DD147369A5 - Verfahren zur synthese eines eukaryontischen proteins durch mikroorganismen - Google Patents

Verfahren zur synthese eines eukaryontischen proteins durch mikroorganismen Download PDF

Info

Publication number: DD147369A5
Authority: DD; German Democratic Republic
Prior art keywords: gene; fragment; nucleotide sequence; eukaryotic; item
Prior art date: 1978-08-11

Application number

DD79214948A

Other languages

German (de)

English (en)

Inventor

William J Rutter

Howard M Goodman

John D Baxter

Original Assignee

Univ California

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.)

1978-08-11

Filing date

1979-08-13

Publication date

1981-04-01

Family has litigation

First worldwide family litigation filed litigation Critical https://patents.darts-ip.com/?family=25463306&utm_source=google_patent&utm_medium=platform_link&utm_campaign=public_patent_search&patent=DD147369(A5) "Global patent litigation dataset” by Darts-ip is licensed under a Creative Commons Attribution 4.0 International License.

1979-08-13 Application filed by Univ California filed Critical Univ California

1981-04-01 Publication of DD147369A5 publication Critical patent/DD147369A5/de

Links

108090000623 proteins and genes Proteins 0.000 title claims abstract description 182
102000004169 proteins and genes Human genes 0.000 title claims abstract description 68
238000000034 method Methods 0.000 title claims abstract description 48
244000005700 microbiome Species 0.000 title claims abstract description 32
230000015572 biosynthetic process Effects 0.000 title claims description 24
238000003786 synthesis reaction Methods 0.000 title claims description 18
230000008569 process Effects 0.000 title claims description 8
239000012634 fragment Substances 0.000 claims abstract description 64
239000002773 nucleotide Substances 0.000 claims abstract description 42
125000003729 nucleotide group Chemical group 0.000 claims abstract description 42
238000012546 transfer Methods 0.000 claims abstract description 37
239000013598 vector Substances 0.000 claims abstract description 34
238000013518 transcription Methods 0.000 claims abstract description 11
230000035897 transcription Effects 0.000 claims abstract description 11
239000013612 plasmid Substances 0.000 claims description 73
230000014509 gene expression Effects 0.000 claims description 51
NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical group 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 claims description 39
108090001061 Insulin Proteins 0.000 claims description 29
108091008146 restriction endonucleases Proteins 0.000 claims description 28
241000588724 Escherichia coli Species 0.000 claims description 24
108010005774 beta-Galactosidase Proteins 0.000 claims description 24
239000000122 growth hormone Substances 0.000 claims description 23
102000004877 Insulin Human genes 0.000 claims description 21
238000003776 cleavage reaction Methods 0.000 claims description 20
229940125396 insulin Drugs 0.000 claims description 20
230000007017 scission Effects 0.000 claims description 20
102000005936 beta-Galactosidase Human genes 0.000 claims description 19
108010051696 Growth Hormone Proteins 0.000 claims description 13
230000000977 initiatory effect Effects 0.000 claims description 10
230000009466 transformation Effects 0.000 claims description 10
230000012010 growth Effects 0.000 claims description 8
238000013519 translation Methods 0.000 claims description 7
108091028043 Nucleic acid sequence Proteins 0.000 claims description 6
230000001580 bacterial effect Effects 0.000 claims description 6
108060002716 Exonuclease Proteins 0.000 claims description 3
102000013165 exonuclease Human genes 0.000 claims description 3
230000002103 transcriptional effect Effects 0.000 claims description 3
108010077805 Bacterial Proteins Proteins 0.000 claims 8
FGUUSXIOTUKUDN-IBGZPJMESA-N C1(=CC=CC=C1)N1C2=C(NC([C@H](C1)NC=1OC(=NN=1)C1=CC=CC=C1)=O)C=CC=C2 Chemical compound C1(=CC=CC=C1)N1C2=C(NC([C@H](C1)NC=1OC(=NN=1)C1=CC=CC=C1)=O)C=CC=C2 FGUUSXIOTUKUDN-IBGZPJMESA-N 0.000 claims 1
102100038803 Somatotropin Human genes 0.000 claims 1
238000010348 incorporation Methods 0.000 claims 1
230000002068 genetic effect Effects 0.000 abstract description 10
108020004414 DNA Proteins 0.000 abstract description 8
102000053602 DNA Human genes 0.000 abstract description 8
230000002194 synthesizing effect Effects 0.000 abstract description 3
230000010039 intracellular degradation Effects 0.000 abstract 1
235000018102 proteins Nutrition 0.000 description 60
210000004027 cell Anatomy 0.000 description 56
101000868151 Rattus norvegicus Somatotropin Proteins 0.000 description 34
102000037865 fusion proteins Human genes 0.000 description 28
108020001507 fusion proteins Proteins 0.000 description 28
150000001413 amino acids Chemical group 0.000 description 25
238000011282 treatment Methods 0.000 description 22
108010076181 Proinsulin Proteins 0.000 description 14
241000894006 Bacteria Species 0.000 description 13
102000004190 Enzymes Human genes 0.000 description 13
108090000790 Enzymes Proteins 0.000 description 13
239000004098 Tetracycline Substances 0.000 description 13
229940088598 enzyme Drugs 0.000 description 13
238000001502 gel electrophoresis Methods 0.000 description 13
229960002180 tetracycline Drugs 0.000 description 13
229930101283 tetracycline Natural products 0.000 description 13
235000019364 tetracycline Nutrition 0.000 description 13
150000003522 tetracyclines Chemical class 0.000 description 13
102000018997 Growth Hormone Human genes 0.000 description 12
235000001014 amino acid Nutrition 0.000 description 12
229940024606 amino acid Drugs 0.000 description 12
108090000204 Dipeptidase 1 Proteins 0.000 description 11
238000012360 testing method Methods 0.000 description 11
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 10
239000007983 Tris buffer Substances 0.000 description 10
LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 10
GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 9
238000007792 addition Methods 0.000 description 9
102000006635 beta-lactamase Human genes 0.000 description 9
238000002474 experimental method Methods 0.000 description 9
239000008101 lactose Substances 0.000 description 9
239000000047 product Substances 0.000 description 9
108020004705 Codon Proteins 0.000 description 8
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 8
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 8
