BE898016A - Muteines appauvries en cysteine provenant de proteines biologiquement actives. - Google Patents
Muteines appauvries en cysteine provenant de proteines biologiquement actives. Download PDFInfo
- Publication number
- BE898016A BE898016A BE0/211722A BE211722A BE898016A BE 898016 A BE898016 A BE 898016A BE 0/211722 A BE0/211722 A BE 0/211722A BE 211722 A BE211722 A BE 211722A BE 898016 A BE898016 A BE 898016A
- Authority
- BE
- Belgium
- Prior art keywords
- cysteine
- ifn
- protein
- codon
- dna
- Prior art date
Links
- 108090000623 proteins and genes Proteins 0.000 title claims abstract description 103
- 102000004169 proteins and genes Human genes 0.000 title claims abstract description 63
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 title claims description 28
- 235000018102 proteins Nutrition 0.000 claims abstract description 61
- 108010002350 Interleukin-2 Proteins 0.000 claims abstract description 48
- 108091034117 Oligonucleotide Proteins 0.000 claims abstract description 38
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 claims abstract description 34
- 150000001413 amino acids Chemical class 0.000 claims abstract description 32
- 235000001014 amino acid Nutrition 0.000 claims abstract description 25
- 230000004071 biological effect Effects 0.000 claims abstract description 17
- 238000002741 site-directed mutagenesis Methods 0.000 claims abstract description 8
- 230000001580 bacterial effect Effects 0.000 claims abstract description 7
- 108020004414 DNA Proteins 0.000 claims description 53
- 108020004705 Codon Proteins 0.000 claims description 50
- 102000000588 Interleukin-2 Human genes 0.000 claims description 39
- 238000000034 method Methods 0.000 claims description 33
- 230000000694 effects Effects 0.000 claims description 31
- 235000018417 cysteine Nutrition 0.000 claims description 30
- 229940024606 amino acid Drugs 0.000 claims description 24
- 230000035772 mutation Effects 0.000 claims description 21
- 241000588724 Escherichia coli Species 0.000 claims description 20
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 claims description 19
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 claims description 18
- 239000013612 plasmid Substances 0.000 claims description 18
- 239000000203 mixture Substances 0.000 claims description 17
- 230000001225 therapeutic effect Effects 0.000 claims description 12
- 108091027305 Heteroduplex Proteins 0.000 claims description 11
- 239000002773 nucleotide Substances 0.000 claims description 11
- 125000003729 nucleotide group Chemical group 0.000 claims description 11
- 239000013598 vector Substances 0.000 claims description 11
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 10
- 241000894006 Bacteria Species 0.000 claims description 9
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 claims description 7
- 239000004473 Threonine Substances 0.000 claims description 7
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 claims description 6
- 239000013604 expression vector Substances 0.000 claims description 6
- 238000002955 isolation Methods 0.000 claims description 6
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 claims description 5
- 102000016928 DNA-directed DNA polymerase Human genes 0.000 claims description 5
- 101001002657 Homo sapiens Interleukin-2 Proteins 0.000 claims description 5
- 230000000295 complement effect Effects 0.000 claims description 5
- 238000004519 manufacturing process Methods 0.000 claims description 5
- 230000009466 transformation Effects 0.000 claims description 5
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 claims description 4
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 claims description 4
- 229930182817 methionine Natural products 0.000 claims description 4
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 claims description 3
- 230000010076 replication Effects 0.000 claims description 3
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 claims description 3
- 239000004471 Glycine Substances 0.000 claims description 2
- 101150083678 IL2 gene Proteins 0.000 claims description 2
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 claims description 2
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 claims description 2
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 claims description 2
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 claims description 2
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 claims description 2
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 claims description 2
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 claims description 2
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 claims description 2
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 claims description 2
- 235000004279 alanine Nutrition 0.000 claims description 2
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 claims description 2
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 claims description 2
- 229960000310 isoleucine Drugs 0.000 claims description 2
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 claims description 2
- 239000004474 valine Substances 0.000 claims description 2
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 claims 4
- 229960005375 lutein Drugs 0.000 claims 1
- KBPHJBAIARWVSC-RGZFRNHPSA-N lutein Chemical compound C([C@H](O)CC=1C)C(C)(C)C=1\C=C\C(\C)=C\C=C\C(\C)=C\C=C\C=C(/C)\C=C\C=C(/C)\C=C\[C@H]1C(C)=C[C@H](O)CC1(C)C KBPHJBAIARWVSC-RGZFRNHPSA-N 0.000 claims 1
- ORAKUVXRZWMARG-WZLJTJAWSA-N lutein Natural products CC(=C/C=C/C=C(C)/C=C/C=C(C)/C=C/C1=C(C)CCCC1(C)C)C=CC=C(/C)C=CC2C(=CC(O)CC2(C)C)C ORAKUVXRZWMARG-WZLJTJAWSA-N 0.000 claims 1
- 235000012680 lutein Nutrition 0.000 claims 1
- 239000001656 lutein Substances 0.000 claims 1
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 claims 1
- 230000001629 suppression Effects 0.000 claims 1
- KBPHJBAIARWVSC-XQIHNALSSA-N trans-lutein Natural products CC(=C/C=C/C=C(C)/C=C/C=C(C)/C=C/C1=C(C)CC(O)CC1(C)C)C=CC=C(/C)C=CC2C(=CC(O)CC2(C)C)C KBPHJBAIARWVSC-XQIHNALSSA-N 0.000 claims 1
- 230000001131 transforming effect Effects 0.000 claims 1
- FJHBOVDFOQMZRV-XQIHNALSSA-N xanthophyll Natural products CC(=C/C=C/C=C(C)/C=C/C=C(C)/C=C/C1=C(C)CC(O)CC1(C)C)C=CC=C(/C)C=CC2C=C(C)C(O)CC2(C)C FJHBOVDFOQMZRV-XQIHNALSSA-N 0.000 claims 1
- 230000015572 biosynthetic process Effects 0.000 abstract description 8
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 abstract description 3
- 238000004132 cross linking Methods 0.000 abstract description 2
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 36
- 210000004027 cell Anatomy 0.000 description 25
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 20
- 239000000872 buffer Substances 0.000 description 16
- 239000000284 extract Substances 0.000 description 16
- 238000009396 hybridization Methods 0.000 description 14
- 235000004400 serine Nutrition 0.000 description 13
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 11
- 238000002703 mutagenesis Methods 0.000 description 11
- 231100000350 mutagenesis Toxicity 0.000 description 11
