LU82757A1 - Genes de la proinsuline humaine et de pre-proinsuline humaine,leur procede de preparation et leurs applications - Google Patents
Genes de la proinsuline humaine et de pre-proinsuline humaine,leur procede de preparation et leurs applications Download PDFInfo
- Publication number
- LU82757A1 LU82757A1 LU82757A LU82757A LU82757A1 LU 82757 A1 LU82757 A1 LU 82757A1 LU 82757 A LU82757 A LU 82757A LU 82757 A LU82757 A LU 82757A LU 82757 A1 LU82757 A1 LU 82757A1
- Authority
- LU
- Luxembourg
- Prior art keywords
- sequence
- proinsulin
- human
- coding
- radical
- Prior art date
Links
- 108090000623 proteins and genes Proteins 0.000 title claims description 137
- 108010076181 Proinsulin Proteins 0.000 title claims description 113
- 108010066381 preproinsulin Proteins 0.000 title claims description 40
- 238000002360 preparation method Methods 0.000 title claims description 15
- 108020004414 DNA Proteins 0.000 claims description 74
- 238000000034 method Methods 0.000 claims description 74
- 102000004169 proteins and genes Human genes 0.000 claims description 67
- 102000053602 DNA Human genes 0.000 claims description 66
- 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 claims description 60
- 238000012546 transfer Methods 0.000 claims description 59
- 239000013598 vector Substances 0.000 claims description 56
- 150000001413 amino acids Chemical group 0.000 claims description 54
- 230000014509 gene expression Effects 0.000 claims description 44
- 239000012634 fragment Substances 0.000 claims description 33
- 239000013612 plasmid Substances 0.000 claims description 33
- 239000002773 nucleotide Substances 0.000 claims description 32
- 229940125396 insulin Drugs 0.000 claims description 31
- 125000003729 nucleotide group Chemical group 0.000 claims description 31
- 102000004877 Insulin Human genes 0.000 claims description 30
- 108090001061 Insulin Proteins 0.000 claims description 30
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 29
- 244000005700 microbiome Species 0.000 claims description 28
- 108091008146 restriction endonucleases Proteins 0.000 claims description 28
- 101000976075 Homo sapiens Insulin Proteins 0.000 claims description 23
- 230000029087 digestion Effects 0.000 claims description 23
- 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 claims description 22
- 230000015572 biosynthetic process Effects 0.000 claims description 20
- 230000008569 process Effects 0.000 claims description 19
- 102000004190 Enzymes Human genes 0.000 claims description 18
- 108090000790 Enzymes Proteins 0.000 claims description 18
- 230000002068 genetic effect Effects 0.000 claims description 18
- 230000007017 scission Effects 0.000 claims description 17
- 238000003786 synthesis reaction Methods 0.000 claims description 17
- 238000003776 cleavage reaction Methods 0.000 claims description 16
- 108010005636 polypeptide C Proteins 0.000 claims description 16
- 239000003795 chemical substances by application Substances 0.000 claims description 15
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 14
- 108010042407 Endonucleases Proteins 0.000 claims description 13
- 241000588724 Escherichia coli Species 0.000 claims description 11
- 235000011178 triphosphate Nutrition 0.000 claims description 11
- 239000001226 triphosphate Substances 0.000 claims description 11
- UNXRWKVEANCORM-UHFFFAOYSA-N triphosphoric acid Chemical compound OP(O)(=O)OP(O)(=O)OP(O)(O)=O UNXRWKVEANCORM-UHFFFAOYSA-N 0.000 claims description 10
- 239000002299 complementary DNA Substances 0.000 claims description 8
- 108020001507 fusion proteins Proteins 0.000 claims description 8
- 102000037865 fusion proteins Human genes 0.000 claims description 8
- 238000004519 manufacturing process Methods 0.000 claims description 8
- 238000006243 chemical reaction Methods 0.000 claims description 7
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 claims description 7
- 101710163270 Nuclease Proteins 0.000 claims description 6
- 230000007062 hydrolysis Effects 0.000 claims description 6