239000000499 gel Substances 0.000 description 8
102000012410 DNA Ligases Human genes 0.000 description 7
108010061982 DNA Ligases Proteins 0.000 description 7
229960000723 ampicillin Drugs 0.000 description 7
238000009739 binding Methods 0.000 description 7
239000013613 expression plasmid Substances 0.000 description 7
229940088597 hormone Drugs 0.000 description 7
239000005556 hormone Substances 0.000 description 7
239000006166 lysate Substances 0.000 description 7
KDCGOANMDULRCW-UHFFFAOYSA-N 7H-purine Chemical compound N1=CNC2=NC=NC2=C1 KDCGOANMDULRCW-UHFFFAOYSA-N 0.000 description 6
108010000521 Human Growth Hormone Proteins 0.000 description 6
240000004808 Saccharomyces cerevisiae Species 0.000 description 6
230000027455 binding Effects 0.000 description 6
AIYUHDOJVYHVIT-UHFFFAOYSA-M caesium chloride Chemical compound [Cl-].[Cs+] AIYUHDOJVYHVIT-UHFFFAOYSA-M 0.000 description 6
230000006870 function Effects 0.000 description 6
YBYRMVIVWMBXKQ-UHFFFAOYSA-N phenylmethanesulfonyl fluoride Chemical compound FS(=O)(=O)CC1=CC=CC=C1 YBYRMVIVWMBXKQ-UHFFFAOYSA-N 0.000 description 6
239000000243 solution Substances 0.000 description 6
230000014616 translation Effects 0.000 description 6
241000282412 Homo Species 0.000 description 5
102000002265 Human Growth Hormone Human genes 0.000 description 5
239000000854 Human Growth Hormone Substances 0.000 description 5
125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 5
238000003018 immunoassay Methods 0.000 description 5
238000003780 insertion Methods 0.000 description 5
230000037431 insertion Effects 0.000 description 5
238000000746 purification Methods 0.000 description 5
241001465754 Metazoa Species 0.000 description 4
DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 4
230000009471 action Effects 0.000 description 4
238000004458 analytical method Methods 0.000 description 4
239000000427 antigen Substances 0.000 description 4
102000036639 antigens Human genes 0.000 description 4
108091007433 antigens Proteins 0.000 description 4
238000005516 engineering process Methods 0.000 description 4
239000002609 medium Substances 0.000 description 4
229920001184 polypeptide Polymers 0.000 description 4
108090000765 processed proteins & peptides Proteins 0.000 description 4
102000004196 processed proteins & peptides Human genes 0.000 description 4
230000035945 sensitivity Effects 0.000 description 4
239000011780 sodium chloride Substances 0.000 description 4
HRPVXLWXLXDGHG-UHFFFAOYSA-N Acrylamide Chemical compound NC(=O)C=C HRPVXLWXLXDGHG-UHFFFAOYSA-N 0.000 description 3
241000283690 Bos taurus Species 0.000 description 3
108010042407 Endonucleases Proteins 0.000 description 3
102000004533 Endonucleases Human genes 0.000 description 3
LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 3
DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 3
UYTPUPDQBNUYGX-UHFFFAOYSA-N Guanine Natural products O=C1NC(N)=NC2=C1N=CN2 UYTPUPDQBNUYGX-UHFFFAOYSA-N 0.000 description 3
101000976075 Homo sapiens Insulin Proteins 0.000 description 3
101710163270 Nuclease Proteins 0.000 description 3
108091034117 Oligonucleotide Proteins 0.000 description 3
VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 3
RWQNBRDOKXIBIV-UHFFFAOYSA-N Thymine Natural products CC1=CNC(=O)NC1=O RWQNBRDOKXIBIV-UHFFFAOYSA-N 0.000 description 3
230000002942 anti-growth Effects 0.000 description 3
238000005119 centrifugation Methods 0.000 description 3
238000006243 chemical reaction Methods 0.000 description 3
ATDGTVJJHBUTRL-UHFFFAOYSA-N cyanogen bromide Chemical compound BrC#N ATDGTVJJHBUTRL-UHFFFAOYSA-N 0.000 description 3
230000029087 digestion Effects 0.000 description 3
239000003814 drug Substances 0.000 description 3
230000000694 effects Effects 0.000 description 3
230000007613 environmental effect Effects 0.000 description 3
239000001963 growth medium Substances 0.000 description 3
230000003834 intracellular effect Effects 0.000 description 3
238000002955 isolation Methods 0.000 description 3
238000004519 manufacturing process Methods 0.000 description 3
108020004999 messenger RNA Proteins 0.000 description 3
239000000203 mixture Substances 0.000 description 3
229920002401 polyacrylamide Polymers 0.000 description 3
238000002360 preparation method Methods 0.000 description 3
XJMOSONTPMZWPB-UHFFFAOYSA-M propidium iodide Chemical compound [I-].[I-].C12=CC(N)=CC=C2C2=CC=C(N)C=C2[N+](CCC[N+](C)(CC)CC)=C1C1=CC=CC=C1 XJMOSONTPMZWPB-UHFFFAOYSA-M 0.000 description 3
238000010187 selection method Methods 0.000 description 3
239000001632 sodium acetate Substances 0.000 description 3
235000017281 sodium acetate Nutrition 0.000 description 3
229940083575 sodium dodecyl sulfate Drugs 0.000 description 3
235000019333 sodium laurylsulphate Nutrition 0.000 description 3
239000000126 substance Substances 0.000 description 3
108091032973 (ribonucleotides)n+m Proteins 0.000 description 2
LTFMZDNNPPEQNG-KVQBGUIXSA-N 2'-deoxyguanosine 5'-monophosphate Chemical compound C1=2NC(N)=NC(=O)C=2N=CN1[C@H]1C[C@H](O)[C@@H](COP(O)(O)=O)O1 LTFMZDNNPPEQNG-KVQBGUIXSA-N 0.000 description 2
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 2
229930024421 Adenine Natural products 0.000 description 2
GFFGJBXGBJISGV-UHFFFAOYSA-N Adenine Chemical compound NC1=NC=NC2=C1N=CN2 GFFGJBXGBJISGV-UHFFFAOYSA-N 0.000 description 2
102000002260 Alkaline Phosphatase Human genes 0.000 description 2
108020004774 Alkaline Phosphatase Proteins 0.000 description 2
108010072454 CTGCAG-specific type II deoxyribonucleases Proteins 0.000 description 2
HEDRZPFGACZZDS-UHFFFAOYSA-N Chloroform Chemical compound ClC(Cl)Cl HEDRZPFGACZZDS-UHFFFAOYSA-N 0.000 description 2
108091026890 Coding region Proteins 0.000 description 2
238000012270 DNA recombination Methods 0.000 description 2
102000016928 DNA-directed DNA polymerase Human genes 0.000 description 2
108010014303 DNA-directed DNA polymerase Proteins 0.000 description 2
IAZDPXIOMUYVGZ-UHFFFAOYSA-N Dimethylsulphoxide Chemical compound CS(C)=O IAZDPXIOMUYVGZ-UHFFFAOYSA-N 0.000 description 2
DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 2
CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 2
ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 2
COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 2
OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 2
KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 2
102000003960 Ligases Human genes 0.000 description 2
