NO851308L - Genetisk ekspresjon av somatostatin som hybridpolypeptid - Google Patents
Genetisk ekspresjon av somatostatin som hybridpolypeptidInfo
- Publication number
- NO851308L NO851308L NO851308A NO851308A NO851308L NO 851308 L NO851308 L NO 851308L NO 851308 A NO851308 A NO 851308A NO 851308 A NO851308 A NO 851308A NO 851308 L NO851308 L NO 851308L
- Authority
- NO
- Norway
- Prior art keywords
- trp
- trpe
- polypeptide
- tryptophan
- plasmid
- Prior art date
Links
- 108010056088 Somatostatin Proteins 0.000 title claims description 41
- 102000005157 Somatostatin Human genes 0.000 title claims description 32
- NHXLMOGPVYXJNR-ATOGVRKGSA-N somatostatin Chemical compound C([C@H]1C(=O)N[C@H](C(N[C@@H](CO)C(=O)N[C@@H](CSSC[C@@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@@H](CC=2C3=CC=CC=C3NC=2)C(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(=O)N1)[C@@H](C)O)NC(=O)CNC(=O)[C@H](C)N)C(O)=O)=O)[C@H](O)C)C1=CC=CC=C1 NHXLMOGPVYXJNR-ATOGVRKGSA-N 0.000 title claims description 32
- 229920001184 polypeptide Polymers 0.000 title claims description 29
- 108090000765 processed proteins & peptides Proteins 0.000 title claims description 29
- 102000004196 processed proteins & peptides Human genes 0.000 title claims description 29
- 229960000553 somatostatin Drugs 0.000 title claims description 15
- 230000002068 genetic effect Effects 0.000 title description 3
- 108090000623 proteins and genes Proteins 0.000 claims description 34
- 210000004027 cell Anatomy 0.000 claims description 28
- 239000013612 plasmid Substances 0.000 claims description 23
- SIKJAQJRHWYJAI-UHFFFAOYSA-N Indole Chemical compound C1=CC=C2NC=CC2=C1 SIKJAQJRHWYJAI-UHFFFAOYSA-N 0.000 claims description 20
- 241000588724 Escherichia coli Species 0.000 claims description 18
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 claims description 15
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 claims description 15
- 150000001413 amino acids Chemical group 0.000 claims description 15
- 238000000034 method Methods 0.000 claims description 15
- 230000001580 bacterial effect Effects 0.000 claims description 11
- PZOUSPYUWWUPPK-UHFFFAOYSA-N indole Natural products CC1=CC=CC2=C1C=CN2 PZOUSPYUWWUPPK-UHFFFAOYSA-N 0.000 claims description 10
- RKJUIXBNRJVNHR-UHFFFAOYSA-N indolenine Natural products C1=CC=C2CC=NC2=C1 RKJUIXBNRJVNHR-UHFFFAOYSA-N 0.000 claims description 10
- 239000013600 plasmid vector Substances 0.000 claims description 10
- ATDGTVJJHBUTRL-UHFFFAOYSA-N cyanogen bromide Chemical compound BrC#N ATDGTVJJHBUTRL-UHFFFAOYSA-N 0.000 claims description 7
- 241000894006 Bacteria Species 0.000 claims description 6
- 230000005764 inhibitory process Effects 0.000 claims description 5
- 238000005273 aeration Methods 0.000 claims description 4
- 230000010261 cell growth Effects 0.000 claims description 4
- 210000003705 ribosome Anatomy 0.000 claims description 4
- 108020004414 DNA Proteins 0.000 description 12
- 239000002609 medium Substances 0.000 description 12
- 102000004169 proteins and genes Human genes 0.000 description 10
- 238000006243 chemical reaction Methods 0.000 description 6
- 238000010276 construction Methods 0.000 description 6
- 239000002773 nucleotide Substances 0.000 description 6
- 125000003729 nucleotide group Chemical group 0.000 description 6
- 239000012634 fragment Substances 0.000 description 5
- 239000000203 mixture Substances 0.000 description 5
- 108020004705 Codon Proteins 0.000 description 4
- 102000012410 DNA Ligases Human genes 0.000 description 4
- 108010061982 DNA Ligases Proteins 0.000 description 4
- 206010013142 Disinhibition Diseases 0.000 description 4
- 229960000723 ampicillin Drugs 0.000 description 4
- 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 4
- 150000001875 compounds Chemical class 0.000 description 4
- 230000012010 growth Effects 0.000 description 4
- 239000002243 precursor Substances 0.000 description 4
- 108091008146 restriction endonucleases Proteins 0.000 description 4