- 239000000047 product Substances 0.000 description 11
- 101100498071 Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) cys-17 gene Proteins 0.000 description 10
- 239000000243 solution Substances 0.000 description 10
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 9
- 230000008859 change Effects 0.000 description 9
- 239000012634 fragment Substances 0.000 description 9
- 238000002360 preparation method Methods 0.000 description 9
- 239000011780 sodium chloride Substances 0.000 description 9
- 102000053602 DNA Human genes 0.000 description 8
- TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 8
- 108091000080 Phosphotransferase Proteins 0.000 description 8
- 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 8
- 239000002299 complementary DNA Substances 0.000 description 8
- 102000020233 phosphotransferase Human genes 0.000 description 8
- 238000000746 purification Methods 0.000 description 8
- 108091008146 restriction endonucleases Proteins 0.000 description 8
- 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 7
- 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 7
- 239000000499 gel Substances 0.000 description 7
- 230000008569 process Effects 0.000 description 7
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 6
- 102000012410 DNA Ligases Human genes 0.000 description 6
- 108010061982 DNA Ligases Proteins 0.000 description 6
- 102100040019 Interferon alpha-1/13 Human genes 0.000 description 6
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 6
- BTANRVKWQNVYAZ-UHFFFAOYSA-N butan-2-ol Chemical compound CCC(C)O BTANRVKWQNVYAZ-UHFFFAOYSA-N 0.000 description 6
- 238000010586 diagram Methods 0.000 description 6
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 6
- 229920001817 Agar Polymers 0.000 description 5
- 108010050904 Interferons Proteins 0.000 description 5
- 102000014150 Interferons Human genes 0.000 description 5
- 239000002253 acid Substances 0.000 description 5
- 239000008272 agar Substances 0.000 description 5
- 238000012217 deletion Methods 0.000 description 5
- 230000037430 deletion Effects 0.000 description 5
- 102000004594 DNA Polymerase I Human genes 0.000 description 4
- 108010017826 DNA Polymerase I Proteins 0.000 description 4
- 108020004682 Single-Stranded DNA Proteins 0.000 description 4
- 241000700605 Viruses Species 0.000 description 4
- 238000006243 chemical reaction Methods 0.000 description 4
- 230000000120 cytopathologic effect Effects 0.000 description 4
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 4
- 229940079322 interferon Drugs 0.000 description 4
- 229910001629 magnesium chloride Inorganic materials 0.000 description 4
- 108020004999 messenger RNA Proteins 0.000 description 4
- 239000000126 substance Substances 0.000 description 4
- 238000012360 testing method Methods 0.000 description 4
- 230000007704 transition Effects 0.000 description 4
- 229960004799 tryptophan Drugs 0.000 description 4
- 241000972773 Aulopiformes Species 0.000 description 3
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 3
- KRKNYBCHXYNGOX-UHFFFAOYSA-K Citrate Chemical compound [O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O KRKNYBCHXYNGOX-UHFFFAOYSA-K 0.000 description 3
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 3
- 229920001917 Ficoll Polymers 0.000 description 3
- 101150103227 IFN gene Proteins 0.000 description 3
- 108090000467 Interferon-beta Proteins 0.000 description 3
- 241001465754 Metazoa Species 0.000 description 3
- 239000000020 Nitrocellulose Substances 0.000 description 3
- 108020004511 Recombinant DNA Proteins 0.000 description 3
- 210000001744 T-lymphocyte Anatomy 0.000 description 3
- 239000011543 agarose gel Substances 0.000 description 3
- 229960000723 ampicillin Drugs 0.000 description 3
- 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 3
- 210000003719 b-lymphocyte Anatomy 0.000 description 3
- 229940098773 bovine serum albumin Drugs 0.000 description 3
- 150000001945 cysteines Chemical class 0.000 description 3
- 239000012153 distilled water Substances 0.000 description 3
- 238000000605 extraction Methods 0.000 description 3
- 238000010438 heat treatment Methods 0.000 description 3
- 230000007062 hydrolysis Effects 0.000 description 3
- 238000006460 hydrolysis reaction Methods 0.000 description 3
- 238000005497 microtitration Methods 0.000 description 3
- 238000012986 modification Methods 0.000 description 3
- 230000004048 modification Effects 0.000 description 3
- 229920001220 nitrocellulos Polymers 0.000 description 3
- 229940079938 nitrocellulose Drugs 0.000 description 3
- 239000012074 organic phase Substances 0.000 description 3
- 239000008188 pellet Substances 0.000 description 3
- 239000002953 phosphate buffered saline Substances 0.000 description 3
- 239000001267 polyvinylpyrrolidone Substances 0.000 description 3
- 229920000036 polyvinylpyrrolidone Polymers 0.000 description 3
- 235000013855 polyvinylpyrrolidone Nutrition 0.000 description 3
- 239000011541 reaction mixture Substances 0.000 description 3
- 235000019515 salmon Nutrition 0.000 description 3
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 2
- 108050009160 DNA polymerase 1 Proteins 0.000 description 2
- 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 2
- 102100031780 Endonuclease Human genes 0.000 description 2
- 102000004190 Enzymes Human genes 0.000 description 2
- 108090000790 Enzymes Proteins 0.000 description 2
- 241001646716 Escherichia coli K-12 Species 0.000 description 2
- 241001524679 Escherichia virus M13 Species 0.000 description 2
- ZHNUHDYFZUAESO-UHFFFAOYSA-N Formamide Chemical compound NC=O ZHNUHDYFZUAESO-UHFFFAOYSA-N 0.000 description 2
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 2
- 239000012981 Hank's balanced salt solution Substances 0.000 description 2
- 241000282412 Homo Species 0.000 description 2
- 108091006905 Human Serum Albumin Proteins 0.000 description 2
- 102000008100 Human Serum Albumin Human genes 0.000 description 2
- 102100026720 Interferon beta Human genes 0.000 description 2
- CSNNHWWHGAXBCP-UHFFFAOYSA-L Magnesium sulfate Chemical compound [Mg+2].[O-][S+2]([O-])([O-])[O-] CSNNHWWHGAXBCP-UHFFFAOYSA-L 0.000 description 2
- 102000001253 Protein Kinase Human genes 0.000 description 2
- 239000004098 Tetracycline Substances 0.000 description 2
- 208000036142 Viral infection Diseases 0.000 description 2
- FJWGYAHXMCUOOM-QHOUIDNNSA-N [(2s,3r,4s,5r,6r)-2-[(2r,3r,4s,5r,6s)-4,5-dinitrooxy-2-(nitrooxymethyl)-6-[(2r,3r,4s,5r,6s)-4,5,6-trinitrooxy-2-(nitrooxymethyl)oxan-3-yl]oxyoxan-3-yl]oxy-3,5-dinitrooxy-6-(nitrooxymethyl)oxan-4-yl] nitrate Chemical compound O([C@@H]1O[C@@H]([C@H]([C@H](O[N+]([O-])=O)[C@H]1O[N+]([O-])=O)O[C@H]1[C@@H]([C@@H](O[N+]([O-])=O)[C@H](O[N+]([O-])=O)[C@@H](CO[N+]([O-])=O)O1)O[N+]([O-])=O)CO[N+](=O)[O-])[C@@H]1[C@@H](CO[N+]([O-])=O)O[C@@H](O[N+]([O-])=O)[C@H](O[N+]([O-])=O)[C@H]1O[N+]([O-])=O FJWGYAHXMCUOOM-QHOUIDNNSA-N 0.000 description 2
- 230000002009 allergenic effect Effects 0.000 description 2
- 238000004458 analytical method Methods 0.000 description 2