108090000364 Ligases Proteins 0.000 description 2
KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 2
XYFCBTPGUUZFHI-UHFFFAOYSA-N Phosphine Chemical compound P XYFCBTPGUUZFHI-UHFFFAOYSA-N 0.000 description 2
108020004511 Recombinant DNA Proteins 0.000 description 2
239000007984 Tris EDTA buffer Substances 0.000 description 2
KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 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
239000002253 acid Substances 0.000 description 2
229960000643 adenine Drugs 0.000 description 2
238000000246 agarose gel electrophoresis Methods 0.000 description 2
BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 2
229910052921 ammonium sulfate Inorganic materials 0.000 description 2
235000011130 ammonium sulphate Nutrition 0.000 description 2
230000005540 biological transmission Effects 0.000 description 2
210000004899 c-terminal region Anatomy 0.000 description 2
238000006555 catalytic reaction Methods 0.000 description 2
230000032823 cell division Effects 0.000 description 2
239000003795 chemical substances by application Substances 0.000 description 2
230000002759 chromosomal effect Effects 0.000 description 2
239000002299 complementary DNA Substances 0.000 description 2
150000001875 compounds Chemical class 0.000 description 2
238000010276 construction Methods 0.000 description 2
230000000875 corresponding effect Effects 0.000 description 2
238000012258 culturing Methods 0.000 description 2
OPTASPLRGRRNAP-UHFFFAOYSA-N cytosine Chemical compound NC=1C=CNC(=O)N=1 OPTASPLRGRRNAP-UHFFFAOYSA-N 0.000 description 2
229940104302 cytosine Drugs 0.000 description 2
238000011161 development Methods 0.000 description 2
238000009826 distribution Methods 0.000 description 2
230000029142 excretion Effects 0.000 description 2
238000000855 fermentation Methods 0.000 description 2
230000004151 fermentation Effects 0.000 description 2
230000003301 hydrolyzing effect Effects 0.000 description 2
230000003053 immunization Effects 0.000 description 2
238000011534 incubation Methods 0.000 description 2
239000003999 initiator Substances 0.000 description 2
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 description 2
239000004026 insulin derivative Substances 0.000 description 2
238000005304 joining Methods 0.000 description 2
230000007246 mechanism Effects 0.000 description 2
238000012986 modification Methods 0.000 description 2
230000004048 modification Effects 0.000 description 2
230000036961 partial effect Effects 0.000 description 2
210000001322 periplasm Anatomy 0.000 description 2
108010081403 pre-beta-lactamase Proteins 0.000 description 2
239000002243 precursor Substances 0.000 description 2
230000001105 regulatory effect Effects 0.000 description 2
230000010076 replication Effects 0.000 description 2
238000011160 research Methods 0.000 description 2
241000894007 species Species 0.000 description 2
230000009870 specific binding Effects 0.000 description 2
239000007858 starting material Substances 0.000 description 2
229940113082 thymine Drugs 0.000 description 2
231100000331 toxic Toxicity 0.000 description 2
230000002588 toxic effect Effects 0.000 description 2
239000004474 valine Substances 0.000 description 2
108700026220 vif Genes Proteins 0.000 description 2
DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 2
ZKHQWZAMYRWXGA-UHFFFAOYSA-N Adenosine triphosphate Natural products C1=NC=2C(N)=NC=NC=2N1C1OC(COP(O)(=O)OP(O)(=O)OP(O)(O)=O)C(O)C1O ZKHQWZAMYRWXGA-UHFFFAOYSA-N 0.000 description 1
239000004475 Arginine Substances 0.000 description 1
DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
108020000946 Bacterial DNA Proteins 0.000 description 1
108020004256 Beta-lactamase Proteins 0.000 description 1
241000908115 Bolivar Species 0.000 description 1
208000010392 Bone Fractures Diseases 0.000 description 1
101001011741 Bos taurus Insulin Proteins 0.000 description 1
210000003771 C cell Anatomy 0.000 description 1
108010075254 C-Peptide Proteins 0.000 description 1
108010092265 CCWGG-specific type II deoxyribonucleases Proteins 0.000 description 1
OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 1
241000282693 Cercopithecidae Species 0.000 description 1
108020004635 Complementary DNA Proteins 0.000 description 1
230000007018 DNA scission Effects 0.000 description 1
108010005054 Deoxyribonuclease BamHI Proteins 0.000 description 1
208000012239 Developmental disease Diseases 0.000 description 1
206010013883 Dwarfism Diseases 0.000 description 1
241000206602 Eukaryota Species 0.000 description 1
108050001049 Extracellular proteins Proteins 0.000 description 1
208000034454 F12-related hereditary angioedema with normal C1Inh Diseases 0.000 description 1
206010017076 Fracture Diseases 0.000 description 1
230000005526 G1 to G0 transition Effects 0.000 description 1
102000002464 Galactosidases Human genes 0.000 description 1
108010093031 Galactosidases Proteins 0.000 description 1
208000012671 Gastrointestinal haemorrhages Diseases 0.000 description 1
WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 1
239000004471 Glycine Substances 0.000 description 1
206010020751 Hypersensitivity Diseases 0.000 description 1
206010062767 Hypophysitis Diseases 0.000 description 1
QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 1
AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 1
FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 1
QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 1
108091026898 Leader sequence (mRNA) Proteins 0.000 description 1
ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
239000004472 Lysine Substances 0.000 description 1
241000282560 Macaca mulatta Species 0.000 description 1
241000124008 Mammalia Species 0.000 description 1
208000030136 Marchiafava-Bignami Disease Diseases 0.000 description 1
208000029725 Metabolic bone disease Diseases 0.000 description 1
102000016943 Muramidase Human genes 0.000 description 1
108010014251 Muramidase Proteins 0.000 description 1
108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
108020004485 Nonsense Codon Proteins 0.000 description 1
108010058846 Ovalbumin Proteins 0.000 description 1
102000035195 Peptidases Human genes 0.000 description 1
108091005804 Peptidases Proteins 0.000 description 1
102000004160 Phosphoric Monoester Hydrolases Human genes 0.000 description 1
108090000608 Phosphoric Monoester Hydrolases Proteins 0.000 description 1
241000288906 Primates Species 0.000 description 1
ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
239000004365 Protease Substances 0.000 description 1
CZPWVGJYEJSRLH-UHFFFAOYSA-N Pyrimidine Chemical compound C1=CN=CN=C1 CZPWVGJYEJSRLH-UHFFFAOYSA-N 0.000 description 1
241000282941 Rangifer tarandus Species 0.000 description 1
108020001027 Ribosomal DNA Proteins 0.000 description 1
229920005654 Sephadex Polymers 0.000 description 1
239000012507 Sephadex™ Substances 0.000 description 1
229920002684 Sepharose Polymers 0.000 description 1
MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
241000191967 Staphylococcus aureus Species 0.000 description 1
229930006000 Sucrose Natural products 0.000 description 1
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 1
RZCIEJXAILMSQK-JXOAFFINSA-N TTP Chemical compound O=C1NC(=O)C(C)=CN1[C@H]1[C@H](O)[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 RZCIEJXAILMSQK-JXOAFFINSA-N 0.000 description 1
AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
239000004473 Threonine Substances 0.000 description 1
229920004890 Triton X-100 Polymers 0.000 description 1
239000013504 Triton X-100 Substances 0.000 description 1
QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 1
108091023045 Untranslated Region Proteins 0.000 description 1
ISAKRJDGNUQOIC-UHFFFAOYSA-N Uracil Natural products O=C1C=CNC(=O)N1 ISAKRJDGNUQOIC-UHFFFAOYSA-N 0.000 description 1
241000700605 Viruses Species 0.000 description 1
241000269370 Xenopus <genus> Species 0.000 description 1
241000269368 Xenopus laevis Species 0.000 description 1
VVBXXVAFSPEIJQ-CVIPOMFBSA-N [(2r)-3-[[(2r)-1-[[(2s,5r,8r,11r,12s,15s,18s,21s)-15-[3-(diaminomethylideneamino)propyl]-21-hydroxy-5-[(4-hydroxyphenyl)methyl]-4,11-dimethyl-2-(2-methylpropyl)-3,6,9,13,16,22-hexaoxo-8-propan-2-yl-10-oxa-1,4,7,14,17-pentazabicyclo[16.3.1]docosan-12-yl]am Chemical compound C([C@@H]1C(=O)N[C@@H](C(=O)O[C@H](C)[C@@H](C(N[C@@H](CCCN=C(N)N)C(=O)N[C@H]2CC[C@H](O)N(C2=O)[C@@H](CC(C)C)C(=O)N1C)=O)NC(=O)[C@H](NC(=O)[C@H](O)COS(O)(=O)=O)CC(C)C)C(C)C)C1=CC=C(O)C=C1 VVBXXVAFSPEIJQ-CVIPOMFBSA-N 0.000 description 1
CTCBPRXHVPZNHB-VQFZJOCSSA-N [[(2r,3s,4r,5r)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl] phosphono hydrogen phosphate;(2r,3r,4s,5r)-2-(6-aminopurin-9-yl)-5-(hydroxymethyl)oxolane-3,4-diol Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@@H]1O[C@H](CO)[C@@H](O)[C@H]1O.C1=NC=2C(N)=NC=NC=2N1[C@@H]1O[C@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)[C@@H](O)[C@H]1O CTCBPRXHVPZNHB-VQFZJOCSSA-N 0.000 description 1
238000010521 absorption reaction Methods 0.000 description 1
230000002411 adverse Effects 0.000 description 1
238000001042 affinity chromatography Methods 0.000 description 1
235000004279 alanine Nutrition 0.000 description 1
PNEYBMLMFCGWSK-UHFFFAOYSA-N aluminium oxide Inorganic materials [O-2].[O-2].[O-2].[Al+3].[Al+3] PNEYBMLMFCGWSK-UHFFFAOYSA-N 0.000 description 1
238000003975 animal breeding Methods 0.000 description 1
239000003242 anti bacterial agent Substances 0.000 description 1
229940088710 antibiotic agent Drugs 0.000 description 1
ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
235000009582 asparagine Nutrition 0.000 description 1
229960001230 asparagine Drugs 0.000 description 1
235000003704 aspartic acid Nutrition 0.000 description 1
238000003556 assay Methods 0.000 description 1
230000009286 beneficial effect Effects 0.000 description 1
230000008901 benefit Effects 0.000 description 1
OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 1
IXIBAKNTJSCKJM-BUBXBXGNSA-N bovine insulin 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)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)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(C)C)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 IXIBAKNTJSCKJM-BUBXBXGNSA-N 0.000 description 1
238000002815 broth microdilution Methods 0.000 description 1
239000000872 buffer Substances 0.000 description 1
238000010804 cDNA synthesis Methods 0.000 description 1
229910052799 carbon Inorganic materials 0.000 description 1
238000005341 cation exchange Methods 0.000 description 1
238000004113 cell culture Methods 0.000 description 1
210000000170 cell membrane Anatomy 0.000 description 1
210000002421 cell wall Anatomy 0.000 description 1
230000036755 cellular response Effects 0.000 description 1
210000003850 cellular structure Anatomy 0.000 description 1
239000007795 chemical reaction product Substances 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
238000004587 chromatography analysis Methods 0.000 description 1
210000000349 chromosome Anatomy 0.000 description 1
238000004140 cleaning Methods 0.000 description 1
230000000295 complement effect Effects 0.000 description 1
239000000356 contaminant Substances 0.000 description 1
230000002596 correlated effect Effects 0.000 description 1
235000018417 cysteine Nutrition 0.000 description 1
XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
210000000805 cytoplasm Anatomy 0.000 description 1
230000001086 cytosolic effect Effects 0.000 description 1
SUYVUBYJARFZHO-RRKCRQDMSA-N dATP Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@H]1C[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 SUYVUBYJARFZHO-RRKCRQDMSA-N 0.000 description 1
SUYVUBYJARFZHO-UHFFFAOYSA-N dATP Natural products C1=NC=2C(N)=NC=NC=2N1C1CC(O)C(COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 SUYVUBYJARFZHO-UHFFFAOYSA-N 0.000 description 1
HAAZLUGHYHWQIW-KVQBGUIXSA-N dGTP Chemical compound C1=NC=2C(=O)NC(N)=NC=2N1[C@H]1C[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 HAAZLUGHYHWQIW-KVQBGUIXSA-N 0.000 description 1
230000003247 decreasing effect Effects 0.000 description 1
230000007812 deficiency Effects 0.000 description 1
238000012217 deletion Methods 0.000 description 1
230000037430 deletion Effects 0.000 description 1
LTFMZDNNPPEQNG-UHFFFAOYSA-N deoxyguanylic acid Natural products C1=2NC(N)=NC(=O)C=2N=CN1C1CC(O)C(COP(O)(O)=O)O1 LTFMZDNNPPEQNG-UHFFFAOYSA-N 0.000 description 1
230000001419 dependent effect Effects 0.000 description 1
206010012601 diabetes mellitus Diseases 0.000 description 1
LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 1
208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
208000035475 disorder Diseases 0.000 description 1
238000004090 dissolution Methods 0.000 description 1
238000001962 electrophoresis Methods 0.000 description 1
ZMMJGEGLRURXTF-UHFFFAOYSA-N ethidium bromide Chemical compound [Br-].C12=CC(N)=CC=C2C2=CC=C(N)C=C2[N+](CC)=C1C1=CC=CC=C1 ZMMJGEGLRURXTF-UHFFFAOYSA-N 0.000 description 1
