NO830682L - Rekombinant plasmid for fremstilling av humaninsulin - Google Patents
Rekombinant plasmid for fremstilling av humaninsulinInfo
- Publication number
- NO830682L NO830682L NO830682A NO830682A NO830682L NO 830682 L NO830682 L NO 830682L NO 830682 A NO830682 A NO 830682A NO 830682 A NO830682 A NO 830682A NO 830682 L NO830682 L NO 830682L
- Authority
- NO
- Norway
- Prior art keywords
- preproinsulin
- human
- human proinsulin
- host
- proinsulin
- Prior art date
Links
- 239000013612 plasmid Substances 0.000 title claims description 58
- 101000976075 Homo sapiens Insulin Proteins 0.000 title claims description 17
- PBGKTOXHQIOBKM-FHFVDXKLSA-N insulin (human) Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@H]1CSSC[C@H]2C(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@H](C(=O)N[C@H](C(N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=3C=CC(O)=CC=3)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=3NC=NC=3)NC(=O)[C@H](CO)NC(=O)CNC1=O)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)NCC(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H]([C@@H](C)O)C(O)=O)C(=O)N[C@@H](CC(N)=O)C(O)=O)=O)CSSC[C@@H](C(N2)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@@H](NC(=O)CN)[C@@H](C)CC)[C@@H](C)CC)[C@@H](C)O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](NC(=O)[C@@H](N)CC=1C=CC=CC=1)C(C)C)C1=CN=CN1 PBGKTOXHQIOBKM-FHFVDXKLSA-N 0.000 title claims description 16
- 238000004519 manufacturing process Methods 0.000 title claims description 9
- 108010076181 Proinsulin Proteins 0.000 claims description 68
- 108010066381 preproinsulin Proteins 0.000 claims description 34
- 108090000623 proteins and genes Proteins 0.000 claims description 27
- 238000000034 method Methods 0.000 claims description 18
- 108020004414 DNA Proteins 0.000 claims description 10
- 210000000170 cell membrane Anatomy 0.000 claims description 8
- 238000000338 in vitro Methods 0.000 claims description 8
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 7
- 238000001727 in vivo Methods 0.000 claims description 7
- 241000588724 Escherichia coli Species 0.000 claims description 6
- 230000008569 process Effects 0.000 claims description 4
- 238000012545 processing Methods 0.000 claims description 4
- 108091026890 Coding region Proteins 0.000 claims description 3
- 108091081024 Start codon Proteins 0.000 claims description 3
- 230000001131 transforming effect Effects 0.000 claims description 3
- 241001646716 Escherichia coli K-12 Species 0.000 claims description 2
- 239000013599 cloning vector Substances 0.000 claims 7
- 239000013598 vector Substances 0.000 claims 2
- NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 69
- 108090001061 Insulin Proteins 0.000 description 35
- 229940125396 insulin Drugs 0.000 description 35
- 102000004877 Insulin Human genes 0.000 description 34
- 239000000047 product Substances 0.000 description 19
- 230000032258 transport Effects 0.000 description 16
- 108090000765 processed proteins & peptides Proteins 0.000 description 14
- VOUAQYXWVJDEQY-QENPJCQMSA-N 33017-11-7 Chemical compound OC(=O)CC[C@H](N)C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](C(C)C)C(=O)NCC(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)NCC(=O)NCC(=O)N1CCC[C@H]1C(=O)NCC(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N1[C@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(O)=O)CCC1 VOUAQYXWVJDEQY-QENPJCQMSA-N 0.000 description 10
- 235000018102 proteins Nutrition 0.000 description 9
- 102000004169 proteins and genes Human genes 0.000 description 9
- 241000894006 Bacteria Species 0.000 description 8
- 238000002474 experimental method Methods 0.000 description 8
- 230000001580 bacterial effect Effects 0.000 description 7
- 239000000499 gel Substances 0.000 description 6
- 108010075254 C-Peptide Proteins 0.000 description 5
- 102000004142 Trypsin Human genes 0.000 description 5
- 108090000631 Trypsin Proteins 0.000 description 5
- 239000002299 complementary DNA Substances 0.000 description 5
- 239000012588 trypsin Substances 0.000 description 5
- 241001465754 Metazoa Species 0.000 description 4
- 230000015556 catabolic process Effects 0.000 description 4
- 238000010276 construction Methods 0.000 description 4
- 238000006731 degradation reaction Methods 0.000 description 4
- 239000012634 fragment Substances 0.000 description 4
- 238000002523 gelfiltration Methods 0.000 description 4