- 238000006460 hydrolysis reaction Methods 0.000 claims description 6
- 108010075254 C-Peptide Proteins 0.000 claims description 5
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 claims description 5
- 102000016928 DNA-directed DNA polymerase Human genes 0.000 claims description 5
- 230000001036 exonucleolytic effect Effects 0.000 claims description 5
- 102000004533 Endonucleases Human genes 0.000 claims description 4
- 238000009739 binding Methods 0.000 claims description 4
- 210000004899 c-terminal region Anatomy 0.000 claims description 4
- 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 claims description 4
- 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 claims description 3
- 230000000694 effects Effects 0.000 claims description 3
- 230000001293 nucleolytic effect Effects 0.000 claims description 3
- 125000003396 thiol group Chemical group [H]S* 0.000 claims description 3
- 239000002253 acid Substances 0.000 claims description 2
- 239000001963 growth medium Substances 0.000 claims description 2
- 239000006166 lysate Substances 0.000 claims description 2
- 230000000750 progressive effect Effects 0.000 claims description 2
- 125000003275 alpha amino acid group Chemical group 0.000 claims 11
- 125000002480 thymidyl group Chemical group 0.000 claims 2
- KHWCHTKSEGGWEX-RRKCRQDMSA-N 2'-deoxyadenosine 5'-monophosphate Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@H]1C[C@H](O)[C@@H](COP(O)(O)=O)O1 KHWCHTKSEGGWEX-RRKCRQDMSA-N 0.000 claims 1
- 102000012410 DNA Ligases Human genes 0.000 claims 1
- 108010061982 DNA Ligases Proteins 0.000 claims 1
- 241001131785 Escherichia coli HB101 Species 0.000 claims 1
- 101500025353 Homo sapiens Insulin A chain Proteins 0.000 claims 1
- 101500025354 Homo sapiens Insulin B chain Proteins 0.000 claims 1
- -1 acids amines Chemical group 0.000 claims 1
- 238000010504 bond cleavage reaction Methods 0.000 claims 1
- 235000018102 proteins Nutrition 0.000 description 56
- 210000004027 cell Anatomy 0.000 description 41
- 235000001014 amino acid Nutrition 0.000 description 28
- 229940024606 amino acid Drugs 0.000 description 28
- 108020004705 Codon Proteins 0.000 description 18
- 229940088598 enzyme Drugs 0.000 description 16
- 238000003780 insertion Methods 0.000 description 14
- 230000037431 insertion Effects 0.000 description 14
- 108091026890 Coding region Proteins 0.000 description 11
- 102100031780 Endonuclease Human genes 0.000 description 11
- 108020004999 messenger RNA Proteins 0.000 description 10
- 238000011282 treatment Methods 0.000 description 9
- 241000700159 Rattus Species 0.000 description 8
- 230000008901 benefit Effects 0.000 description 8
- RWQNBRDOKXIBIV-UHFFFAOYSA-N thymine Chemical compound CC1=CNC(=O)NC1=O RWQNBRDOKXIBIV-UHFFFAOYSA-N 0.000 description 8
- 230000014616 translation Effects 0.000 description 8
- 241000894006 Bacteria Species 0.000 description 7
- 239000013613 expression plasmid Substances 0.000 description 7
- 238000002955 isolation Methods 0.000 description 7
- 238000000746 purification Methods 0.000 description 7
- KDCGOANMDULRCW-UHFFFAOYSA-N 7H-purine Chemical compound N1=CNC2=NC=NC2=C1 KDCGOANMDULRCW-UHFFFAOYSA-N 0.000 description 6
- 230000006870 function Effects 0.000 description 6
- 238000013519 translation Methods 0.000 description 6
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 5
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 5
- 108091028043 Nucleic acid sequence Proteins 0.000 description 5
- 108020004511 Recombinant DNA Proteins 0.000 description 5
- ISAKRJDGNUQOIC-UHFFFAOYSA-N Uracil Natural products O=C1C=CNC(=O)N1 ISAKRJDGNUQOIC-UHFFFAOYSA-N 0.000 description 5
- 230000000295 complement effect Effects 0.000 description 5
- 238000005516 engineering process Methods 0.000 description 5
- 238000009396 hybridization Methods 0.000 description 5
- 238000000338 in vitro Methods 0.000 description 5
- 230000000977 initiatory effect Effects 0.000 description 5
- 230000001105 regulatory effect Effects 0.000 description 5
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 4