229960005542 ethidium bromide Drugs 0.000 description 1
239000000284 extract Substances 0.000 description 1
238000011049 filling Methods 0.000 description 1
230000004927 fusion Effects 0.000 description 1
208000030304 gastrointestinal bleeding Diseases 0.000 description 1
238000007429 general method Methods 0.000 description 1
235000013922 glutamic acid Nutrition 0.000 description 1
239000004220 glutamic acid Substances 0.000 description 1
ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
208000037824 growth disorder Diseases 0.000 description 1
230000035876 healing Effects 0.000 description 1
208000016861 hereditary angioedema type 3 Diseases 0.000 description 1
HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
230000007062 hydrolysis Effects 0.000 description 1
238000006460 hydrolysis reaction Methods 0.000 description 1
238000002649 immunization Methods 0.000 description 1
230000000984 immunochemical effect Effects 0.000 description 1
239000012535 impurity Substances 0.000 description 1
238000011081 inoculation Methods 0.000 description 1
230000010189 intracellular transport Effects 0.000 description 1
150000002500 ions Chemical class 0.000 description 1
229960000310 isoleucine Drugs 0.000 description 1
AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 1
150000002597 lactoses Chemical class 0.000 description 1
238000007169 ligase reaction Methods 0.000 description 1
239000007788 liquid Substances 0.000 description 1
239000004325 lysozyme Substances 0.000 description 1
229960000274 lysozyme Drugs 0.000 description 1
235000010335 lysozyme Nutrition 0.000 description 1
239000000463 material Substances 0.000 description 1
230000008774 maternal effect Effects 0.000 description 1
230000002503 metabolic effect Effects 0.000 description 1
229930182817 methionine Natural products 0.000 description 1
230000002906 microbiologic effect Effects 0.000 description 1
238000002156 mixing Methods 0.000 description 1
239000004570 mortar (masonry) Substances 0.000 description 1
230000005257 nucleotidylation Effects 0.000 description 1
230000003287 optical effect Effects 0.000 description 1
229940092253 ovalbumin Drugs 0.000 description 1
210000000496 pancreas Anatomy 0.000 description 1
230000003094 perturbing effect Effects 0.000 description 1
COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 1
239000002953 phosphate buffered saline Substances 0.000 description 1
125000002467 phosphate group Chemical group [H]OP(=O)(O[H])O[*] 0.000 description 1
150000004713 phosphodiesters Chemical class 0.000 description 1
229910000073 phosphorus hydride Inorganic materials 0.000 description 1
208000003068 pituitary dwarfism Diseases 0.000 description 1
230000001817 pituitary effect Effects 0.000 description 1
210000003635 pituitary gland Anatomy 0.000 description 1
210000002381 plasma Anatomy 0.000 description 1
239000002985 plastic film Substances 0.000 description 1
229920006255 plastic film Polymers 0.000 description 1
238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
108091033319 polynucleotide Proteins 0.000 description 1
102000040430 polynucleotide Human genes 0.000 description 1
239000002157 polynucleotide Substances 0.000 description 1
239000002244 precipitate Substances 0.000 description 1
238000001556 precipitation Methods 0.000 description 1
108010066381 preproinsulin Proteins 0.000 description 1
125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
238000001243 protein synthesis Methods 0.000 description 1
230000002285 radioactive effect Effects 0.000 description 1
239000000700 radioactive tracer Substances 0.000 description 1
238000003127 radioimmunoassay Methods 0.000 description 1
230000000384 rearing effect Effects 0.000 description 1
238000005215 recombination Methods 0.000 description 1
230000006798 recombination Effects 0.000 description 1
238000011084 recovery Methods 0.000 description 1
230000003362 replicative effect Effects 0.000 description 1
230000004044 response Effects 0.000 description 1
230000000717 retained effect Effects 0.000 description 1
230000002441 reversible effect Effects 0.000 description 1
210000003705 ribosome Anatomy 0.000 description 1
239000007320 rich medium Substances 0.000 description 1
230000005070 ripening Effects 0.000 description 1
229920002477 rna polymer Polymers 0.000 description 1
238000000926 separation method Methods 0.000 description 1
210000002966 serum Anatomy 0.000 description 1
238000003307 slaughter Methods 0.000 description 1
238000000527 sonication Methods 0.000 description 1
230000006641 stabilisation Effects 0.000 description 1
238000011105 stabilization Methods 0.000 description 1
238000010561 standard procedure Methods 0.000 description 1
239000000758 substrate Substances 0.000 description 1
239000005720 sucrose Substances 0.000 description 1
239000006228 supernatant Substances 0.000 description 1
238000002560 therapeutic procedure Methods 0.000 description 1
108010042582 tosylarginine methyl ester hydrolase Proteins 0.000 description 1
230000007704 transition Effects 0.000 description 1
238000000539 two dimensional gel electrophoresis 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
241001515965 unidentified phage Species 0.000 description 1
229940035893 uracil Drugs 0.000 description 1
238000005406 washing Methods 0.000 description 1
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
239000012130 whole-cell lysate Substances 0.000 description 1
230000029663 wound healing Effects 0.000 description 1
150000003952 β-lactams Chemical class 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
- C07K14/62—Insulins
- 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
- C07K14/61—Growth hormone [GH], i.e. somatotropin
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/70—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)
Chemical & Material Sciences (AREA)
Organic Chemistry (AREA)
Life Sciences & Earth Sciences (AREA)
Endocrinology (AREA)
Zoology (AREA)
Medicinal Chemistry (AREA)
Toxicology (AREA)
Biochemistry (AREA)
Biophysics (AREA)
General Health & Medical Sciences (AREA)
Genetics & Genomics (AREA)
Gastroenterology & Hepatology (AREA)
Molecular Biology (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Diabetes (AREA)
Micro-Organisms Or Cultivation Processes Thereof (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Peptides Or Proteins (AREA)