- 230000000840 anti-viral effect Effects 0.000 description 2
- 238000000376 autoradiography Methods 0.000 description 2
- 238000011161 development Methods 0.000 description 2
- 239000000539 dimer Substances 0.000 description 2
- 239000003814 drug Substances 0.000 description 2
- 238000001962 electrophoresis Methods 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 239000000706 filtrate Substances 0.000 description 2
- 238000010353 genetic engineering Methods 0.000 description 2
- 125000003147 glycosyl group Chemical group 0.000 description 2
- 238000000338 in vitro Methods 0.000 description 2
- 239000007791 liquid phase Substances 0.000 description 2
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 2
- 231100000252 nontoxic Toxicity 0.000 description 2
- 230000003000 nontoxic effect Effects 0.000 description 2
- 108020004707 nucleic acids Proteins 0.000 description 2
- 102000039446 nucleic acids Human genes 0.000 description 2
- 150000007523 nucleic acids Chemical class 0.000 description 2
- 210000000287 oocyte Anatomy 0.000 description 2
- 238000007254 oxidation reaction Methods 0.000 description 2
- 210000005105 peripheral blood lymphocyte Anatomy 0.000 description 2
- 239000002504 physiological saline solution Substances 0.000 description 2
- 229920002401 polyacrylamide Polymers 0.000 description 2
- 239000013641 positive control Substances 0.000 description 2
- 238000001556 precipitation Methods 0.000 description 2
- 108060006633 protein kinase Proteins 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 230000035945 sensitivity Effects 0.000 description 2
- 238000000926 separation method Methods 0.000 description 2
- 239000012064 sodium phosphate buffer Substances 0.000 description 2
- 239000006228 supernatant Substances 0.000 description 2
- 239000000725 suspension Substances 0.000 description 2
- 230000002194 synthesizing effect Effects 0.000 description 2
- 229960002180 tetracycline Drugs 0.000 description 2
- 229930101283 tetracycline Natural products 0.000 description 2
- 235000019364 tetracycline Nutrition 0.000 description 2
- 150000003522 tetracyclines Chemical class 0.000 description 2
- CWERGRDVMFNCDR-UHFFFAOYSA-N thioglycolic acid Chemical compound OC(=O)CS CWERGRDVMFNCDR-UHFFFAOYSA-N 0.000 description 2
- 125000003396 thiol group Chemical group [H]S* 0.000 description 2
- GPRLSGONYQIRFK-MNYXATJNSA-N triton Chemical compound [3H+] GPRLSGONYQIRFK-MNYXATJNSA-N 0.000 description 2
- 230000003612 virological effect Effects 0.000 description 2
- 239000011534 wash buffer Substances 0.000 description 2
- OJHZNMVJJKMFGX-RNWHKREASA-N (4r,4ar,7ar,12bs)-9-methoxy-3-methyl-1,2,4,4a,5,6,7a,13-octahydro-4,12-methanobenzofuro[3,2-e]isoquinoline-7-one;2,3-dihydroxybutanedioic acid Chemical compound OC(=O)C(O)C(O)C(O)=O.O=C([C@@H]1O2)CC[C@H]3[C@]4([H])N(C)CC[C@]13C1=C2C(OC)=CC=C1C4 OJHZNMVJJKMFGX-RNWHKREASA-N 0.000 description 1
- LJGHYPLBDBRCRZ-UHFFFAOYSA-N 3-(3-aminophenyl)sulfonylaniline Chemical compound NC1=CC=CC(S(=O)(=O)C=2C=C(N)C=CC=2)=C1 LJGHYPLBDBRCRZ-UHFFFAOYSA-N 0.000 description 1
- QFVHZQCOUORWEI-UHFFFAOYSA-N 4-[(4-anilino-5-sulfonaphthalen-1-yl)diazenyl]-5-hydroxynaphthalene-2,7-disulfonic acid Chemical compound C=12C(O)=CC(S(O)(=O)=O)=CC2=CC(S(O)(=O)=O)=CC=1N=NC(C1=CC=CC(=C11)S(O)(=O)=O)=CC=C1NC1=CC=CC=C1 QFVHZQCOUORWEI-UHFFFAOYSA-N 0.000 description 1
- 101150101112 7 gene Proteins 0.000 description 1
- 241000193830 Bacillus <bacterium> Species 0.000 description 1
- 244000063299 Bacillus subtilis Species 0.000 description 1
- 235000014469 Bacillus subtilis Nutrition 0.000 description 1
- 241000770536 Bacillus thermophilus Species 0.000 description 1
- 241000193388 Bacillus thuringiensis Species 0.000 description 1
- 208000035143 Bacterial infection Diseases 0.000 description 1
- 108020004638 Circular DNA Proteins 0.000 description 1
- 108091026890 Coding region Proteins 0.000 description 1
- 241000699802 Cricetulus griseus Species 0.000 description 1
- 108010042407 Endonucleases Proteins 0.000 description 1
- 108060002716 Exonuclease Proteins 0.000 description 1
- 206010017533 Fungal infection Diseases 0.000 description 1
- 101100232904 Homo sapiens IL2 gene Proteins 0.000 description 1
- 101150112617 IFNE gene Proteins 0.000 description 1
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
- 206010061598 Immunodeficiency Diseases 0.000 description 1
- 208000029462 Immunodeficiency disease Diseases 0.000 description 1
- 102000003996 Interferon-beta Human genes 0.000 description 1
- 102000008070 Interferon-gamma Human genes 0.000 description 1
- 108010074328 Interferon-gamma Proteins 0.000 description 1
- 108010002352 Interleukin-1 Proteins 0.000 description 1
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 1
- 102000003960 Ligases Human genes 0.000 description 1
- 108090000364 Ligases Proteins 0.000 description 1
- 102000004083 Lymphotoxin-alpha Human genes 0.000 description 1
- 108090000542 Lymphotoxin-alpha Proteins 0.000 description 1
- 208000031888 Mycoses Diseases 0.000 description 1
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 1
- 229910017974 NH40H Inorganic materials 0.000 description 1
- 208000030852 Parasitic disease Diseases 0.000 description 1
- 241000364057 Peoria Species 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 208000010362 Protozoan Infections Diseases 0.000 description 1
- 241000589516 Pseudomonas Species 0.000 description 1
- 108010092799 RNA-directed DNA polymerase Proteins 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 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
- NSOXQYCFHDMMGV-UHFFFAOYSA-N Tetrakis(2-hydroxypropyl)ethylenediamine Chemical compound CC(O)CN(CC(C)O)CCN(CC(C)O)CC(C)O NSOXQYCFHDMMGV-UHFFFAOYSA-N 0.000 description 1
- JZRWCGZRTZMZEH-UHFFFAOYSA-N Thiamine Natural products CC1=C(CCO)SC=[N+]1CC1=CN=C(C)N=C1N JZRWCGZRTZMZEH-UHFFFAOYSA-N 0.000 description 1
- 108060008682 Tumor Necrosis Factor Proteins 0.000 description 1
- 241000269368 Xenopus laevis Species 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 229960000583 acetic acid Drugs 0.000 description 1
- PAAZCQANMCYGAW-UHFFFAOYSA-N acetic acid;2,2,2-trifluoroacetic acid Chemical compound CC(O)=O.OC(=O)C(F)(F)F PAAZCQANMCYGAW-UHFFFAOYSA-N 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 239000002671 adjuvant Substances 0.000 description 1
- 150000001412 amines Chemical class 0.000 description 1
- 230000003321 amplification Effects 0.000 description 1
- 210000004102 animal cell Anatomy 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 239000008346 aqueous phase Substances 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 229940097012 bacillus thuringiensis Drugs 0.000 description 1
- 208000022362 bacterial infectious disease Diseases 0.000 description 1
- 230000000903 blocking effect Effects 0.000 description 1
- 238000006664 bond formation reaction Methods 0.000 description 1
- UDSAIICHUKSCKT-UHFFFAOYSA-N bromophenol blue Chemical compound C1=C(Br)C(O)=C(Br)C=C1C1(C=2C=C(Br)C(O)=C(Br)C=2)C2=CC=CC=C2S(=O)(=O)O1 UDSAIICHUKSCKT-UHFFFAOYSA-N 0.000 description 1