- 239000012133 immunoprecipitate Substances 0.000 description 4
- 230000003204 osmotic effect Effects 0.000 description 4
- 210000001322 periplasm Anatomy 0.000 description 4
- 210000004739 secretory vesicle Anatomy 0.000 description 4
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
- 241000283690 Bos taurus Species 0.000 description 3
- 108090000204 Dipeptidase 1 Proteins 0.000 description 3
- 235000001014 amino acid Nutrition 0.000 description 3
- 150000001413 amino acids Chemical group 0.000 description 3
- 230000015572 biosynthetic process Effects 0.000 description 3
- 238000012512 characterization method Methods 0.000 description 3
- 239000000463 material Substances 0.000 description 3
- 238000012986 modification Methods 0.000 description 3
- 230000004048 modification Effects 0.000 description 3
- 239000000813 peptide hormone Substances 0.000 description 3
- 239000002243 precursor Substances 0.000 description 3
- 102000004196 processed proteins & peptides Human genes 0.000 description 3
- 108091008146 restriction endonucleases Proteins 0.000 description 3
- 241000894007 species Species 0.000 description 3
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 2
- 108060002716 Exonuclease Proteins 0.000 description 2
- 108010087702 Penicillinase Proteins 0.000 description 2
- 102000035195 Peptidases Human genes 0.000 description 2
- 108091005804 Peptidases Proteins 0.000 description 2
- 239000004365 Protease Substances 0.000 description 2
- 108010076504 Protein Sorting Signals Proteins 0.000 description 2
- 108020004511 Recombinant DNA Proteins 0.000 description 2
- 230000008955 bacterial trafficking Effects 0.000 description 2
- 108010005774 beta-Galactosidase Proteins 0.000 description 2
- 102000006635 beta-lactamase Human genes 0.000 description 2
- 210000004027 cell Anatomy 0.000 description 2
- 210000002421 cell wall Anatomy 0.000 description 2
- 238000006243 chemical reaction Methods 0.000 description 2
- 238000003776 cleavage reaction Methods 0.000 description 2
- 206010012601 diabetes mellitus Diseases 0.000 description 2
- XBDQKXXYIPTUBI-UHFFFAOYSA-N dimethylselenoniopropionate Natural products CCC(O)=O XBDQKXXYIPTUBI-UHFFFAOYSA-N 0.000 description 2
- 238000001962 electrophoresis Methods 0.000 description 2
- 102000013165 exonuclease Human genes 0.000 description 2
- 210000002288 golgi apparatus Anatomy 0.000 description 2
- 230000007246 mechanism Effects 0.000 description 2
- 239000002773 nucleotide Substances 0.000 description 2
- 125000003729 nucleotide group Chemical group 0.000 description 2
- 229950009506 penicillinase Drugs 0.000 description 2
- 229920001184 polypeptide Polymers 0.000 description 2
- 238000003127 radioimmunoassay Methods 0.000 description 2
- 230000007017 scission Effects 0.000 description 2
- 230000028327 secretion Effects 0.000 description 2
- 238000006467 substitution reaction Methods 0.000 description 2
- 230000000153 supplemental effect Effects 0.000 description 2
- 230000009466 transformation Effects 0.000 description 2
- 235000002374 tyrosine Nutrition 0.000 description 2
- 125000001493 tyrosinyl group Chemical class [H]OC1=C([H])C([H])=C(C([H])=C1[H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 2
- HRPVXLWXLXDGHG-UHFFFAOYSA-N Acrylamide Chemical compound NC(=O)C=C HRPVXLWXLXDGHG-UHFFFAOYSA-N 0.000 description 1
- 229920000936 Agarose Polymers 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- 102000003670 Carboxypeptidase B Human genes 0.000 description 1
- 108090000087 Carboxypeptidase B Proteins 0.000 description 1
- 108010078791 Carrier Proteins Proteins 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- 108010047524 Deoxyribonuclease HindIII Proteins 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 241000206602 Eukaryota Species 0.000 description 1
- 108700039691 Genetic Promoter Regions Proteins 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 101500025353 Homo sapiens Insulin A chain Proteins 0.000 description 1
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 108010067035 Pancrelipase Proteins 0.000 description 1
- 238000012300 Sequence Analysis Methods 0.000 description 1
- NINIDFKCEFEMDL-UHFFFAOYSA-N Sulfur Chemical compound [S] NINIDFKCEFEMDL-UHFFFAOYSA-N 0.000 description 1
- 239000004098 Tetracycline Substances 0.000 description 1