DD79214948A 1978-08-11 1979-08-13 Verfahren zur synthese eines eukaryontischen proteins durch mikroorganismen DD147369A5 (de)

Applications Claiming Priority (1)

Application Number	Priority Date	Filing Date	Title
US93303578A	1978-08-11	1978-08-11

Publications (1)

Publication Number	Publication Date
DD147369A5 true DD147369A5 (de)	1981-04-01

Family

ID=25463306

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
DD79214948A DD147369A5 (de)	1978-08-11	1979-08-13	Verfahren zur synthese eines eukaryontischen proteins durch mikroorganismen

Country Status (20)

Country	Link
EP (1)	EP0012494B1 (nl)
JP (1)	JPS5545395A (nl)
AT (1)	AT373917B (nl)
AU (1)	AU533035B2 (nl)
CS (1)	CS219257B2 (nl)
DD (1)	DD147369A5 (nl)
DE (1)	DE2966390D1 (nl)
DK (1)	DK334979A (nl)
FI (1)	FI792481A (nl)
GB (1)	GB2031434B (nl)
GR (1)	GR71912B (nl)
IE (1)	IE48385B1 (nl)
IL (1)	IL58016A (nl)
IT (1)	IT7925087A0 (nl)
NZ (1)	NZ191278A (nl)
PH (1)	PH22855A (nl)
PL (1)	PL217721A1 (nl)
PT (1)	PT70051A (nl)
YU (1)	YU195679A (nl)
ZA (1)	ZA794172B (nl)