- 239000006285 cell suspension Substances 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 239000003638 chemical reducing agent Substances 0.000 description 1
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 208000027618 chronic mucocutaneous candidiasis due to lymphokine deficiency Diseases 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- ARUVKPQLZAKDPS-UHFFFAOYSA-L copper(II) sulfate Chemical compound [Cu+2].[O-][S+2]([O-])([O-])[O-] ARUVKPQLZAKDPS-UHFFFAOYSA-L 0.000 description 1
- 229910000366 copper(II) sulfate Inorganic materials 0.000 description 1
- 239000012228 culture supernatant Substances 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- 238000005520 cutting process Methods 0.000 description 1
- 230000002559 cytogenic effect Effects 0.000 description 1
- 230000007423 decrease Effects 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 238000000151 deposition Methods 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 239000008121 dextrose Substances 0.000 description 1
- 238000003745 diagnosis Methods 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
- 230000008034 disappearance Effects 0.000 description 1
- 125000002228 disulfide group Chemical group 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 238000001035 drying Methods 0.000 description 1
- 230000008030 elimination Effects 0.000 description 1
- 238000003379 elimination reaction 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
- 210000003527 eukaryotic cell Anatomy 0.000 description 1
- 102000013165 exonuclease Human genes 0.000 description 1
- 239000013613 expression plasmid Substances 0.000 description 1
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 238000009472 formulation Methods 0.000 description 1
- 229940044627 gamma-interferon Drugs 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 239000012362 glacial acetic acid Substances 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 230000013595 glycosylation Effects 0.000 description 1
- 238000006206 glycosylation reaction Methods 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 102000055277 human IL2 Human genes 0.000 description 1
- 230000036737 immune function Effects 0.000 description 1
- 230000007813 immunodeficiency Effects 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 239000004615 ingredient Substances 0.000 description 1
- 229940047124 interferons Drugs 0.000 description 1
- 238000007918 intramuscular administration Methods 0.000 description 1
- 238000007912 intraperitoneal administration Methods 0.000 description 1
- 238000001990 intravenous administration Methods 0.000 description 1
- BAUYGSIQEAFULO-UHFFFAOYSA-L iron(2+) sulfate (anhydrous) Chemical compound [Fe+2].[O-]S([O-])(=O)=O BAUYGSIQEAFULO-UHFFFAOYSA-L 0.000 description 1
- 229910000359 iron(II) sulfate Inorganic materials 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 239000006166 lysate Substances 0.000 description 1
- 229920002521 macromolecule Polymers 0.000 description 1
- 229910052943 magnesium sulfate Inorganic materials 0.000 description 1
- 235000019341 magnesium sulphate Nutrition 0.000 description 1
- 238000013507 mapping Methods 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- NSDFGJHUGMTLFI-UHFFFAOYSA-N methylaminomethanol tetrahydrochloride Chemical compound Cl.Cl.Cl.Cl.CNCO NSDFGJHUGMTLFI-UHFFFAOYSA-N 0.000 description 1
- 239000013586 microbial product Substances 0.000 description 1
- 238000013508 migration Methods 0.000 description 1
- 230000005012 migration Effects 0.000 description 1
- 239000007758 minimum essential medium Substances 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 238000012544 monitoring process Methods 0.000 description 1
- 210000000822 natural killer cell Anatomy 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 238000003199 nucleic acid amplification method Methods 0.000 description 1
- 238000011275 oncology therapy Methods 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 210000001672 ovary Anatomy 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000010979 pH adjustment Methods 0.000 description 1
- 230000003071 parasitic effect Effects 0.000 description 1
- VLTRZXGMWDSKGL-UHFFFAOYSA-M perchlorate Inorganic materials [O-]Cl(=O)(=O)=O VLTRZXGMWDSKGL-UHFFFAOYSA-M 0.000 description 1
- VLTRZXGMWDSKGL-UHFFFAOYSA-N perchloric acid Chemical compound OCl(=O)(=O)=O VLTRZXGMWDSKGL-UHFFFAOYSA-N 0.000 description 1
- 239000012071 phase Substances 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 229920001184 polypeptide Polymers 0.000 description 1
- 239000002244 precipitate Substances 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 102000004196 processed proteins & peptides Human genes 0.000 description 1
- 108090000765 processed proteins & peptides Proteins 0.000 description 1
- 230000001737 promoting effect Effects 0.000 description 1
- 238000000163 radioactive labelling Methods 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 239000013643 reference control Substances 0.000 description 1
- 238000010405 reoxidation reaction Methods 0.000 description 1
- 239000011347 resin Substances 0.000 description 1
- 229920005989 resin Polymers 0.000 description 1
- 238000012552 review Methods 0.000 description 1
- 238000013207 serial dilution Methods 0.000 description 1
- 150000003355 serines Chemical class 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 239000001632 sodium acetate Substances 0.000 description 1
- 235000017281 sodium acetate Nutrition 0.000 description 1
- 239000007974 sodium acetate buffer Substances 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 238000005063 solubilization Methods 0.000 description 1
- 230000007928 solubilization Effects 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- LXMSZDCAJNLERA-ZHYRCANASA-N spironolactone Chemical compound C([C@@H]1[C@]2(C)CC[C@@H]3[C@@]4(C)CCC(=O)C=C4C[C@H]([C@@H]13)SC(=O)C)C[C@@]21CCC(=O)O1 LXMSZDCAJNLERA-ZHYRCANASA-N 0.000 description 1
- 230000006641 stabilisation Effects 0.000 description 1
- 238000011105 stabilization Methods 0.000 description 1
- 230000004936 stimulating effect Effects 0.000 description 1
- 208000003265 stomatitis Diseases 0.000 description 1
- 238000007920 subcutaneous administration Methods 0.000 description 1
- 238000006467 substitution reaction Methods 0.000 description 1
- 239000005720 sucrose Substances 0.000 description 1
- 229940124597 therapeutic agent Drugs 0.000 description 1
- 238000002560 therapeutic procedure Methods 0.000 description 1
- KYMBYSLLVAOCFI-UHFFFAOYSA-N thiamine Chemical compound CC1=C(CCO)SCN1CC1=CN=C(C)N=C1N KYMBYSLLVAOCFI-UHFFFAOYSA-N 0.000 description 1
- 235000019157 thiamine Nutrition 0.000 description 1
- 229960003495 thiamine Drugs 0.000 description 1
- 239000011721 thiamine Substances 0.000 description 1
- 230000000699 topical effect Effects 0.000 description 1
- 239000001226 triphosphate Substances 0.000 description 1
- 235000011178 triphosphate Nutrition 0.000 description 1
- 125000002264 triphosphate group Chemical class [H]OP(=O)(O[H])OP(=O)(O[H])OP(=O)(O[H])O* 0.000 description 1
