutrition 0.000 description 1
- 229910001628 calcium chloride Inorganic materials 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 210000002421 cell wall Anatomy 0.000 description 1
- 229960005091 chloramphenicol Drugs 0.000 description 1
- WIIZWVCIJKGZOK-RKDXNWHRSA-N chloramphenicol Chemical compound ClC(Cl)C(=O)N[C@H](CO)[C@H](O)C1=CC=C([N+]([O-])=O)C=C1 WIIZWVCIJKGZOK-RKDXNWHRSA-N 0.000 description 1
- RCTYPNKXASFOBE-UHFFFAOYSA-M chloromercury Chemical compound [Hg]Cl RCTYPNKXASFOBE-UHFFFAOYSA-M 0.000 description 1
- 239000012228 culture supernatant Substances 0.000 description 1
- 210000004748 cultured cell Anatomy 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- -1 disodium salt Chemical class 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 230000002538 fungal effect Effects 0.000 description 1
- 238000001641 gel filtration chromatography Methods 0.000 description 1
- 238000005227 gel permeation chromatography Methods 0.000 description 1
- 239000008273 gelatin Substances 0.000 description 1
- 229920000159 gelatin Polymers 0.000 description 1
- 235000019322 gelatine Nutrition 0.000 description 1
- 235000011852 gelatine desserts Nutrition 0.000 description 1
- 238000003306 harvesting Methods 0.000 description 1
- 238000000703 high-speed centrifugation Methods 0.000 description 1
- 230000001771 impaired effect Effects 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 238000009776 industrial production Methods 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 230000001320 lysogenic effect Effects 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 235000021317 phosphate Nutrition 0.000 description 1
- 235000011007 phosphoric acid Nutrition 0.000 description 1
- 150000003013 phosphoric acid derivatives Chemical class 0.000 description 1
- 150000003016 phosphoric acids Chemical class 0.000 description 1
- 229940012957 plasmin Drugs 0.000 description 1
- 229920001223 polyethylene glycol Polymers 0.000 description 1
- 230000000644 propagated effect Effects 0.000 description 1
- 230000010076 replication Effects 0.000 description 1
- 238000005185 salting out Methods 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 230000007928 solubilization Effects 0.000 description 1
- 238000005063 solubilization Methods 0.000 description 1
- 229960005202 streptokinase Drugs 0.000 description 1
- 239000012134 supernatant fraction Substances 0.000 description 1
- 230000009466 transformation Effects 0.000 description 1
- 210000002700 urine Anatomy 0.000 description 1
- 229960005356 urokinase Drugs 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 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
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/305—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Micrococcaceae (F)
- C07K14/31—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Micrococcaceae (F) from Staphylococcus (G)
-
- 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)
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Genetics & Genomics (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biochemistry (AREA)
- Zoology (AREA)
- Molecular Biology (AREA)
- Wood Science & Technology (AREA)
- General Health & Medical Sciences (AREA)
- Biotechnology (AREA)
- Biomedical Technology (AREA)
- Biophysics (AREA)
- General Engineering & Computer Science (AREA)
- Medicinal Chemistry (AREA)
- Gastroenterology & Hepatology (AREA)
- Microbiology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Physics & Mathematics (AREA)
- Plant Pathology (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Enzymes And Modification Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP56164064A JPS5867181A (ja) | 1981-10-16 | 1981-10-16 | スタフイロキナーゼ産生遺伝情報を担うｄｎａ断片組み換え体ｄｎａおよびそれを導入した大腸菌 |