- 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 4
- 108091034117 Oligonucleotide Proteins 0.000 description 4
- OPTASPLRGRRNAP-UHFFFAOYSA-N cytosine Chemical compound NC=1C=CNC(=O)N=1 OPTASPLRGRRNAP-UHFFFAOYSA-N 0.000 description 4
- RGWHQCVHVJXOKC-SHYZEUOFSA-N dCTP Chemical compound O=C1N=C(N)C=CN1[C@@H]1O[C@H](CO[P@](O)(=O)O[P@](O)(=O)OP(O)(O)=O)[C@@H](O)C1 RGWHQCVHVJXOKC-SHYZEUOFSA-N 0.000 description 4
- 230000008030 elimination Effects 0.000 description 4
- 238000003379 elimination reaction Methods 0.000 description 4
- 210000003527 eukaryotic cell Anatomy 0.000 description 4
- 230000029142 excretion Effects 0.000 description 4
- 229940088597 hormone Drugs 0.000 description 4
- 239000005556 hormone Substances 0.000 description 4
- 239000008101 lactose Substances 0.000 description 4
- 210000000496 pancreas Anatomy 0.000 description 4
- 229940113082 thymine Drugs 0.000 description 4
- 238000013518 transcription Methods 0.000 description 4
- 230000035897 transcription Effects 0.000 description 4
- 108010008286 DNA nucleotidylexotransferase Proteins 0.000 description 3
- 102100029764 DNA-directed DNA/RNA polymerase mu Human genes 0.000 description 3
- 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 3
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 3
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 3
- 108010076504 Protein Sorting Signals Proteins 0.000 description 3
- 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 3
- 210000003719 b-lymphocyte Anatomy 0.000 description 3
- 230000001580 bacterial effect Effects 0.000 description 3
- 230000027455 binding Effects 0.000 description 3
- 238000010276 construction Methods 0.000 description 3
- 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 3
- 230000002255 enzymatic effect Effects 0.000 description 3
- 238000001502 gel electrophoresis Methods 0.000 description 3
- UYTPUPDQBNUYGX-UHFFFAOYSA-N guanine Chemical compound O=C1NC(N)=NC2=C1N=CN2 UYTPUPDQBNUYGX-UHFFFAOYSA-N 0.000 description 3
- 230000003301 hydrolyzing effect Effects 0.000 description 3
- 230000007246 mechanism Effects 0.000 description 3
- 229930182817 methionine Natural products 0.000 description 3
- 229920001184 polypeptide Polymers 0.000 description 3
- 238000000926 separation method Methods 0.000 description 3
- 241000894007 species Species 0.000 description 3
- 230000009466 transformation Effects 0.000 description 3
- 229940035893 uracil Drugs 0.000 description 3
- 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 2
- 239000004475 Arginine Substances 0.000 description 2
- 108020004635 Complementary DNA Proteins 0.000 description 2
- 108060002716 Exonuclease Proteins 0.000 description 2
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 2
- 239000004471 Glycine Substances 0.000 description 2
- 241000282412 Homo Species 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
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-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
- 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
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 2
- 241000124008 Mammalia Species 0.000 description 2
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 2
- 108010087702 Penicillinase Proteins 0.000 description 2
- 108010092799 RNA-directed DNA polymerase Proteins 0.000 description 2
- 239000004098 Tetracycline Substances 0.000 description 2
- 102000004142 Trypsin Human genes 0.000 description 2
- 108090000631 Trypsin Proteins 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
- 230000009471 action Effects 0.000 description 2
- 235000004279 alanine Nutrition 0.000 description 2
- 125000003295 alanine group Chemical group N[C@@H](C)C(=O)* 0.000 description 2
- 229960000723 ampicillin Drugs 0.000 description 2
- 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 2
- 238000004458 analytical method Methods 0.000 description 2
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 2
- 238000000376 autoradiography Methods 0.000 description 2
- 235000015278 beef Nutrition 0.000 description 2