- SOBHUZYZLFQYFK-UHFFFAOYSA-K trisodium;hydroxy-[[phosphonatomethyl(phosphonomethyl)amino]methyl]phosphinate Chemical compound [Na+].[Na+].[Na+].OP(O)(=O)CN(CP(O)([O-])=O)CP([O-])([O-])=O SOBHUZYZLFQYFK-UHFFFAOYSA-K 0.000 description 1
- 102000003390 tumor necrosis factor Human genes 0.000 description 1
- 238000002604 ultrasonography Methods 0.000 description 1
- 208000005925 vesicular stomatitis Diseases 0.000 description 1
- 230000009385 viral infection Effects 0.000 description 1
- 238000012800 visualization Methods 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
-
- 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
- C07K14/52—Cytokines; Lymphokines; Interferons
- C07K14/54—Interleukins [IL]
- C07K14/55—IL-2
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/12—Antivirals
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
-
- 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
- C07K14/52—Cytokines; Lymphokines; Interferons
- C07K14/555—Interferons [IFN]
- C07K14/565—IFN-beta
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/10—Processes for the isolation, preparation or purification of DNA or RNA
- C12N15/102—Mutagenizing nucleic acids
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S530/00—Chemistry: natural resins or derivatives; peptides or proteins; lignins or reaction products thereof
- Y10S530/808—Materials and products related to genetic engineering or hybrid or fused cell technology, e.g. hybridoma, monoclonal products
- Y10S530/809—Fused cells, e.g. hybridoma
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S930/00—Peptide or protein sequence
- Y10S930/01—Peptide or protein sequence
- Y10S930/14—Lymphokine; related peptides
- Y10S930/141—Interleukin
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S930/00—Peptide or protein sequence
- Y10S930/01—Peptide or protein sequence
- Y10S930/14—Lymphokine; related peptides
- Y10S930/142—Interferon
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Genetics & Genomics (AREA)
- Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Zoology (AREA)
- Medicinal Chemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biomedical Technology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- General Engineering & Computer Science (AREA)
- Molecular Biology (AREA)
- Wood Science & Technology (AREA)
- Biotechnology (AREA)
- Pharmacology & Pharmacy (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Animal Behavior & Ethology (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Microbiology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Gastroenterology & Hepatology (AREA)
- Toxicology (AREA)
- Plant Pathology (AREA)
- Physics & Mathematics (AREA)
- Virology (AREA)
- Oncology (AREA)
- Communicable Diseases (AREA)
- Crystallography & Structural Chemistry (AREA)
- Immunology (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US43515482A | 1982-10-19 | 1982-10-19 | |
| US48616283A | 1983-04-15 | 1983-04-15 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| BE898016A true BE898016A (fr) | 1984-02-15 |
Family
ID=27030446
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| BE0/211722A BE898016A (fr) | 1982-10-19 | 1983-10-18 | Muteines appauvries en cysteine provenant de proteines biologiquement actives. |
Country Status (23)
| Country | Link |
|---|---|
| EP (4) | EP0192811B1 (cg-RX-API-DMAC7.html) |
| JP (2) | JPS6128392A (cg-RX-API-DMAC7.html) |
| KR (1) | KR910009900B1 (cg-RX-API-DMAC7.html) |
| AT (4) | ATE73493T1 (cg-RX-API-DMAC7.html) |
| AU (1) | AU563962B2 (cg-RX-API-DMAC7.html) |
| BE (1) | BE898016A (cg-RX-API-DMAC7.html) |
| CA (1) | CA1340861C (cg-RX-API-DMAC7.html) |
| CH (1) | CH669395A5 (cg-RX-API-DMAC7.html) |
| DE (4) | DE3376271D1 (cg-RX-API-DMAC7.html) |
| DK (2) | DK168767B1 (cg-RX-API-DMAC7.html) |
| ES (4) | ES526541A0 (cg-RX-API-DMAC7.html) |
| FI (1) | FI82266C (cg-RX-API-DMAC7.html) |
| FR (1) | FR2534594B1 (cg-RX-API-DMAC7.html) |
| GB (1) | GB2130219B (cg-RX-API-DMAC7.html) |
| GR (1) | GR79408B (cg-RX-API-DMAC7.html) |
| IE (1) | IE56026B1 (cg-RX-API-DMAC7.html) |
| IL (1) | IL69970A (cg-RX-API-DMAC7.html) |
| LU (3) | LU88761I2 (cg-RX-API-DMAC7.html) |
| NL (2) | NL930119I2 (cg-RX-API-DMAC7.html) |
| NO (1) | NO173740C (cg-RX-API-DMAC7.html) |
| NZ (1) | NZ205922A (cg-RX-API-DMAC7.html) |
| PH (2) | PH20343A (cg-RX-API-DMAC7.html) |
| PT (1) | PT77512B (cg-RX-API-DMAC7.html) |
Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1985004328A1 (en) | 1984-03-28 | 1985-10-10 | Cetus Corporation | Pharmaceutical compositions of microbially produced interleukin-2 |
| EP0174785A1 (en) | 1984-08-31 | 1986-03-19 | Cetus Corporation | A positive retroregulatory element, plasmid and cells comprising said element and their production, a method of enhancing gene expression using said element and a method of enhancing RNA half life using said element |
| EP0606673A3 (en) * | 1984-03-28 | 1995-01-25 | Cetus Oncology Corp | Controlled oxidation of microbially produced, cysteine-containing proteins. |
Families Citing this family (122)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| FI82266C (fi) * | 1982-10-19 | 1991-02-11 | Cetus Corp | Foerfarande foer framstaellning av il-2 -mutein. |
| DK265384A (da) * | 1983-06-01 | 1984-12-02 | Hoffmann La Roche | Polypeptider med interferonaktivitet |
| WO1985000817A1 (en) * | 1983-08-10 | 1985-02-28 | Amgen | Microbial expression of interleukin ii |
| GB8334102D0 (en) * | 1983-12-21 | 1984-02-01 | Searle & Co | Interferons with cysteine pattern |
| EP0163603B1 (en) * | 1984-05-08 | 1989-12-13 | Genetics Institute, Inc. | A human t-cell growth factor |
| GB8412564D0 (en) * | 1984-05-17 | 1984-06-20 | Searle & Co | Structure and properties |
| US5683688A (en) * | 1984-05-31 | 1997-11-04 | Genentech, Inc. | Unglycosylated recombinant human lymphotoxin polypeptides and compositions |
| NZ212207A (en) * | 1984-05-31 | 1991-07-26 | Genentech Inc | Recombinant lymphotoxin |
| US5672347A (en) * | 1984-07-05 | 1997-09-30 | Genentech, Inc. | Tumor necrosis factor antagonists and their use |
| WO1986002068A1 (fr) * | 1984-09-26 | 1986-04-10 | Takeda Chemical Industries, Ltd. | Separation mutuelle de proteines |
| IL76360A0 (en) | 1984-09-26 | 1986-01-31 | Takeda Chemical Industries Ltd | Mutual separation of proteins |
| US4857316A (en) * | 1984-10-03 | 1989-08-15 | Syntex (U.S.A.) Inc. | Synergistic antiviral composition |
| US4606917A (en) * | 1984-10-03 | 1986-08-19 | Syntex (U.S.A) Inc. | Synergistic antiviral composition |
| US4959314A (en) | 1984-11-09 | 1990-09-25 | Cetus Corporation | Cysteine-depleted muteins of biologically active proteins |
| US4572798A (en) * | 1984-12-06 | 1986-02-25 | Cetus Corporation | Method for promoting disulfide bond formation in recombinant proteins |
| US6107465A (en) * | 1984-12-21 | 2000-08-22 | Otsuka Pharmaceutical Co., Ltd. | IL-1β and derivatives thereof and drugs |
| US5342614A (en) * | 1984-12-21 | 1994-08-30 | Otsuka Pharmaceutical Co., Ltd. | Method of treating arthritus or inflammation with IL-1β or derivatives thereof |
