NO830682L - Rekombinant plasmid for fremstilling av humaninsulin - Google Patents

Rekombinant plasmid for fremstilling av humaninsulin

Info

Publication number: NO830682L
Authority: NO; Norway
Prior art keywords: preproinsulin; human; human proinsulin; host; proinsulin
Prior art date: 1981-06-29

Application number

NO830682A

Other languages

English (en)

Norwegian (no)

Inventor

Chander Prakash

Original Assignee

Cetus Corp

Priority date (The priority date 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 date listed.)

1981-06-29

Filing date

1983-02-28

Publication date

1983-02-28

1983-02-28 Application filed by Cetus Corp filed Critical Cetus Corp

1983-02-28 Publication of NO830682L publication Critical patent/NO830682L/no

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)
Organic Chemistry (AREA)
Engineering & Computer Science (AREA)
Zoology (AREA)
Molecular Biology (AREA)
Biomedical Technology (AREA)
General Engineering & Computer Science (AREA)
General Health & Medical Sciences (AREA)
Biophysics (AREA)
Biochemistry (AREA)
Biotechnology (AREA)
Bioinformatics & Cheminformatics (AREA)
Wood Science & Technology (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Medicinal Chemistry (AREA)
Physics & Mathematics (AREA)
Gastroenterology & Hepatology (AREA)
Toxicology (AREA)
Plant Pathology (AREA)
Endocrinology (AREA)
Microbiology (AREA)
Diabetes (AREA)
Peptides Or Proteins (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)
Micro-Organisms Or Cultivation Processes Thereof (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)

NO830682A 1981-06-29 1983-02-28 Rekombinant plasmid for fremstilling av humaninsulin NO830682L (no)

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 (da)
EP (1)	EP0070632A3 (da)
JP (1)	JPS58501227A (da)
AU (1)	AU556980B2 (da)
CA (1)	CA1201074A (da)
DK (1)	DK84583A (da)
ES (1)	ES513522A0 (da)
IL (1)	IL66102A0 (da)
NO (1)	NO830682L (da)
PT (1)	PT75075B (da)
WO (1)	WO1983000164A1 (da)
ZA (1)	ZA824218B (da)

Families Citing this family (11)

* Cited by examiner, † Cited by third party
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
DE3752347T2 (de) *	1986-05-20	2002-09-26	The General Hospital Corp., Boston	Verfahren zur pharmakokinetischen Studie der Insulin-Expression mit nicht-menschlichem Transgen-Säugetier
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 (9)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
JPS5210872B2 (da) *	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
IE48385B1 (en) *	1978-08-11	1984-12-26	Univ California	Synthesis of a eucaryotic protein by a microorganism
GR70279B (da) *	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
EP0036258A3 (en)	1980-03-14	1982-02-10	Cetus Corporation	Process for producing aspartame
US4338397A (en) *	1980-04-11	1982-07-06	President And Fellows Of Harvard College	Mature protein synthesis
GR76959B (da) *	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 WO PCT/US1982/000858 patent/WO1983000164A1/en not_active Ceased
- 1982-06-25 AU AU87623/82A patent/AU556980B2/en not_active Ceased
- 1982-06-25 EP EP82303340A patent/EP0070632A3/en not_active Withdrawn
- 1982-06-25 JP JP57502369A patent/JPS58501227A/ja active Pending
- 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
USH245H (en)	1987-04-07
PT75075A (en)	1982-07-01
DK84583D0 (da)	1983-02-24
EP0070632A3 (en)	1983-06-29
ZA824218B (en)	1983-04-27
DK84583A (da)	1983-02-24
PT75075B (en)	1983-12-28
IL66102A0 (en)	1982-09-30
JPS58501227A (ja)	1983-07-28
WO1983000164A1 (en)	1983-01-20
CA1201074A (en)	1986-02-25
AU556980B2 (en)	1986-11-27
AU8762382A (en)	1983-02-02
EP0070632A2 (en)	1983-01-26
ES8304430A1 (es)	1983-03-01
ES513522A0 (es)	1983-03-01

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Hoppe et al.	1989	Preparation of biologically active platelet-derived growth factor type BB from a fusion protein expressed in Escherichia
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Seeburg et al.	1978	Synthesis of growth hormone by bacteria
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NO830682L (no)	1983-02-28	Rekombinant plasmid for fremstilling av humaninsulin
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WO1992002550A1 (en)	1992-02-20	Expression of recombinant polypeptides with improved purification
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US6001604A (en)	1999-12-14	Refolding of proinsulins without addition of reducing agents
Roepe et al.	1989	A five-residue sequence near the carboxyl terminus of the polytopic membrane protein lac permease is required for stability within the membrane.
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JPH03228682A (ja)	1991-10-09	Ｅ．コリでの非融合タンパク質の調製方法
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Upton et al.	1992	Production and characterization of recombinant chicken insulin-like growth factor-I from Escherichia coli
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JPH0779701B2 (ja)	1995-08-30	成長ホルモン放出因子を含むハイブリドポリペプチドをコ−ドする遺伝子
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