- AIYUHDOJVYHVIT-UHFFFAOYSA-M caesium chloride Chemical compound [Cl-].[Cs+] AIYUHDOJVYHVIT-UHFFFAOYSA-M 0.000 description 2
- 210000000170 cell membrane Anatomy 0.000 description 2
- 210000004671 cell-free system Anatomy 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 238000001311 chemical methods and process Methods 0.000 description 2
- 238000004587 chromatography analysis Methods 0.000 description 2
- 239000000470 constituent Substances 0.000 description 2
- 229940104302 cytosine Drugs 0.000 description 2
- 206010012601 diabetes mellitus Diseases 0.000 description 2
- 102000013165 exonuclease Human genes 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 230000004927 fusion Effects 0.000 description 2
- 238000001727 in vivo Methods 0.000 description 2
- 239000003999 initiator Substances 0.000 description 2
- 239000002609 medium Substances 0.000 description 2
- 230000002503 metabolic effect Effects 0.000 description 2
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 2
- 229950009506 penicillinase Drugs 0.000 description 2
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 2
- 235000015277 pork Nutrition 0.000 description 2
- 210000001236 prokaryotic cell Anatomy 0.000 description 2
- 230000000644 propagated effect Effects 0.000 description 2
- 238000001243 protein synthesis Methods 0.000 description 2
- 239000011541 reaction mixture Substances 0.000 description 2
- 230000029058 respiratory gaseous exchange Effects 0.000 description 2
- 230000009870 specific binding Effects 0.000 description 2
- 230000002269 spontaneous effect Effects 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 229960002180 tetracycline Drugs 0.000 description 2
- 229930101283 tetracycline Natural products 0.000 description 2
- 235000019364 tetracycline Nutrition 0.000 description 2
- 150000003522 tetracyclines Chemical class 0.000 description 2
- 230000032258 transport Effects 0.000 description 2
- 125000002264 triphosphate group Chemical group [H]OP(=O)(O[H])OP(=O)(O[H])OP(=O)(O[H])O* 0.000 description 2
- 239000012588 trypsin Substances 0.000 description 2
- 241001515965 unidentified phage Species 0.000 description 2
- OCKGFTQIICXDQW-ZEQRLZLVSA-N 5-[(1r)-1-hydroxy-2-[4-[(2r)-2-hydroxy-2-(4-methyl-1-oxo-3h-2-benzofuran-5-yl)ethyl]piperazin-1-yl]ethyl]-4-methyl-3h-2-benzofuran-1-one Chemical compound C1=C2C(=O)OCC2=C(C)C([C@@H](O)CN2CCN(CC2)C[C@H](O)C2=CC=C3C(=O)OCC3=C2C)=C1 OCKGFTQIICXDQW-ZEQRLZLVSA-N 0.000 description 1
- ZKHQWZAMYRWXGA-KQYNXXCUSA-J ATP(4-) Chemical compound 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 ZKHQWZAMYRWXGA-KQYNXXCUSA-J 0.000 description 1
- 229930024421 Adenine Natural products 0.000 description 1
- GFFGJBXGBJISGV-UHFFFAOYSA-N Adenine Chemical compound NC1=NC=NC2=C1N=CN2 GFFGJBXGBJISGV-UHFFFAOYSA-N 0.000 description 1
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 1
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
- 102000003670 Carboxypeptidase B Human genes 0.000 description 1
- 108090000087 Carboxypeptidase B Proteins 0.000 description 1
- 102000005572 Cathepsin A Human genes 0.000 description 1
- 108010059081 Cathepsin A Proteins 0.000 description 1
- 102000003902 Cathepsin C Human genes 0.000 description 1
- 108090000267 Cathepsin C Proteins 0.000 description 1
- 108020004638 Circular DNA Proteins 0.000 description 1
- 108090000204 Dipeptidase 1 Proteins 0.000 description 1
- 102000003839 Human Proteins Human genes 0.000 description 1
- 108090000144 Human Proteins Proteins 0.000 description 1
- 229920001202 Inulin Polymers 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
- DEFJQIDDEAULHB-IMJSIDKUSA-N L-alanyl-L-alanine Chemical compound C[C@H](N)C(=O)N[C@@H](C)C(O)=O DEFJQIDDEAULHB-IMJSIDKUSA-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
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 1
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
- 102000003960 Ligases Human genes 0.000 description 1
- 108090000364 Ligases Proteins 0.000 description 1