| DK172052B1 (da) * | 1984-12-21 | 1997-09-29 | Otsuka Pharma Co Ltd | Antitumor-aktivt stof, fremgangsmåde til dets fremstilling, lægemiddel indeholdende stoffet, gen kodende for stoffet, vektor indeholdende genet samt rekombinant mikroorganisme transformet med en sådan vektor |
| DE3500681A1 (de) * | 1985-01-11 | 1986-07-17 | Hoechst Ag, 6230 Frankfurt | Verfahren zur isolierung und reinigung von lymphokinen |
| US4863849A (en) * | 1985-07-18 | 1989-09-05 | New York Medical College | Automatable process for sequencing nucleotide |
| US4810643A (en) * | 1985-08-23 | 1989-03-07 | Kirin- Amgen Inc. | Production of pluripotent granulocyte colony-stimulating factor |
| US6004548A (en) | 1985-08-23 | 1999-12-21 | Amgen, Inc. | Analogs of pluripotent granulocyte colony-stimulating factor |
| CA1297003C (en) * | 1985-09-20 | 1992-03-10 | Jack H. Nunberg | Composition and method for treating animals |
| US5359035A (en) * | 1985-12-21 | 1994-10-25 | Hoechst Aktiengesellschaft | Bifunctional proteins including interleukin-2 (IL-2) and granuloctyte macrophage colony stimulating factor (GM-CSF) |
| US5008374A (en) * | 1986-03-14 | 1991-04-16 | Otsuka Pharmaceutical Co., Ltd. | IL-1α derivatives and drugs |
| AU595864B2 (en) * | 1986-03-14 | 1990-04-12 | Otsuka Pharmaceutical Co., Ltd. | Il-1 alpha derivatives and drugs |
| ATE72582T1 (de) * | 1986-09-05 | 1992-02-15 | Cetus Corp | Oxidationsresistente muteine von beta-interferon, deren herstellung und diese muteine enthaltende praeparate. |
| JP2526965B2 (ja) * | 1987-02-24 | 1996-08-21 | 武田薬品工業株式会社 | ムテイン，ｄｎａおよびその用途 |
| US4987070A (en) * | 1987-03-04 | 1991-01-22 | Suntory Limited | Use of a 97 amino acid leader sequence from the E. coli B-galactosidase gene for the production of hanp and hptc as fusion proteins |
| AU629176B2 (en) * | 1987-07-07 | 1992-10-01 | Scios Nova Inc. | Recombinant fibroblast growth factors |
| AU625394B2 (en) * | 1987-11-04 | 1992-07-09 | Byk Gulden Lomberg Chemische Fabrik Gmbh | Alveolar surfactant proteins |
| DE68929273T2 (de) * | 1988-08-24 | 2001-07-05 | American Cyanamid Co., Wayne | Stabilisierung von Somatotropinen durch Modifikation von Cystein-Resten durch orts-spezifische Mutagenese oder chemische Derivatisierung |
| US5079230A (en) * | 1988-09-12 | 1992-01-07 | Pitman-Moore, Inc. | Stable bioactive somatotropins |
| CA2003886A1 (en) * | 1988-12-16 | 1990-06-16 | Anthony F. Purchio | Cloning and expression of simian transforming growth factor-beta 1 |
| EP0456642A1 (en) * | 1989-01-31 | 1991-11-21 | The Upjohn Company | Somatotropin analogs |
| ATE133993T1 (de) * | 1989-02-17 | 1996-02-15 | Merck & Co Inc | Protein-antikrebsmittel |
| US5621078A (en) * | 1989-03-22 | 1997-04-15 | Merck & Co., Inc. | Modified pseudomonas exotoxin PE40 |
| AU5355790A (en) * | 1989-04-19 | 1990-11-16 | Cetus Corporation | Multifunctional m-csf proteins and genes encoding therefor |
| US6207798B1 (en) | 1989-08-03 | 2001-03-27 | Merck & Co., Inc. | Modified PE40 toxin fusion proteins |
| US5173297A (en) * | 1991-07-01 | 1992-12-22 | Quest International Flavors & Food Ingredients Company Division Of Indopco, Inc. | Bacteriocin from lactococcus lactis subspecies lactis |
| IL98528A0 (en) * | 1990-06-21 | 1992-07-15 | Merck & Co Inc | Pharmaceutical compositions containing hybrid for killing bladder cancer cells |
| FR2671554A1 (fr) * | 1991-01-11 | 1992-07-17 | Clonatec Sa | Peptides synthetiques derivant de l'antigene hbc du virus de l'hepatite b, leurs applications a la detection d'une infection par ce virus et a la vaccination contre l'hepatite b. |
| FR2686899B1 (fr) | 1992-01-31 | 1995-09-01 | Rhone Poulenc Rorer Sa | Nouveaux polypeptides biologiquement actifs, leur preparation et compositions pharmaceutiques les contenant. |
| US5545723A (en) * | 1994-03-15 | 1996-08-13 | Biogen Inc. | Muteins of IFN-β |
| US5814485A (en) * | 1995-06-06 | 1998-09-29 | Chiron Corporation | Production of interferon-β (IFN-β) in E. coli |
| DE19544167A1 (de) * | 1995-11-17 | 1997-05-22 | Schering Ag | Verwendung von Interferon-ß zur Behandlung von Bronchialkarzinom bei Bestrahlungstherapie |
| AU6399996A (en) * | 1996-06-19 | 1998-01-07 | Chiron Corporation | Bacterial production of interferon-beta using low levels of sodium and potassium ions |
| CN1100875C (zh) * | 1998-03-06 | 2003-02-05 | 上海华晨生物技术研究所 | 新型重组人白细胞介素2的制备方法及其表达载体和工程菌 |
| EP1983055A1 (en) | 2000-04-12 | 2008-10-22 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| EP1935431A3 (en) | 2000-05-15 | 2008-08-13 | Health Research, Inc. | Cancer treatments by using a combination of an antibody against her2 and interleukin-2 |
| DE10112825A1 (de) | 2001-03-16 | 2002-10-02 | Fresenius Kabi De Gmbh | HESylierung von Wirkstoffen in wässriger Lösung |
| US6887462B2 (en) | 2001-04-09 | 2005-05-03 | Chiron Corporation | HSA-free formulations of interferon-beta |
| AU2002326991A1 (en) * | 2001-09-18 | 2003-04-01 | Chiron Corporation | Methods for treating multiple sclerosis |
| KR100511749B1 (ko) * | 2001-11-06 | 2005-09-02 | 선바이오(주) | 변형된 인터페론-베타, 및 이의 화학적으로 변형된 배합체 |
| EP2261250B1 (en) | 2001-12-21 | 2015-07-01 | Human Genome Sciences, Inc. | GCSF-Albumin fusion proteins |
| WO2005003296A2 (en) | 2003-01-22 | 2005-01-13 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| DE10209822A1 (de) | 2002-03-06 | 2003-09-25 | Biotechnologie Ges Mittelhesse | Kopplung niedermolekularer Substanzen an ein modifiziertes Polysaccharid |
| DE10209821A1 (de) | 2002-03-06 | 2003-09-25 | Biotechnologie Ges Mittelhesse | Kopplung von Proteinen an ein modifiziertes Polysaccharid |
| CA2496317C (en) | 2002-09-11 | 2014-02-18 | Fresenius Kabi Deutschland Gmbh | Method of producing hydroxyalkyl starch derivatives |
| US7538092B2 (en) | 2002-10-08 | 2009-05-26 | Fresenius Kabi Deutschland Gmbh | Pharmaceutically active oligosaccharide conjugates |
| WO2005014655A2 (en) | 2003-08-08 | 2005-02-17 | Fresenius Kabi Deutschland Gmbh | Conjugates of hydroxyalkyl starch and a protein |
| WO2005044294A2 (en) | 2003-11-04 | 2005-05-19 | Chiron Corporation | Method of therapy for cancers expressing the cd40 antigen |
| JP2007527242A (ja) * | 2004-03-05 | 2007-09-27 | カイロン コーポレーション | 治療剤の患者耐容性を予測するためのインビトロ試験システム |
| BRPI0508607A (pt) | 2004-03-11 | 2007-07-31 | Fresenius Kabi De Gmbh | conjugados de amido de hidroxialquila e uma proteìna, preparados pela aminação redutiva |
| US7642072B2 (en) * | 2004-07-26 | 2010-01-05 | Enzon Pharmaceuticals, Inc. | Optimized interferon-beta gene |
| GB0523282D0 (en) | 2005-11-15 | 2005-12-21 | Isis Innovation | Methods using pores |
| GB2453377A (en) | 2007-10-05 | 2009-04-08 | Isis Innovation | Transmembrane protein pores and molecular adapters therefore. |
| EP2070950A1 (en) | 2007-12-14 | 2009-06-17 | Fresenius Kabi Deutschland GmbH | Hydroxyalkyl starch derivatives and process for their preparation |
| ATE548052T1 (de) | 2008-01-17 | 2012-03-15 | Philogen Spa | Kombination aus einem anti-edb-fibronectin- antikörper-il-2-fusionsprotein und einem b-zellen bindenden molekül, b-zellen-vorläufern und/oder deren krebserregendem gegenspieler |
| US20110229877A1 (en) | 2008-07-07 | 2011-09-22 | Oxford Nanopore Technologies Limited | Enzyme-pore constructs |