Families Citing this family (40)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
DE2862495D1 (en) *	1977-11-08	1989-05-24	Genentech Inc	Plasmid for transforming bacterial host to render it capable of polypeptide expression
BR7807290A (pt) *	1977-11-08	1979-06-12	Genentech Inc	Plasmideo,processo para producao de um polipeptido especifico veiculo clonal,cultura bacteriana transformante,processo para produzir uma substancia imunogenica processo para preparar um gene estrutural,e polidesoxirribonucleotido de faixa dupla
US4565785A (en) *	1978-06-08	1986-01-21	The President And Fellows Of Harvard College	Recombinant DNA molecule
US6270955B1 (en)	1978-12-22	2001-08-07	Biogen, Inc.	Pharmaceutical compositions and methods for producing antibodies to hepatitis b virus and kits and methods for detecting antibodies to hepatitis b virus
ZA802992B (en) *	1979-06-01	1981-10-28	Univ California	Human pre-growth hormone
US4342832A (en) *	1979-07-05	1982-08-03	Genentech, Inc.	Method of constructing a replicable cloning vehicle having quasi-synthetic genes
GR70279B (nl) *	1979-09-12	1982-09-03	Univ California
US6835557B1 (en)	1980-01-08	2004-12-28	Biogen, Inc.	DNA sequences, recombinant DNA molecules and processes for producing human interferon-like polypeptides
US4530901A (en) *	1980-01-08	1985-07-23	Biogen N.V.	Recombinant DNA molecules and their use in producing human interferon-like polypeptides
DE3001928A1 (de) *	1980-01-19	1981-08-06	Hoechst Ag, 6000 Frankfurt	Genprodukt eines hoeheren organismus aus einem dieses gen enthaltenden mikroorganismus
US4443539A (en) *	1980-02-05	1984-04-17	The Upjohn Company	Process for preparing bovine growth hormone
AU545912B2 (en) *	1980-03-10	1985-08-08	Cetus Corporation	Cloned heterologous jive products in bacillies
ES500397A0 (es) *	1980-03-17	1982-06-01	Harvard College	Un metodo de determinar la cantidad de un polipeptido enca- riotico o procariotico producido por un microorganismo
IL59690A (en)	1980-03-24	1983-11-30	Yeda Res & Dev	Production of bovine growth hormone by microorganisms and modified microorganisms adapted to produce it
IN156128B (nl)	1980-04-03	1985-05-18	Biogen Nv
US4338397A (en) *	1980-04-11	1982-07-06	President And Fellows Of Harvard College	Mature protein synthesis
IE52755B1 (en) *	1980-08-26	1988-02-17	Univ California	Bovine pre-growth and growth hormone
US6692941B1 (en)	1980-08-26	2004-02-17	The Regents Of The University Of California	Bovine growth hormone
US4874702A (en) *	1980-09-08	1989-10-17	Biogen, Inc.	Vectors and methods for making such vectors and for expressive cloned genes
NZ199391A (en) *	1981-01-02	1985-12-13	Genentech Inc	Chimeric polypeptides comprising a proinsulin sequence,and preparation by recombinant dna technique;production of human insulin
JPS57181098A (en) *	1981-04-30	1982-11-08	Japan Found Cancer	Novel recombinant dna
JPS58996A (ja) *	1981-06-01	1983-01-06	ザ・ボ−ド・オブ・トラステイ−ズ・ミシガンステ−トユニバ−シテイ−	細菌中での牛成長ホルモン遺伝子のクロ−ン化
JPS58134998A (ja) *	1982-02-04	1983-08-11	Wakunaga Yakuhin Kk	２７−デスアミドセクレチンの製造法
JPS57200343A (en) *	1981-06-02	1982-12-08	Wakunaga Yakuhin Kk	27-desamidosecretin and its preparation
ZA824218B (en) *	1981-06-29	1983-04-27	Cetus Corp	Plasmid for producing human insulin
US5254463A (en) *	1981-09-18	1993-10-19	Genentech, Inc.	Method for expression of bovine growth hormone
JPS5863395A (ja) *	1981-10-13	1983-04-15	Suntory Ltd	アルフア・ネオ・エンドルフインの製造法
US4460689A (en) *	1982-04-15	1984-07-17	Merck & Co., Inc.	DNA Cloning vector TG1, derivatives, and processes of making
US4508826A (en) *	1982-04-15	1985-04-02	Merck & Co., Inc.	Bacteriophage DNA cloning vector TG1 and microorganisms containing TG1
EP0103395A3 (en) *	1982-08-17	1985-05-22	Biogen N.V.	Dna sequences, recombinant dna molecules and processes for producing bovine growth hormone-like polypeptides in high yield
WO1984001150A1 (en) *	1982-09-16	1984-03-29	Amgen	Avian growth hormones
SE8300693L (sv) *	1983-02-09	1984-08-10	Sven Lofdahl	Sett att framstella och isolera proteiner och polypeptider samt en hybridvektor for detta
US4703009A (en) *	1983-03-08	1987-10-27	Merck & Co., Inc.	RDNA cloning vector pVE1, deletion and hybrid mutants and recombinant derivatives thereof products and processes
PH23920A (en) *	1983-12-20	1990-01-23	Cetus Corp	Glucoamylase cdna
EP0148311B1 (en) *	1983-12-26	1988-07-20	Asahi Kasei Kogyo Kabushiki Kaisha	A novel physiologically active polypeptide
US5489529A (en) *	1984-07-19	1996-02-06	De Boer; Herman A.	DNA for expression of bovine growth hormone
DK594084A (da) *	1984-12-12	1986-06-13	Novo Industri As	Fremgangsmaade til stabilisering af extra-chromosomale elementer i bakterier under dyrkning
JPH01144992A (ja) *	1987-11-30	1989-06-07	Agency Of Ind Science & Technol	融合タンパク質の作成方法
FR2687410A1 (fr) *	1992-02-14	1993-08-20	Pasteur Institut	Beta-lactamase recombinante, utilisable en tant que molecule porteuse pour la preparation de compositions immunogenes.
JPH05332763A (ja) *	1992-06-02	1993-12-14	Railway Technical Res Inst	携帯型電機子ブラシ寸法測定装置

Family Cites Families (8)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
GB1521032A (en) *	1974-08-08	1978-08-09	Ici Ltd	Biological treatment
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
US4190495A (en) *	1976-09-27	1980-02-26	Research Corporation	Modified microorganisms and method of preparing and using same
CA1081510A (en) *	1977-03-08	1980-07-15	James M. Lapeyre	Controlled reflection readout for displays
DE2712615A1 (de) *	1977-03-18	1978-09-21	Max Planck Gesellschaft	Verfahren zur herstellung von filamentoesen phagen als vektor fuer synthetische rekombinate
NZ187300A (en) *	1977-05-27	1982-08-17	Univ California	Dna transfer vector and micro-organism modified to contain a nucleotide sequence equivalent to the gene of a higher organism
CH656640A5 (de) *	1977-11-08	1986-07-15	Genentech Inc	Verfahren zur herstellung eines polypeptids.
DE2862495D1 (en) *	1977-11-08	1989-05-24	Genentech Inc	Plasmid for transforming bacterial host to render it capable of polypeptide expression