- 101500021084 Locusta migratoria 5 kDa peptide Proteins 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- 206010028980 Neoplasm Diseases 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 101800004937 Protein C Proteins 0.000 description 1
- CZPWVGJYEJSRLH-UHFFFAOYSA-N Pyrimidine Chemical compound C1=CN=CN=C1 CZPWVGJYEJSRLH-UHFFFAOYSA-N 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- 101800001700 Saposin-D Proteins 0.000 description 1
- 102400000827 Saposin-D Human genes 0.000 description 1
- 229920005654 Sephadex Polymers 0.000 description 1
- 239000012507 Sephadex™ Substances 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- 108700005078 Synthetic Genes Proteins 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
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- 229960000643 adenine Drugs 0.000 description 1
- 108010056243 alanylalanine Proteins 0.000 description 1
- 230000000172 allergic effect Effects 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 239000000427 antigen Substances 0.000 description 1
- 108091007433 antigens Proteins 0.000 description 1
- 102000036639 antigens Human genes 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
- 208000010668 atopic eczema Diseases 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
- 102000006635 beta-lactamase Human genes 0.000 description 1
- 239000011230 binding agent Substances 0.000 description 1
- 230000001851 biosynthetic effect Effects 0.000 description 1
- 238000010804 cDNA synthesis Methods 0.000 description 1
- 230000003197 catalytic effect Effects 0.000 description 1
- 239000002131 composite material Substances 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 239000004020 conductor Substances 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- ATDGTVJJHBUTRL-UHFFFAOYSA-N cyanogen bromide Chemical compound BrC#N ATDGTVJJHBUTRL-UHFFFAOYSA-N 0.000 description 1
- 125000004122 cyclic group Chemical group 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
- 238000013461 design Methods 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 230000018109 developmental process Effects 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- 229960001484 edetic acid Drugs 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- 210000002472 endoplasmic reticulum Anatomy 0.000 description 1
- 238000011049 filling Methods 0.000 description 1
- 238000005194 fractionation Methods 0.000 description 1
- 238000013467 fragmentation Methods 0.000 description 1
- 238000006062 fragmentation reaction Methods 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
- 150000002333 glycines Chemical class 0.000 description 1
- 230000001456 gonadotroph Effects 0.000 description 1
- 230000009931 harmful effect Effects 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 238000011065 in-situ storage Methods 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 206010022498 insulinoma Diseases 0.000 description 1
- JYJIGFIDKWBXDU-MNNPPOADSA-N inulin Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)OC[C@]1(OC[C@]2(OC[C@]3(OC[C@]4(OC[C@]5(OC[C@]6(OC[C@]7(OC[C@]8(OC[C@]9(OC[C@]%10(OC[C@]%11(OC[C@]%12(OC[C@]%13(OC[C@]%14(OC[C@]%15(OC[C@]%16(OC[C@]%17(OC[C@]%18(OC[C@]%19(OC[C@]%20(OC[C@]%21(OC[C@]%22(OC[C@]%23(OC[C@]%24(OC[C@]%25(OC[C@]%26(OC[C@]%27(OC[C@]%28(OC[C@]%29(OC[C@]%30(OC[C@]%31(OC[C@]%32(OC[C@]%33(OC[C@]%34(OC[C@]%35(OC[C@]%36(O[C@@H]%37[C@@H]([C@@H](O)[C@H](O)[C@@H](CO)O%37)O)[C@H]([C@H](O)[C@@H](CO)O%36)O)[C@H]([C@H](O)[C@@H](CO)O%35)O)[C@H]([C@H](O)[C@@H](CO)O%34)O)[C@H]([C@H](O)[C@@H](CO)O%33)O)[C@H]([C@H](O)[C@@H](CO)O%32)O)[C@H]([C@H](O)[C@@H](CO)O%31)O)[C@H]([C@H](O)[C@@H](CO)O%30)O)[C@H]([C@H](O)[C@@H](CO)O%29)O)[C@H]([C@H](O)[C@@H](CO)O%28)O)[C@H]([C@H](O)[C@@H](CO)O%27)O)[C@H]([C@H](O)[C@@H](CO)O%26)O)[C@H]([C@H](O)[C@@H](CO)O%25)O)[C@H]([C@H](O)[C@@H](CO)O%24)O)[C@H]([C@H](O)[C@@H](CO)O%23)O)[C@H]([C@H](O)[C@@H](CO)O%22)O)[C@H]([C@H](O)[C@@H](CO)O%21)O)[C@H]([C@H](O)[C@@H](CO)O%20)O)[C@H]([C@H](O)[C@@H](CO)O%19)O)[C@H]([C@H](O)[C@@H](CO)O%18)O)[C@H]([C@H](O)[C@@H](CO)O%17)O)[C@H]([C@H](O)[C@@H](CO)O%16)O)[C@H]([C@H](O)[C@@H](CO)O%15)O)[C@H]([C@H](O)[C@@H](CO)O%14)O)[C@H]([C@H](O)[C@@H](CO)O%13)O)[C@H]([C@H](O)[C@@H](CO)O%12)O)[C@H]([C@H](O)[C@@H](CO)O%11)O)[C@H]([C@H](O)[C@@H](CO)O%10)O)[C@H]([C@H](O)[C@@H](CO)O9)O)[C@H]([C@H](O)[C@@H](CO)O8)O)[C@H]([C@H](O)[C@@H](CO)O7)O)[C@H]([C@H](O)[C@@H](CO)O6)O)[C@H]([C@H](O)[C@@H](CO)O5)O)[C@H]([C@H](O)[C@@H](CO)O4)O)[C@H]([C@H](O)[C@@H](CO)O3)O)[C@H]([C@H](O)[C@@H](CO)O2)O)[C@@H](O)[C@H](O)[C@@H](CO)O1 JYJIGFIDKWBXDU-MNNPPOADSA-N 0.000 description 1