- HCHKCACWOHOZIP-UHFFFAOYSA-N Zinc Chemical compound [Zn] HCHKCACWOHOZIP-UHFFFAOYSA-N 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 210000000227 basophil cell of anterior lobe of hypophysis Anatomy 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 102000005936 beta-Galactosidase Human genes 0.000 description 1
- 238000002144 chemical decomposition reaction Methods 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 239000002131 composite material Substances 0.000 description 1
- 238000009833 condensation Methods 0.000 description 1
- 230000005494 condensation Effects 0.000 description 1
- 238000012790 confirmation Methods 0.000 description 1
- 230000009260 cross reactivity Effects 0.000 description 1
- 230000002950 deficient Effects 0.000 description 1
- 230000000694 effects Effects 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 230000001747 exhibiting effect Effects 0.000 description 1
- 108010092809 exonuclease Bal 31 Proteins 0.000 description 1
- 239000013613 expression plasmid Substances 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 230000004927 fusion Effects 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 150000004678 hydrides Chemical class 0.000 description 1
- 238000003018 immunoassay Methods 0.000 description 1
- 230000002163 immunogen Effects 0.000 description 1
- 238000001114 immunoprecipitation Methods 0.000 description 1
- 238000011065 in-situ storage Methods 0.000 description 1
- 239000003999 initiator Substances 0.000 description 1
- 210000004153 islets of langerhan Anatomy 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- 230000002503 metabolic effect Effects 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 210000000496 pancreas Anatomy 0.000 description 1
- 230000000135 prohibitive effect Effects 0.000 description 1
- 235000019260 propionic acid Nutrition 0.000 description 1
- IUVKMZGDUIUOCP-BTNSXGMBSA-N quinbolone Chemical compound O([C@H]1CC[C@H]2[C@H]3[C@@H]([C@]4(C=CC(=O)C=C4CC3)C)CC[C@@]21C)C1=CCCC1 IUVKMZGDUIUOCP-BTNSXGMBSA-N 0.000 description 1
- 238000010188 recombinant method Methods 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 210000003660 reticulum Anatomy 0.000 description 1
- 210000003705 ribosome Anatomy 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- 229910052717 sulfur Inorganic materials 0.000 description 1
- 239000011593 sulfur Substances 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 229960002180 tetracycline Drugs 0.000 description 1
- 229930101283 tetracycline Natural products 0.000 description 1
- 235000019364 tetracycline Nutrition 0.000 description 1
- 150000003522 tetracyclines Chemical class 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- 230000007723 transport mechanism Effects 0.000 description 1
- 238000010396 two-hybrid screening Methods 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- 238000011144 upstream manufacturing Methods 0.000 description 1
- 239000011701 zinc Substances 0.000 description 1
- 229910052725 zinc Inorganic materials 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
- 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
- C12N15/625—DNA sequences coding for fusion proteins containing a sequence coding for a signal sequence
-
- 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
- C07K14/62—Insulins
-
- 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
- C07K2319/70—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)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Organic Chemistry (AREA)
- Zoology (AREA)
- Biomedical Technology (AREA)
- Molecular Biology (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Health & Medical Sciences (AREA)
- Wood Science & Technology (AREA)
- General Engineering & Computer Science (AREA)
- Biotechnology (AREA)
- Physics & Mathematics (AREA)
- Microbiology (AREA)
- Plant Pathology (AREA)
- Diabetes (AREA)
- Endocrinology (AREA)
- Toxicology (AREA)
- Gastroenterology & Hepatology (AREA)
- Medicinal Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US27833181A | 1981-06-29 | 1981-06-29 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| NO830682L true NO830682L (no) | 1983-02-28 |
Family
ID=23064574
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| NO830682A NO830682L (no) | 1981-06-29 | 1983-02-28 | Rekombinant plasmid for fremstilling av humaninsulin |
Country Status (12)
| Country | Link |
|---|---|