| JP81-164064 | 1982-10-16 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| KR840002029A KR840002029A (ko) | 1984-06-11 |
| KR910001807B1 true KR910001807B1 (ko) | 1991-03-26 |
Family
ID=15786090
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| KR8204582A Expired KR910001807B1 (ko) | 1981-10-16 | 1982-10-12 | 스태필로키나아제를 생산하는 유전자를 함유하는 새로운 대장균 및 스태필로키나아제의 제조법 |
Country Status (7)
| Country | Link |
|---|---|
| US (1) | US4532211A (enExample) |
| EP (1) | EP0077664B1 (enExample) |
| JP (1) | JPS5867181A (enExample) |
| KR (1) | KR910001807B1 (enExample) |
| CA (1) | CA1206109A (enExample) |
| DE (1) | DE3280175D1 (enExample) |
| DK (1) | DK164001C (enExample) |
Families Citing this family (12)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| AU561372B2 (en) * | 1983-10-10 | 1987-05-07 | Board Of Regents Of The University Of Oklahoma, The | Streptokinase-coding recombinant vectors |
| US4764469A (en) * | 1984-03-02 | 1988-08-16 | Board Of Regents For The University Of Oklahoma | Streptokinase-coding recombinant vectors |
| US5066589A (en) * | 1984-03-02 | 1991-11-19 | Board Of Regents Of The University Of Okla. | Streptokinase-coding recombinant vectors |
| US5683909A (en) * | 1984-03-02 | 1997-11-04 | Van Den Bergh Foods Company, Division Of Conopco, Inc. | Plasmids replicatable in Bacillus subtilis, E. coli and lactic acid streptococcus bacteria |
| IL76422A0 (en) * | 1984-09-26 | 1986-01-31 | Lilly Co Eli | Method for expression and secretion in bacillus |
| IT1176997B (it) * | 1984-10-17 | 1987-08-26 | Anic Spa | Procedimento per la produzione di proteasi neutra |
| DE68912383T3 (de) * | 1988-04-14 | 1999-06-02 | Kabushiki Kaisha Yakult Honsha, Tokio/Tokyo | Plasminogenaktivator und thrombolytischer Wirkstoff. |
| ES2089784T3 (es) * | 1991-12-30 | 1996-10-01 | Medac Klinische Spezialpraep | Expresion de estafilocinasas sin peptido de señal. |
| CN1035192C (zh) * | 1994-04-04 | 1997-06-18 | 上海医科大学 | 一种重组葡激酶的制备方法 |
| US6383483B1 (en) | 1995-01-06 | 2002-05-07 | Désiré José Collen | Staphylokinase derivatives with cysteine substitutions |
| US5951980A (en) * | 1995-01-06 | 1999-09-14 | Leuven Research & Development Vzw | Identification, production and use of new staphylokinase derivatives with reduced immunogenicity |
| RU2156299C1 (ru) * | 1999-02-03 | 2000-09-20 | Закрытое акционерное общество "Фосфосорб" | Рекомбинантная плазмидная днк, кодирующая полную последовательность стафилокиназы, штамм escherichia coli sa 9325 - продуцент рекомбинантного белка |
Family Cites Families (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4366246A (en) * | 1977-11-08 | 1982-12-28 | Genentech, Inc. | Method for microbial polypeptide expression |
| JPS54107589A (en) * | 1978-02-09 | 1979-08-23 | Ajinomoto Co Inc | Separation and purification of staphylokinase |
-
1981
- 1981-10-16 JP JP56164064A patent/JPS5867181A/ja active Granted
-
1982
- 1982-10-12 KR KR8204582A patent/KR910001807B1/ko not_active Expired
- 1982-10-15 CA CA000413486A patent/CA1206109A/en not_active Expired
- 1982-10-15 DK DK460182A patent/DK164001C/da active
- 1982-10-15 US US06/434,503 patent/US4532211A/en not_active Expired - Lifetime
- 1982-10-15 EP EP82305508A patent/EP0077664B1/en not_active Expired - Lifetime
- 1982-10-15 DE DE8282305508T patent/DE3280175D1/de not_active Expired - Lifetime
Also Published As
| Publication number | Publication date |
|---|---|
| DK164001C (da) | 1992-09-21 |
| EP0077664A2 (en) | 1983-04-27 |
| DK460182A (da) | 1983-04-17 |
| EP0077664B1 (en) | 1990-05-16 |
| EP0077664A3 (en) | 1984-05-02 |
| DE3280175D1 (de) | 1990-06-21 |
| JPH0478276B2 (enExample) | 1992-12-10 |
| CA1206109A (en) | 1986-06-17 |
| JPS5867181A (ja) | 1983-04-21 |
| KR840002029A (ko) | 1984-06-11 |
| US4532211A (en) | 1985-07-30 |
| DK164001B (da) | 1992-04-27 |
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