- 229940029339 inulin 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
- 229960000310 isoleucine Drugs 0.000 description 1
- 238000005304 joining Methods 0.000 description 1
- 238000002372 labelling Methods 0.000 description 1
- 150000002597 lactoses Chemical class 0.000 description 1
- 125000003588 lysine group Chemical group [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 230000008384 membrane barrier Effects 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 208000021255 pancreatic insulinoma Diseases 0.000 description 1
- 230000037361 pathway Effects 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- 210000001322 periplasm Anatomy 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 125000002467 phosphate group Chemical group [H]OP(=O)(O[H])O[*] 0.000 description 1
- 230000001817 pituitary effect Effects 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 229940025656 proin Drugs 0.000 description 1
- 230000035755 proliferation Effects 0.000 description 1
- 229960000856 protein c Drugs 0.000 description 1
- 230000007026 protein scission Effects 0.000 description 1
- 238000011403 purification operation Methods 0.000 description 1
- 238000003127 radioimmunoassay Methods 0.000 description 1
- 210000003705 ribosome Anatomy 0.000 description 1
- 229920002477 rna polymer Polymers 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 210000004739 secretory vesicle Anatomy 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 238000006467 substitution reaction Methods 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 230000001629 suppression Effects 0.000 description 1
- 238000001308 synthesis method Methods 0.000 description 1
- 230000002194 synthesizing effect Effects 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 230000001225 therapeutic effect Effects 0.000 description 1
- 230000001131 transforming effect Effects 0.000 description 1
- 230000017105 transposition Effects 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
- 239000004474 valine Substances 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/575—Hormones
- C07K14/62—Insulins
-
- 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
-
- 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
- C12N1/00—Microorganisms, e.g. protozoa; Compositions thereof; Processes of propagating, maintaining or preserving microorganisms or compositions thereof; Processes of preparing or isolating a composition containing a microorganism; Culture media therefor
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Organic Chemistry (AREA)
- Genetics & Genomics (AREA)
- Zoology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Wood Science & Technology (AREA)
- Biotechnology (AREA)
- Biomedical Technology (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Biophysics (AREA)
- Molecular Biology (AREA)
- Microbiology (AREA)
- Medicinal Chemistry (AREA)
- Virology (AREA)
- Physics & Mathematics (AREA)
- Tropical Medicine & Parasitology (AREA)
- Plant Pathology (AREA)
- Diabetes (AREA)
- Endocrinology (AREA)
- Toxicology (AREA)
- Gastroenterology & Hepatology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Saccharide Compounds (AREA)
- Peptides Or Proteins (AREA)
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US7519279A | 1979-09-12 | 1979-09-12 | |
US7519279 | 1979-09-12 |
Publications (1)
Publication Number | Publication Date |
---|---|
LU82757A1 true LU82757A1 (fr) | 1981-02-02 |
Family
ID=22124154
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
LU82757A LU82757A1 (fr) | 1979-09-12 | 1980-09-10 | Genes de la proinsuline humaine et de pre-proinsuline humaine,leur procede de preparation et leurs applications |