- 238000003786 synthesis reaction Methods 0.000 description 4
- 238000010367 cloning Methods 0.000 description 3
- 239000013613 expression plasmid Substances 0.000 description 3
- 239000001963 growth medium Substances 0.000 description 3
- 238000004519 manufacturing process Methods 0.000 description 3
- 230000009467 reduction Effects 0.000 description 3
- 102000053602 DNA Human genes 0.000 description 2
- 108091034117 Oligonucleotide Proteins 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- 239000004098 Tetracycline Substances 0.000 description 2
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 2
- 239000007864 aqueous solution Substances 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- 238000003776 cleavage reaction Methods 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 2
- 230000007017 scission Effects 0.000 description 2
- 229960002180 tetracycline Drugs 0.000 description 2
- 229930101283 tetracycline Natural products 0.000 description 2
- 235000019364 tetracycline Nutrition 0.000 description 2
- 150000003522 tetracyclines Chemical class 0.000 description 2
- 230000009466 transformation Effects 0.000 description 2
- 229920001817 Agar Polymers 0.000 description 1
- 108010077805 Bacterial Proteins Proteins 0.000 description 1
- 241000908115 Bolivar Species 0.000 description 1
- CPELXLSAUQHCOX-UHFFFAOYSA-M Bromide Chemical compound [Br-] CPELXLSAUQHCOX-UHFFFAOYSA-M 0.000 description 1
- 241000557626 Corvus corax Species 0.000 description 1
- 108010042407 Endonucleases Proteins 0.000 description 1
- 102000004533 Endonucleases Human genes 0.000 description 1
- 210000000712 G cell Anatomy 0.000 description 1
- 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 1
- 241000124008 Mammalia Species 0.000 description 1
- 108091028043 Nucleic acid sequence Proteins 0.000 description 1
- 239000004793 Polystyrene Substances 0.000 description 1
- 108010076504 Protein Sorting Signals Proteins 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- -1 SS14 amino acids Chemical class 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- 108700005078 Synthetic Genes Proteins 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 239000008272 agar Substances 0.000 description 1
- 239000011543 agarose gel Substances 0.000 description 1
- 238000000246 agarose gel electrophoresis Methods 0.000 description 1
- 238000013019 agitation 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
- 238000004458 analytical method Methods 0.000 description 1
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 1
- 229940041514 candida albicans extract Drugs 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 239000003638 chemical reducing agent Substances 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 239000013611 chromosomal DNA Substances 0.000 description 1
- 230000002759 chromosomal effect Effects 0.000 description 1
- 210000000349 chromosome Anatomy 0.000 description 1
- 238000010924 continuous production Methods 0.000 description 1
- 238000012217 deletion Methods 0.000 description 1
- 230000037430 deletion Effects 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 239000000284 extract Substances 0.000 description 1
- 108020001507 fusion proteins Proteins 0.000 description 1
- 102000037865 fusion proteins Human genes 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 229940088597 hormone Drugs 0.000 description 1
- 239000005556 hormone Substances 0.000 description 1
- 238000003119 immunoblot Methods 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 239000000813 peptide hormone Substances 0.000 description 1
- 229920002223 polystyrene Polymers 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 230000009711 regulatory function Effects 0.000 description 1
- 230000010076 replication Effects 0.000 description 1
- 239000007320 rich medium Substances 0.000 description 1
- 230000035945 sensitivity Effects 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 239000007790 solid phase Substances 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000012137 tryptone Substances 0.000 description 1