| US (1) | USH245H (es) |
| EP (1) | EP0070632A3 (es) |
| JP (1) | JPS58501227A (es) |
| AU (1) | AU556980B2 (es) |
| CA (1) | CA1201074A (es) |
| DK (1) | DK84583A (es) |
| ES (1) | ES513522A0 (es) |
| IL (1) | IL66102A0 (es) |
| NO (1) | NO830682L (es) |
| PT (1) | PT75075B (es) |
| WO (1) | WO1983000164A1 (es) |
| ZA (1) | ZA824218B (es) |
Families Citing this family (11)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1983003413A1 (en) * | 1982-03-31 | 1983-10-13 | Genetics Inst | Creation of dna sequences encoding modified proinsulin precursors |
| DE3245665A1 (de) * | 1982-05-04 | 1983-11-10 | Boehringer Mannheim Gmbh, 6800 Mannheim | Verfahren zur herstellung permanenter tierischer und humaner zellinien und deren verwendung |
| US5670371A (en) * | 1983-07-15 | 1997-09-23 | Bio-Technology General Corp. | Bacterial expression of superoxide dismutase |
| DK58285D0 (da) * | 1984-05-30 | 1985-02-08 | Novo Industri As | Peptider samt fremstilling og anvendelse deraf |
| US4767709A (en) | 1984-06-28 | 1988-08-30 | The Johns Hopkins University | Growth-related hormones |
| PH25772A (en) * | 1985-08-30 | 1991-10-18 | Novo Industri As | Insulin analogues, process for their preparation |
| US5496924A (en) * | 1985-11-27 | 1996-03-05 | Hoechst Aktiengesellschaft | Fusion protein comprising an interleukin-2 fragment ballast portion |
| ES2090006T3 (es) * | 1986-05-20 | 1996-10-16 | Gen Hospital Corp | Evaluacion de la expresion de preproinsulina, proinsulina o insulina. |
| US6348327B1 (en) * | 1991-12-06 | 2002-02-19 | Genentech, Inc. | Non-endocrine animal host cells capable of expressing variant proinsulin and processing the same to form active, mature insulin and methods of culturing such cells |
| US6001604A (en) * | 1993-12-29 | 1999-12-14 | Bio-Technology General Corp. | Refolding of proinsulins without addition of reducing agents |
| US20180057920A1 (en) * | 2016-08-31 | 2018-03-01 | General Electric Company | Grain refinement in in706 using laves phase precipitation |
Family Cites Families (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS5210872B2 (es) * | 1973-07-14 | 1977-03-26 | ||
| US4082613A (en) * | 1976-04-23 | 1978-04-04 | The Regents Of The University Of Minnesota | Process for the production of insulin by genetically transformed fungal cells |
| US4411994A (en) * | 1978-06-08 | 1983-10-25 | The President And Fellows Of Harvard College | Protein synthesis |
| GR71912B (es) * | 1978-08-11 | 1983-08-16 | Univ California | |
| GR70279B (es) * | 1979-09-12 | 1982-09-03 | Univ California | |
| DE3001928A1 (de) * | 1980-01-19 | 1981-08-06 | Hoechst Ag, 6000 Frankfurt | Genprodukt eines hoeheren organismus aus einem dieses gen enthaltenden mikroorganismus |
| US4338397A (en) * | 1980-04-11 | 1982-07-06 | President And Fellows Of Harvard College | Mature protein synthesis |
| GR76959B (es) * | 1981-01-02 | 1984-09-04 | Univ New York State Res Found |
-
1982
- 1982-06-15 ZA ZA824218A patent/ZA824218B/xx unknown
- 1982-06-18 PT PT75075A patent/PT75075B/pt unknown
- 1982-06-21 IL IL66102A patent/IL66102A0/xx unknown
- 1982-06-25 EP EP82303340A patent/EP0070632A3/en not_active Withdrawn
- 1982-06-25 JP JP57502369A patent/JPS58501227A/ja active Pending
- 1982-06-25 WO PCT/US1982/000858 patent/WO1983000164A1/en active Application Filing
- 1982-06-25 AU AU87623/82A patent/AU556980B2/en not_active Ceased
- 1982-06-28 ES ES513522A patent/ES513522A0/es active Granted
- 1982-06-29 CA CA000406245A patent/CA1201074A/en not_active Expired
-
1983
- 1983-02-24 DK DK84583A patent/DK84583A/da not_active Application Discontinuation
- 1983-02-28 NO NO830682A patent/NO830682L/no unknown
-
1984
- 1984-06-27 US US06/625,176 patent/USH245H/en not_active Abandoned
Also Published As
| Publication number | Publication date |
|---|---|
| ES8304430A1 (es) | 1983-03-01 |
| DK84583D0 (da) | 1983-02-24 |
| PT75075B (en) | 1983-12-28 |
| DK84583A (da) | 1983-02-24 |
| EP0070632A3 (en) | 1983-06-29 |
| USH245H (en) | 1987-04-07 |
| PT75075A (en) | 1982-07-01 |
| CA1201074A (en) | 1986-02-25 |
| WO1983000164A1 (en) | 1983-01-20 |
| ES513522A0 (es) | 1983-03-01 |
| AU8762382A (en) | 1983-02-02 |
| IL66102A0 (en) | 1982-09-30 |
| ZA824218B (en) | 1983-04-27 |
| JPS58501227A (ja) | 1983-07-28 |
| AU556980B2 (en) | 1986-11-27 |
| EP0070632A2 (en) | 1983-01-26 |
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