Country Status (28)
Country | Link |
---|---|
EP (1) | EP0026598A1 (en]) |
JP (1) | JP2637393B2 (en]) |
KR (1) | KR870000501B1 (en]) |
AT (1) | AT377003B (en]) |
AU (1) | AU538154B2 (en]) |
BE (1) | BE885196A (en]) |
BG (2) | BG41136A3 (en]) |
CA (1) | CA1180289A (en]) |
CZ (2) | CZ278883B6 (en]) |
DD (3) | DD155004A5 (en]) |
DK (1) | DK385980A (en]) |
ES (3) | ES8107307A1 (en]) |
FI (1) | FI802837A7 (en]) |
FR (1) | FR2464997B1 (en]) |
GR (1) | GR70279B (en]) |
IE (1) | IE52781B1 (en]) |
IL (1) | IL61041A (en]) |
IT (1) | IT1129250B (en]) |
LU (1) | LU82757A1 (en]) |
NZ (1) | NZ194786A (en]) |
PH (1) | PH26475A (en]) |
PL (1) | PL226725A1 (en]) |
PT (1) | PT71790B (en]) |
RO (1) | RO80005A (en]) |
SK (1) | SK621580A3 (en]) |
SU (1) | SU1491345A3 (en]) |
YU (1) | YU233480A (en]) |
ZA (1) | ZA805341B (en]) |
Families Citing this family (14)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US4342832A (en) * | 1979-07-05 | 1982-08-03 | Genentech, Inc. | Method of constructing a replicable cloning vehicle having quasi-synthetic genes |
DE3001928A1 (de) * | 1980-01-19 | 1981-08-06 | Hoechst Ag, 6000 Frankfurt | Genprodukt eines hoeheren organismus aus einem dieses gen enthaltenden mikroorganismus |
US4249952A (en) * | 1980-03-03 | 1981-02-10 | Pennsylvania Engineering Corporation | Method for producing cement clinker from cement kiln waste dust |
AU545912B2 (en) * | 1980-03-10 | 1985-08-08 | Cetus Corporation | Cloned heterologous jive products in bacillies |
US4338397A (en) * | 1980-04-11 | 1982-07-06 | President And Fellows Of Harvard College | Mature protein synthesis |
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 |
ZA824218B (en) * | 1981-06-29 | 1983-04-27 | Cetus Corp | Plasmid for producing human insulin |
JPS58183659A (ja) * | 1982-03-31 | 1983-10-26 | ジェネテイックス、インスチチュ−ト、インコ−ポレ−テッド | 修飾プロインシュリン前駆体、これを暗号化するdna配列およびそれらの産生方法 |
US5023321A (en) * | 1982-12-13 | 1991-06-11 | Howard Florey Institute Of Experimental Physiology & Medicine | Molecular cloning and characterization of a further gene sequence coding for human relaxin |
IL70414A (en) * | 1982-12-13 | 1991-06-10 | Florey Howard Inst | Polypeptide having human h2-relaxin activity,double-stranded dna fragments coding therefor,vectors containing the dna fragments and methods for preparing the polypeptide,dna fragments and vectors |
IL71991A (en) | 1983-06-06 | 1994-05-30 | Genentech Inc | Preparation of human FGI and FGE in their processed form through recombinant AND tranology in prokaryotes |
DE3751863T2 (de) * | 1986-05-20 | 1996-12-12 | Gen Hospital Corp | Bestimmung der Insulin Expression |
EP1997900A3 (en) | 1996-04-05 | 2010-10-06 | Novartis Vaccines and Diagnostics, Inc. | Recombinant alphavirus-based vectors with reduced inhibition of cellular macromolecular synthesis |
AUPP655698A0 (en) * | 1998-10-16 | 1998-11-05 | Commonwealth Scientific And Industrial Research Organisation | Delivery system for porcine somatotropin |
Family Cites Families (5)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
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 |
CA1215921A (en) * | 1977-11-08 | 1986-12-30 | Arthur D. Riggs | Method and means for microbial polypeptide expression |
FI783367A7 (fi) * | 1977-11-08 | 1979-05-09 | Genentech Inc | Syntetisk dna och foerfarande foer dess framstaellning |
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 |
-
1980
- 1980-08-25 GR GR62740A patent/GR70279B/el unknown
- 1980-08-27 NZ NZ194786A patent/NZ194786A/en unknown
- 1980-08-28 ZA ZA00805341A patent/ZA805341B/xx unknown
- 1980-09-09 FR FR8019399A patent/FR2464997B1/fr not_active Expired
- 1980-09-10 PT PT71790A patent/PT71790B/pt unknown
- 1980-09-10 FI FI802837A patent/FI802837A7/fi not_active Application Discontinuation
- 1980-09-10 IL IL61041A patent/IL61041A/xx not_active IP Right Cessation
- 1980-09-10 LU LU82757A patent/LU82757A1/fr unknown
- 1980-09-11 SU SU802994154A patent/SU1491345A3/ru active
- 1980-09-11 IT IT68405/80A patent/IT1129250B/it active