- 239000012138 yeast extract Substances 0.000 description 1
Classifications
-
- 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
- C07K14/575—Hormones
- C07K14/655—Somatostatins
-
- 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
- C12N15/09—Recombinant DNA-technology
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
- C12N15/62—DNA sequences coding for fusion proteins
-
- 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
- C12N15/09—Recombinant DNA-technology
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/70—Vectors or expression systems specially adapted for E. coli
- C12N15/71—Expression systems using regulatory sequences derived from the trp-operon
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/01—Fusion polypeptide containing a localisation/targetting motif
- C07K2319/02—Fusion polypeptide containing a localisation/targetting motif containing a signal sequence
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/61—Fusion polypeptide containing an enzyme fusion for detection (lacZ, luciferase)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/70—Fusion polypeptide containing domain for protein-protein interaction
- C07K2319/74—Fusion polypeptide containing domain for protein-protein interaction containing a fusion for binding to a cell surface receptor
- C07K2319/75—Fusion polypeptide containing domain for protein-protein interaction containing a fusion for binding to a cell surface receptor containing a fusion for activation of a cell surface receptor, e.g. thrombopoeitin, NPY and other peptide hormones
Landscapes
- Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Zoology (AREA)
- Biomedical Technology (AREA)
- Biotechnology (AREA)
- Wood Science & Technology (AREA)
- Molecular Biology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Microbiology (AREA)
- Plant Pathology (AREA)
- Physics & Mathematics (AREA)
- Toxicology (AREA)
- Endocrinology (AREA)
- Gastroenterology & Hepatology (AREA)
- Medicinal Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| IT47976/84A IT1198443B (it) | 1984-03-30 | 1984-03-30 | Espressione genetica di polipeptidi ibridi contenenti la sequenza della somatostatina |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| NO851308L true NO851308L (no) | 1985-10-01 |
Family
ID=11263727
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| NO851308A NO851308L (no) | 1984-03-30 | 1985-03-29 | Genetisk ekspresjon av somatostatin som hybridpolypeptid |
Country Status (11)
| Country | Link |
|---|---|
| EP (1) | EP0160190A3 (fr) |
| JP (1) | JPS615788A (fr) |
| AU (2) | AU4046185A (fr) |
| CA (1) | CA1301676C (fr) |
| DK (1) | DK131285A (fr) |
| ES (1) | ES8605284A1 (fr) |
| FI (1) | FI851288L (fr) |
| IL (1) | IL74620A (fr) |
| IT (1) | IT1198443B (fr) |
| NO (1) | NO851308L (fr) |
| ZA (1) | ZA852035B (fr) |
Families Citing this family (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| IT1234977B (it) * | 1985-03-22 | 1992-06-09 | Serono Ist Farm | Espressione in e. coli polipeptidi ibridi contenenti la sequenza del fattore di rilascio dell'ormone della crescita |
| JPS63304996A (ja) * | 1987-06-04 | 1988-12-13 | Toray Ind Inc | 融合タンパク質およびその製造方法 |
| JPH0722517B2 (ja) * | 1989-08-24 | 1995-03-15 | 株式会社三和化学研究所 | モチリン様ポリペプチドの製法並びにそのための組換えｄｎａ及び発現用プラスミド |
Family Cites Families (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| BG38165A3 (en) * | 1977-11-08 | 1985-10-15 | Genentech, Inc. | Method for preparing recombinant cloning vector suitable for transformation of microbial receptor |
| GB2052516B (en) * | 1979-06-01 | 1983-06-29 | Searle & Co | Plasmid vectors production and use thereof |
| IE52122B1 (en) * | 1980-08-25 | 1987-06-24 | Univ California | Somatostatin or somatostatin precursors |
| EP0068719A3 (fr) * | 1981-06-16 | 1984-03-28 | Takeda Chemical Industries, Ltd. | Acides désoxyribonucléiques, leur production et utilisation |