1979
- 1979-08-09 GR GR59805A patent/GR71912B/el unknown
- 1979-08-09 IE IE1533/79A patent/IE48385B1/en unknown
- 1979-08-09 FI FI792481A patent/FI792481A/fi not_active Application Discontinuation
- 1979-08-10 CS CS795492A patent/CS219257B2/cs unknown
- 1979-08-10 DK DK334979A patent/DK334979A/da not_active Application Discontinuation
- 1979-08-10 YU YU01956/79A patent/YU195679A/xx unknown
- 1979-08-10 ZA ZA00794172A patent/ZA794172B/xx unknown
- 1979-08-10 JP JP10214579A patent/JPS5545395A/ja active Pending
- 1979-08-10 IL IL58016A patent/IL58016A/xx unknown
- 1979-08-10 PT PT70051A patent/PT70051A/pt unknown
- 1979-08-10 PH PH22887A patent/PH22855A/en unknown
- 1979-08-10 NZ NZ191278A patent/NZ191278A/xx unknown
- 1979-08-11 PL PL21772179A patent/PL217721A1/xx unknown
- 1979-08-13 AT AT0550579A patent/AT373917B/de not_active IP Right Cessation
- 1979-08-13 IT IT7925087A patent/IT7925087A0/it unknown
- 1979-08-13 GB GB7928156A patent/GB2031434B/en not_active Expired
- 1979-08-13 AU AU49843/79A patent/AU533035B2/en not_active Ceased
- 1979-08-13 DE DE7979301630T patent/DE2966390D1/de not_active Expired
- 1979-08-13 EP EP79301630A patent/EP0012494B1/en not_active Expired
- 1979-08-13 DD DD79214948A patent/DD147369A5/de unknown

Also Published As

Publication number	Publication date
PL217721A1 (nl)	1980-07-01
FI792481A (fi)	1980-02-12
DK334979A (da)	1980-02-12
GR71912B (nl)	1983-08-16
GB2031434B (en)	1983-03-02
AU533035B2 (en)	1983-10-27
IL58016A0 (en)	1979-12-30
GB2031434A (en)	1980-04-23
IL58016A (en)	1983-10-31
ZA794172B (en)	1980-12-31
IE48385B1 (en)	1984-12-26
ATA550579A (de)	1983-07-15
CS219257B2 (en)	1983-03-25
PH22855A (en)	1989-01-19
AT373917B (de)	1984-03-12
DE2966390D1 (en)	1983-12-15
NZ191278A (en)	1982-11-23
IT7925087A0 (it)	1979-08-13
EP0012494A1 (en)	1980-06-25
PT70051A (en)	1979-09-01
YU195679A (en)	1984-02-29
EP0012494B1 (en)	1983-11-09
AU4984379A (en)	1980-04-24
JPS5545395A (en)	1980-03-31

Publication	Publication Date	Title
DD147369A5 (de)	1981-04-01	Verfahren zur synthese eines eukaryontischen proteins durch mikroorganismen
DE3072205T2 (de)	1993-08-05	Dns-transfer-vektor, damit transformierter wirt, impfstoff und ihre herstellung.
DE69233008T2 (de)	2004-01-22	Fusionierung von Peptiden und Proteinen mit Thioredoxin und thioredoxin-ähnlichen Molekülen
DE3587558T2 (de)	1994-03-31	Rekombinante DNS-Vektoren fähig zur Apoaequorinexpression, Apoaequorinpeptide und deren Herstellung und diese Vektoren enthaltende Mikroorganismen.
DE3050722C2 (nl)	1987-09-24
DE3486425T2 (de)	1996-10-17	Wachstumshormon-Analoga, pharmazeutische und veterinäre Zusammensetzungen, die diese enthalten, sowie Methoden für ihre Herstellung
DE3880739T2 (de)	1993-08-19	Expression von menschlichem proapolipoprotein a-1.
DE69228705T2 (de)	1999-08-19	Methode zur rückfaltung von igf-i in eine aktive konformation
DE3020528C2 (nl)	1990-05-03
DD204711A5 (de)	1983-12-07	Verfahren zur herstellung eines dns-uebertragungsvektors
DE2858357C2 (nl)	1990-03-15
DE3650553T2 (de)	1997-02-27	Verfahren zur Herstellung biologisch aktiver Rinder- und Schweine-Wachstumshormone und Mischung mit biologisch aktivem Schweine-Wachstumshormon
DD202045A5 (de)	1983-08-24	Verfahren zum klonieren einer deoxynucleotidsequenz
DD203071A5 (de)	1983-10-12	Verfahren zur herstellung von rekombinant-dna-molekuele
EP0023882A2 (de)	1981-02-11	Plasmidvektoren, Plasmide mit Genen für alkalische Phosphatasen und Bakterien, die letztere enthalten, ihre Herstellung und Verwendung
DE3523634A1 (de)	1986-01-09	Ss-urogastron-gen, rekombinant-plasmide, transformanten, deren herstellung und herstellung von ss-urogastron
DD201693A5 (de)	1983-08-03	Verfahren zur synthetisierung von menschlichem proinsulin
DE3751081T2 (de)	1995-10-19	[Leu 13] Motilin, dessen kodierende DNS-Moleküle und Verfahren zu dessen Herstellung.
DE3485923T2 (de)	1993-03-04	Dna-gen, verfahren zu seiner herstellung und dieses gen enthaltendes plasmid.
DE69033772T2 (de)	2002-06-20	Verbesserte plasmidvektoren für zelluläre schleimpilze der gattung dictyostelium
DE69930118T2 (de)	2006-11-02	Verfahren zur herstellung von proteinen in transformierten hefezellen
JPS59501852A (ja)	1984-11-08	鳥類の成長ホルモン
AT389890B (de)	1990-02-12	Verfahren zur herstellung von humaninsulin
AT389891B (de)	1990-02-12	Verfahren zur herstellung von menschlichem proinsulin
AT386607B (de)	1988-09-26	Verfahren zum herstellen eines dns-transfer-vektors