- 1980-09-11 AT AT0458580A patent/AT377003B/de not_active IP Right Cessation
- 1980-09-11 PH PH24566A patent/PH26475A/en unknown
- 1980-09-11 AU AU62324/80A patent/AU538154B2/en not_active Expired
- 1980-09-11 EP EP80303195A patent/EP0026598A1/en not_active Ceased
- 1980-09-11 DK DK385980A patent/DK385980A/da not_active Application Discontinuation
- 1980-09-11 CA CA000360565A patent/CA1180289A/en not_active Expired
- 1980-09-11 BE BE0/202074A patent/BE885196A/fr not_active IP Right Cessation
- 1980-09-12 PL PL22672580A patent/PL226725A1/xx unknown
- 1980-09-12 IE IE1912/80A patent/IE52781B1/en unknown
- 1980-09-12 CZ CS806215A patent/CZ278883B6/cs unknown
- 1980-09-12 BG BG049043A patent/BG41136A3/xx unknown
- 1980-09-12 KR KR1019800003590A patent/KR870000501B1/ko not_active Expired
- 1980-09-12 RO RO80102151A patent/RO80005A/ro unknown
- 1980-09-12 DD DD80223873A patent/DD155004A5/de unknown
- 1980-09-12 YU YU02334/80A patent/YU233480A/xx unknown
- 1980-09-12 DD DD80238569A patent/DD201693A5/de unknown
- 1980-09-12 JP JP55127043A patent/JP2637393B2/ja not_active Expired - Lifetime
- 1980-09-12 SK SK6215-80A patent/SK621580A3/sk unknown
- 1980-09-12 BG BG057337A patent/BG41137A3/xx unknown
- 1980-09-12 DD DD80238563A patent/DD208989A5/de unknown
- 1980-09-12 ES ES495030A patent/ES8107307A1/es not_active Expired
-
1981
- 1981-06-30 ES ES503567A patent/ES503567A0/es active Granted
- 1981-06-30 ES ES503568A patent/ES503568A0/es active Granted
-
1984
- 1984-07-16 CZ CS845488A patent/CZ548884A3/cs unknown
Also Published As
Similar Documents
Publication | Publication Date | Title |
---|---|---|
US4431740A (en) | DNA Transfer vector and transformed microorganism containing human proinsulin and pre-proinsulin genes | |
DK166784B1 (da) | Rekombinant dna-sekvens, en mikroorganisme indeholdende sekvensen og en fremgangsmaade til fremstilling af et eucaryot protein | |
FR2460330A1 (fr) | Procede de production d'un vecteur de clonage duplicable comportant un gene quasi-synthetique codant une proteine, vecteur de clonage ainsi obtenu et procede d'obtention de la proteine codee par le gene quasi-synthetique | |
CS219257B2 (en) | Method of making the eukaryotic protein | |
FR2730495A1 (fr) | Derive de proinsuline et procede pour la production d'insuline humaine | |
KR101299417B1 (ko) | 카복시-말단 아미드화 펩티드를 제조하는 방법 | |
LU82757A1 (fr) | Genes de la proinsuline humaine et de pre-proinsuline humaine,leur procede de preparation et leurs applications | |
FR2555199A1 (fr) | Procede de clivage d'adn bicatenaire en n'importe quel point donne | |
JP2892596B2 (ja) | ヒト−レラキシン遺伝子 | |
JP2000504574A (ja) | カルシトニン・フラグメントの組換え調製、ならびにカルシトニンおよび関連アナログの調製におけるその使用 | |
WO1986005803A1 (fr) | Procede d'obtention d'adn, arn, peptides, polypeptides ou proteines, par une technique de recombinaison d'adn | |
Izard et al. | Physical and conformational properties of synthetic idealized signal sequences parallel their biological function | |
JPS59156284A (ja) | ヒト−レラキシンh2遺伝子 | |
RU2144957C1 (ru) | РЕКОМБИНАНТНАЯ ПЛАЗМИДНАЯ ДНК pPINS07, КОДИРУЮЩАЯ ГИБРИДНЫЙ ПОЛИПЕПТИД, СОДЕРЖАЩИЙ ПРОИНСУЛИН ЧЕЛОВЕКА, И ШТАММ БАКТЕРИЙ Escherichia coli - ПРОДУЦЕНТ ГИБРИДНОГО ПОЛИПЕПТИДА, СОДЕРЖАЩЕГО ПРОИНСУЛИН ЧЕЛОВЕКА | |
JPH03503596A (ja) | 蛋白質若しくはポリペプチドの調製方法、該ポリペプチドをコードするdna配列、該dna配列およびポリペプチドを有する微生物および該ポリペプチドの薬学的製剤としての利用 | |
EP0252894A2 (fr) | Polypeptides hybrides comprenant la somatocrinine et l'alpha1-antitrypsine, méthode pour leur production à partir de clones bactériens et leur utilisation pour la production de somatocrinine | |
EP0259891B1 (en) | [Leu 13] motilin, DNAs coding for same and methods for producing same | |
JP2612264B2 (ja) | Dna配列体 | |
KR0161656B1 (ko) | 글루카곤의 생산방법 | |
JPS58183659A (ja) | 修飾プロインシュリン前駆体、これを暗号化するdna配列およびそれらの産生方法 | |
CA1302321C (en) | Preparation of polypeptides | |
RIGGS et al. | Synthesis, cloning, and expression of hormone genes in Escherichia coli | |
JPS60502136A (ja) | 微生物によるインタ−ル−キン2の形質発現 | |
JPS60501989A (ja) | インシュリン様成長因子の微生物発現 | |
KR19980061879A (ko) | 조피볼낙 성장 호르몬의 대량생산 방법 |