| JPS59203495A (ja) * | 1983-04-28 | 1984-11-17 | Kyowa Hakko Kogyo Co Ltd | 外来遺伝子の新規な発現方法 |
-
1984
- 1984-03-30 IT IT47976/84A patent/IT1198443B/it active
-
1985
- 1985-03-13 EP EP85102891A patent/EP0160190A3/fr not_active Withdrawn
- 1985-03-15 IL IL74620A patent/IL74620A/xx unknown
- 1985-03-19 ZA ZA852035A patent/ZA852035B/xx unknown
- 1985-03-22 DK DK131285A patent/DK131285A/da not_active Application Discontinuation
- 1985-03-28 AU AU40461/85A patent/AU4046185A/en not_active Abandoned
- 1985-03-29 CA CA000477979A patent/CA1301676C/fr not_active Expired - Lifetime
- 1985-03-29 ES ES541782A patent/ES8605284A1/es not_active Expired
- 1985-03-29 NO NO851308A patent/NO851308L/no unknown
- 1985-03-29 FI FI851288A patent/FI851288L/fi not_active Application Discontinuation
- 1985-03-30 JP JP60065088A patent/JPS615788A/ja active Pending
-
1989
- 1989-08-11 AU AU39547/89A patent/AU611048B2/en not_active Ceased
Also Published As
| Publication number | Publication date |
|---|---|
| IL74620A (en) | 1990-12-23 |
| AU611048B2 (en) | 1991-05-30 |
| AU3954789A (en) | 1989-11-30 |
| EP0160190A3 (fr) | 1987-07-15 |
| IT8447976A0 (it) | 1984-03-30 |
| FI851288L (fi) | 1985-10-01 |
| EP0160190A2 (fr) | 1985-11-06 |
| CA1301676C (fr) | 1992-05-26 |
| ZA852035B (en) | 1985-11-27 |
| DK131285A (da) | 1985-10-01 |
| DK131285D0 (da) | 1985-03-22 |
| IL74620A0 (en) | 1985-06-30 |
| FI851288A0 (fi) | 1985-03-29 |
| ES8605284A1 (es) | 1986-04-01 |
| JPS615788A (ja) | 1986-01-11 |
| ES541782A0 (es) | 1986-04-01 |
| AU4046185A (en) | 1985-10-31 |
| IT1198443B (it) | 1988-12-21 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| AU648670B2 (en) | A-C-B Proinsulin, method of manufacturing and using same, and intermediates in insulin production | |
| EP0489780B1 (fr) | Preparation de proteines de fusion | |
| JP3878207B2 (ja) | ｏｓｍＢ プロモータで制御される発現プラスミド | |
| JPH06502548A (ja) | 特にコリネバクテリア中で用いることのできる蛋白質の発現および分泌系 | |
| AU607973B2 (en) | Process for production of physiologically active peptide containing cysteine residue | |
| Tsurimoto et al. | Bacteriophage lambda initiators: preparation from a strain that overproduces the O and P proteins | |
| KR101026526B1 (ko) | 대장균에서 외래단백질을 분비 생산하는 방법 | |
| JPH03503596A (ja) | 蛋白質若しくはポリペプチドの調製方法、該ポリペプチドをコードするｄｎａ配列、該ｄｎａ配列およびポリペプチドを有する微生物および該ポリペプチドの薬学的製剤としての利用 | |
| FI93125B (fi) | Kasvuhormonia vapauttavan tekijän sekvenssin sisältävien hybridipolypeptidien ilmentäminen E. colissa | |
| Emerick et al. | Expression of a β-lactamase preproinsulin fusion protein in Escherichia coli | |
| NO851308L (no) | Genetisk ekspresjon av somatostatin som hybridpolypeptid | |
| US5643791A (en) | Characterization and structure of an endodglucanase gene of Cellulomonas fimi | |
| Lepage et al. | Recombinant technology as an alternative to chemical peptide synthesis: Expression and characterization of HIV-1 Rev recombinant peptides | |
| US5378613A (en) | Method for increased expression of low molecular weight recombinant polypeptides | |
| DK156072B (da) | Syntetisk dna-sekvens indeholdende et ribosombindingssted | |
| FI97549C (fi) | Menetelmä vierasproteiinien valmistamiseksi Streptomycessoluissa | |
| JPS61149089A (ja) | Ｄｎａ塩基配列、ポリペプチド分泌発現ベクター及び形質転換微生物 | |
| EP0361956A2 (fr) | Expression augmentée de protéines recombinantes à faible poids moléculaire | |
| US5268278A (en) | Genetic expression of somatostatin as hybrid polypeptide | |
| RU2325440C1 (ru) | РЕКОМБИНАНТНАЯ ПЛАЗМИДНАЯ ДНК pGG-1, КОДИРУЮЩАЯ ПОЛИПЕПТИД ПРОИНСУЛИНА GLARGIN ЧЕЛОВЕКА И ШТАММ БАКТЕРИЙ ESCHERICHIA COLI BGG18 - ПРОДУЦЕНТ РЕКОМБИНАНТНОГО ПРОИНСУЛИНА GLARGIN | |
| Roytrakul et al. | A Rapid and Simple Method for Construction and Expression of a Synthetic | |
| JPH02257883A (ja) | シグナルペプチド、ｄｎａ配列、ベクター、細菌、およびポリペプチド周辺質生産法 | |
| JPH08103278A (ja) | 活性型ヒトａｌｔの製造方法 | |
| CA2232841A1 (fr) | Procede de production de peptides natriuretiques par l'intermediaire de proteines de fusion de streptavidine | |
| JPH0928380A (ja) | ニトリラーゼ遺伝子発現に関わる調節因子およびその遺伝子 |