| WO2010004273A1 (en) | 2008-07-07 | 2010-01-14 | Oxford Nanopore Technologies Limited | Base-detecting pore |
| US9077937B2 (en) * | 2008-11-06 | 2015-07-07 | Alcatel Lucent | Method and apparatus for fast channel change |
| GB0820927D0 (en) | 2008-11-14 | 2008-12-24 | Isis Innovation | Method |
| KR101797773B1 (ko) | 2009-01-30 | 2017-11-15 | 옥스포드 나노포어 테크놀로지즈 리미티드 | 막횡단 시퀀싱에서 핵산 구축물용 어댑터 |
| CN102482330A (zh) | 2009-01-30 | 2012-05-30 | 牛津纳米孔技术有限公司 | 酶突变体 |
| GB0905140D0 (en) | 2009-03-25 | 2009-05-06 | Isis Innovation | Method |
| AU2012215135B9 (en) | 2011-02-11 | 2017-03-09 | Oxford Nanopore Technologies Limited | Mutant pores |
| AU2012228418B2 (en) | 2011-03-11 | 2016-09-29 | Assistance Publique - Hopitaux De Paris | Use of low dose IL-2 for treating autoimmune - related or inflammatory disorders |
| CA2843136C (en) | 2011-07-25 | 2020-12-29 | Oxford Nanopore Technologies Limited | Hairpin loop method for double strand polynucleotide sequencing using transmembrane pores |
| GB201119244D0 (en) | 2011-11-08 | 2011-12-21 | British American Tobacco Co | Smoking article |
| KR102083695B1 (ko) | 2012-04-10 | 2020-03-02 | 옥스포드 나노포어 테크놀로지즈 리미티드 | 돌연변이체 리세닌 기공 |
| US11155860B2 (en) | 2012-07-19 | 2021-10-26 | Oxford Nanopore Technologies Ltd. | SSB method |
| SG11201507138RA (en) | 2013-03-08 | 2015-10-29 | Oxford Nanopore Tech Ltd | Enzyme stalling method |
| GB201314695D0 (en) | 2013-08-16 | 2013-10-02 | Oxford Nanopore Tech Ltd | Method |
| GB201313477D0 (en) | 2013-07-29 | 2013-09-11 | Univ Leuven Kath | Nanopore biosensors for detection of proteins and nucleic acids |
| WO2014206899A1 (en) | 2013-06-25 | 2014-12-31 | Icm (Institut Du Cerveau Et De La Moelle Épinière) | Boosting treg cells for treating alzheimer disease and related disorders |
| GB201403096D0 (en) | 2014-02-21 | 2014-04-09 | Oxford Nanopore Tech Ltd | Sample preparation method |
| EP2918285A1 (en) | 2014-03-11 | 2015-09-16 | Université Pierre et Marie Curie (Paris 6) | Interleukin-2 for treating food allergy |
| US10443097B2 (en) | 2014-05-02 | 2019-10-15 | Oxford Nanopore Technologies Ltd. | Method of improving the movement of a target polynucleotide with respect to a transmembrane pore |
| CN117164683A (zh) | 2014-09-01 | 2023-12-05 | 弗拉芒区生物技术研究所 | 突变csgg孔 |
| EP3204511B1 (en) | 2014-10-07 | 2021-07-28 | Oxford Nanopore Technologies Limited | Mutant pores |
| GB201418159D0 (en) | 2014-10-14 | 2014-11-26 | Oxford Nanopore Tech Ltd | Method |
| WO2016172445A2 (en) * | 2015-04-24 | 2016-10-27 | The University Of Florida Research Foundation, Inc. | Methods of identifying biologically active random peptides in plants and libraries of plants expressing candidate biologically active random peptides |
| US10876109B2 (en) | 2015-04-24 | 2020-12-29 | University Of Florida Research Foundation, Inc. | Methods of identifying biologically active random peptides in prokaryotic cells and libraries of prokaryotic cells expressing candidate biologically active random peptides |
| US10801023B2 (en) * | 2015-04-24 | 2020-10-13 | University Of Florida Research Foundation, Inc. | Methods of identifying biologically active random peptides in plants and libraries of plants expressing candidate biologically active random peptides |
| KR102740102B1 (ko) | 2015-10-22 | 2024-12-06 | 일투 파마 | Il-2의 약학 조성물 |
| GB201609220D0 (en) | 2016-05-25 | 2016-07-06 | Oxford Nanopore Tech Ltd | Method |
| AU2017281469B2 (en) | 2016-06-22 | 2023-08-31 | David Klatzmann | Genetically modified T lymphocytes |
| AU2018234810B2 (en) | 2017-03-15 | 2023-05-11 | Pandion Operations, Inc. | Targeted immunotolerance |
| SG11201909949XA (en) | 2017-05-24 | 2019-11-28 | Pandion Therapeutics Inc | Targeted immunotolerance |
| US10946068B2 (en) | 2017-12-06 | 2021-03-16 | Pandion Operations, Inc. | IL-2 muteins and uses thereof |
| US10174092B1 (en) | 2017-12-06 | 2019-01-08 | Pandion Therapeutics, Inc. | IL-2 muteins |
| USRE50550E1 (en) | 2017-12-06 | 2025-08-26 | Pandion Operations, Inc. | IL-2 muteins and uses thereof |
| US11534479B2 (en) | 2018-02-16 | 2022-12-27 | Iltoo Pharma | Use of interleukin 2 for treating Sjögren's syndrome |
| GB201807793D0 (en) | 2018-05-14 | 2018-06-27 | Oxford Nanopore Tech Ltd | Method |
| WO2019241315A1 (en) | 2018-06-12 | 2019-12-19 | Obsidian Therapeutics, Inc. | Pde5 derived regulatory constructs and methods of use in immunotherapy |
| WO2020007937A1 (en) | 2018-07-03 | 2020-01-09 | Iltoo Pharma | Use of interleukin-2 for treating systemic sclerosis |
| EP3836954B1 (en) | 2018-08-13 | 2025-05-07 | Iltoo Pharma | Combination of interleukin-2 with an interleukin 1 inhibitor, conjugates and therapeutic uses thereof |
| EP3880838B1 (en) | 2018-11-15 | 2024-12-25 | The Board of Trustees of the Leland Stanford Junior University | Compositions and methods of prognosis and classification for preeclampsia |
| KR20220035333A (ko) | 2019-05-20 | 2022-03-22 | 팬디온 오퍼레이션스, 인코포레이티드 | Madcam 표적 면역관용 |
| WO2021116444A1 (en) | 2019-12-12 | 2021-06-17 | Iltoo Pharma | Interleukin 2 chimeric constructs |
| US11981715B2 (en) | 2020-02-21 | 2024-05-14 | Pandion Operations, Inc. | Tissue targeted immunotolerance with a CD39 effector |
| AU2021230103A1 (en) | 2020-03-06 | 2022-09-22 | Assistance Publique - Hopitaux De Paris | Low dose human interleukin-2 for the treatment of amyotrophic lateral sclerosis |
| CN116075523A (zh) * | 2020-04-29 | 2023-05-05 | 基因制药株式会社 | 具有融合的干扰素-β突变蛋白和抗体的重组蛋白以及包含其的药物组合物 |
| BR112022022035A2 (pt) * | 2020-04-29 | 2023-01-03 | Abion Inc | Interferon-beta humano variante, polinucleotídeo, vetor de expressão, célula animal transformada, métodos para preparar um interferon-beta humano variante, melhorar a estabilidade de um interferon-beta r27t humano variante e tratar uma doença, composição farmacêutica e uso |
| KR20230092880A (ko) * | 2020-08-28 | 2023-06-26 | 조인트 스탁 컴퍼니 "바이오케드" | AAV5-기반의 SARS-CoV-2 백신 |
| CA3233644A1 (en) | 2021-10-06 | 2023-04-13 | David Klatzmann | Interleukin 2 chimeric constructs with targeting specificy to inflamed tissues |
| WO2023226873A1 (en) * | 2022-05-24 | 2023-11-30 | Jhm Biopharmaceutical (Hangzhou) Co., Ltd. | Recombinant botulinum neurotoxin of type a and preparation method thereof |
| WO2023245097A2 (en) | 2022-06-16 | 2023-12-21 | Cephalon Llc | Anti-pd-1 antibody-attenuated il-2 immunoconjugates and uses thereof |
| AU2022477937A1 (en) | 2022-09-12 | 2025-04-10 | Assistance Publique - Hôpitaux De Paris | Interleukin-2 for use in treating autism spectrum disorder |
| EP4630035A1 (en) | 2022-12-05 | 2025-10-15 | Centre Hospitalier Universitaire de Nimes | Low dose human interleukin-2 for the treatment of amyotrophic lateral sclerosis in a subgroup of patients |
| WO2025032158A1 (en) | 2023-08-08 | 2025-02-13 | Institut National de la Santé et de la Recherche Médicale | Method to treat tauopathies |
Family Cites Families (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS5359688A (en) * | 1976-11-11 | 1978-05-29 | Tanpakushitsu Kenkiyuu Shiyour | Production of novel polypeptide |
