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)
- Biomedical Technology (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Molecular Biology (AREA)
- Biotechnology (AREA)
- General Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (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 (fi) |
| JP (1) | JPS615788A (fi) |
| AU (2) | AU4046185A (fi) |
| CA (1) | CA1301676C (fi) |
| DK (1) | DK131285A (fi) |
| ES (1) | ES8605284A1 (fi) |
| FI (1) | FI851288L (fi) |
| IL (1) | IL74620A (fi) |
| IT (1) | IT1198443B (fi) |
| NO (1) | NO851308L (fi) |
| ZA (1) | ZA852035B (fi) |
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 |
|---|---|---|---|---|
| DK173092B1 (da) * | 1977-11-08 | 2000-01-10 | Genentech Inc | Rekombinant plasmid, fremgangsmåde til fremstilling af plasmidet, bakterie indeholdende plasmidet, samt fremgangsmåde til f |
| AU542264B2 (en) * | 1979-06-01 | 1985-02-14 | G.D. Searle & Co. | Plasmid vectors |
| IE52122B1 (en) * | 1980-08-25 | 1987-06-24 | Univ California | Somatostatin or somatostatin precursors |
| EP0068719A3 (en) * | 1981-06-16 | 1984-03-28 | Takeda Chemical Industries, Ltd. | Deoxyribonucleic acids, their production and use |
| 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/en 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 NO NO851308A patent/NO851308L/no unknown
- 1985-03-29 CA CA000477979A patent/CA1301676C/en not_active Expired - Lifetime
- 1985-03-29 ES ES541782A patent/ES8605284A1/es not_active Expired
- 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 |
|---|---|
| ES8605284A1 (es) | 1986-04-01 |
| IL74620A (en) | 1990-12-23 |
| AU611048B2 (en) | 1991-05-30 |
| CA1301676C (en) | 1992-05-26 |
| IT8447976A0 (it) | 1984-03-30 |
| DK131285D0 (da) | 1985-03-22 |
| ES541782A0 (es) | 1986-04-01 |
| IL74620A0 (en) | 1985-06-30 |
| FI851288L (fi) | 1985-10-01 |
| AU3954789A (en) | 1989-11-30 |
| AU4046185A (en) | 1985-10-31 |
| ZA852035B (en) | 1985-11-27 |
| IT1198443B (it) | 1988-12-21 |
| EP0160190A3 (en) | 1987-07-15 |
| EP0160190A2 (en) | 1985-11-06 |
| FI851288A0 (fi) | 1985-03-29 |
| JPS615788A (ja) | 1986-01-11 |
| DK131285A (da) | 1985-10-01 |
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