| US4399216A (en) * | 1980-02-25 | 1983-08-16 | The Trustees Of Columbia University | Processes for inserting DNA into eucaryotic cells and for producing proteinaceous materials |
| NO811118L (no) * | 1980-04-03 | 1981-10-05 | Biogen Nv | Dna-sekvenser, rekombinante dna-molekyler og fremgangsmaate ved fremstilling av polypeptider |
| JPS58110548A (ja) * | 1981-12-24 | 1983-07-01 | Asahi Chem Ind Co Ltd | 新規な生理活性ペプチド |
| US6936694B1 (en) * | 1982-05-06 | 2005-08-30 | Intermune, Inc. | Manufacture and expression of large structural genes |
| FI82266C (fi) * | 1982-10-19 | 1991-02-11 | Cetus Corp | Foerfarande foer framstaellning av il-2 -mutein. |
| DK265384A (da) * | 1983-06-01 | 1984-12-02 | Hoffmann La Roche | Polypeptider med interferonaktivitet |
| WO1985000817A1 (en) * | 1983-08-10 | 1985-02-28 | Amgen | Microbial expression of interleukin ii |
| US4959314A (en) * | 1984-11-09 | 1990-09-25 | Cetus Corporation | Cysteine-depleted muteins of biologically active proteins |
-
1983
- 1983-10-10 FI FI833681A patent/FI82266C/fi not_active IP Right Cessation
- 1983-10-10 IE IE2380/83A patent/IE56026B1/en active Protection Beyond IP Right Term
- 1983-10-11 NZ NZ205922A patent/NZ205922A/en unknown
- 1983-10-12 AU AU20086/83A patent/AU563962B2/en not_active Expired
- 1983-10-12 PH PH29685A patent/PH20343A/en unknown
- 1983-10-12 CA CA000438878A patent/CA1340861C/en not_active Expired - Lifetime
- 1983-10-13 EP EP85109295A patent/EP0192811B1/en not_active Expired - Lifetime
- 1983-10-13 GB GB08327490A patent/GB2130219B/en not_active Expired
- 1983-10-13 LU LU88761C patent/LU88761I2/fr unknown
- 1983-10-13 EP EP87103350A patent/EP0234599B1/en not_active Expired - Lifetime
- 1983-10-13 DE DE8383306221T patent/DE3376271D1/de not_active Expired
- 1983-10-13 DE DE8686110595T patent/DE3380598D1/de not_active Expired
- 1983-10-13 AT AT87103350T patent/ATE73493T1/de not_active IP Right Cessation
- 1983-10-13 AT AT86110595T patent/ATE46539T1/de active
- 1983-10-13 DE DE8787103350T patent/DE3382528D1/de not_active Expired - Lifetime
- 1983-10-13 DE DE8585109295T patent/DE3382197D1/de not_active Expired - Lifetime
- 1983-10-13 EP EP83306221A patent/EP0109748B1/en not_active Expired
- 1983-10-13 AT AT83306221T patent/ATE33503T1/de not_active IP Right Cessation
- 1983-10-13 AT AT85109295T patent/ATE61407T1/de not_active IP Right Cessation
- 1983-10-13 EP EP86110595A patent/EP0218825B1/en not_active Expired
- 1983-10-14 IL IL69970A patent/IL69970A/xx not_active IP Right Cessation
- 1983-10-17 PT PT77512A patent/PT77512B/pt unknown
- 1983-10-17 GR GR72712A patent/GR79408B/el unknown
- 1983-10-18 BE BE0/211722A patent/BE898016A/fr not_active IP Right Cessation
- 1983-10-18 CH CH5667/83A patent/CH669395A5/fr not_active IP Right Cessation
- 1983-10-18 NO NO833793A patent/NO173740C/no not_active IP Right Cessation
- 1983-10-18 ES ES526541A patent/ES526541A0/es active Granted
- 1983-10-18 KR KR1019830004927A patent/KR910009900B1/ko not_active Expired
- 1983-10-18 FR FR8316543A patent/FR2534594B1/fr not_active Expired
- 1983-10-19 DK DK481383A patent/DK168767B1/da not_active IP Right Cessation
-
1984
- 1984-06-01 ES ES533054A patent/ES8506801A1/es not_active Expired
- 1984-06-01 ES ES533053A patent/ES533053A0/es active Granted
- 1984-09-08 JP JP18730184A patent/JPS6128392A/ja active Granted
-
1985
- 1985-05-03 ES ES542829A patent/ES8608043A1/es not_active Expired
-
1986
- 1986-03-13 PH PH33519A patent/PH23702A/en unknown
-
1988
- 1988-03-14 JP JP63058544A patent/JPS6420096A/ja active Pending
-
1992
- 1992-08-26 DK DK105892A patent/DK171681B1/da not_active IP Right Cessation
-
1993
- 1993-06-30 NL NL930119C patent/NL930119I2/nl unknown
- 1993-07-01 LU LU88357C patent/LU88357I2/fr unknown
-
1996
- 1996-05-29 NL NL960013C patent/NL960013I2/nl unknown
-
1999
- 1999-07-07 LU LU90413C patent/LU90413I2/fr unknown
Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1985004328A1 (en) | 1984-03-28 | 1985-10-10 | Cetus Corporation | Pharmaceutical compositions of microbially produced interleukin-2 |
| EP0606673A3 (en) * | 1984-03-28 | 1995-01-25 | Cetus Oncology Corp | Controlled oxidation of microbially produced, cysteine-containing proteins. |
| EP0174785A1 (en) | 1984-08-31 | 1986-03-19 | Cetus Corporation | A positive retroregulatory element, plasmid and cells comprising said element and their production, a method of enhancing gene expression using said element and a method of enhancing RNA half life using said element |
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| BE898016A (fr) | Muteines appauvries en cysteine provenant de proteines biologiquement actives. | |
| DE3687763T2 (de) | Oxidationsbestaendige il-2-muteine und ihre herstellung, diese muteine enthaltende zusammensetzungen, solche muteine kodierende dns-sequenzen und expressionsvektoren und korrespondierende transformierte wirtzellen. | |
| US4853332A (en) | Structural genes, plasmids and transformed cells for producing cysteine depleted muteins of biologically active proteins | |
| US4588585A (en) | Human recombinant cysteine depleted interferon-β muteins | |
| US4518584A (en) | Human recombinant interleukin-2 muteins | |
| US5116943A (en) | Oxidation-resistant muteins of Il-2 and other protein | |
| US4752585A (en) | Oxidation-resistant muteins | |
| MC1424A1 (fr) | Interferons de leucocytes humains hybrides et procede pour leur preparation microbiologique | |
| FR2514783A1 (fr) | Interferon immunitaire humain | |
| FR2486098A1 (fr) | Interferons et procede pour leur preparation | |
| NL8104400A (nl) | Microbiele bereiding van menselijk fibroblast interferon. | |
| CH672790A5 (cg-RX-API-DMAC7.html) | ||
| JP3217698B2 (ja) | 成熟ヒト インターロイキン１タンパク質 | |
| JPS6128393A (ja) | 変形されたインターロイキン―２をコードするｄｎａ、このｄｎａを含有するプラスミド及びこのプラスミドにより形質転換された大腸菌 | |
| JPH0229317B2 (cg-RX-API-DMAC7.html) | ||
| EP0260350B1 (en) | Oxidation-resistant interferon-beta muteins and their production; formulations containing such muteins | |
| CH669394A5 (en) | Synthetic protein analogues lacking cysteine residues | |
| FI87233B (fi) | Gen vilken kodar en mutein. | |
| BG60510B2 (bg) | Структурни гени,плазмиди и трансформирани клетки за получаване на бедни на цистеин мутеини на биологично активни протеини | |
| JPH01165399A (ja) | 組換えヒトインターロイキン２およびその製造法 | |
| NO306951B1 (no) | DNA-sekvens som koder for et modifisert human-IFM-(beta) samt fremgangsmåte for fremstilling derav |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| CCPA | Application for a supplementary protection certificate |
Free format text: 093C0180 |
|
| CCPV | Grant of a supplementary protection certificate |
Free format text: 093C0180, EXPIRES 20040703 |
|
| RE20 | Patent expired |
Owner name: *CHIRON CORP. Effective date: 20031018 |
|
| CCRE | Expiry of a supplementary protection certificate |
Free format text: PRODUCT NAME: DES-ALANYL-1, SERINE-125, HUMAAN INTERLEUKINE-2 (RECOMBINANTD INTERLEUKINE-2); NAT. REGISTRATION NO/DATE: 3001 IE 1 F 0 / 19900406; FIRST REGISTRATION: DK 6793 19890703 Spc suppl protection certif: 93C0180 Filing date: 19930701 Expiry date: 20031018 Extension date: 20040703 |