DD267739A5 - Verfahren zur Herstellung eines zu Hefe heterologen Poly-Peptids - Google Patents
Verfahren zur Herstellung eines zu Hefe heterologen Poly-Peptids Download PDFInfo
- Publication number
- DD267739A5 DD267739A5 DD31325586A DD31325586A DD267739A5 DD 267739 A5 DD267739 A5 DD 267739A5 DD 31325586 A DD31325586 A DD 31325586A DD 31325586 A DD31325586 A DD 31325586A DD 267739 A5 DD267739 A5 DD 267739A5
- Authority
- DD
- German Democratic Republic
- Prior art keywords
- yeast
- dna
- promoter
- hybrid
- gene
- Prior art date
Links
- 240000004808 Saccharomyces cerevisiae Species 0.000 title claims abstract description 158
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 75
- 102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 74
- 238000000034 method Methods 0.000 title claims description 51
- 230000008569 process Effects 0.000 title claims description 9
- 238000002360 preparation method Methods 0.000 title description 13
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 94
- 239000013598 vector Substances 0.000 claims abstract description 87
- 229920001184 polypeptide Polymers 0.000 claims abstract description 72
- 238000011144 upstream manufacturing Methods 0.000 claims abstract description 33
- 108700026226 TATA Box Proteins 0.000 claims abstract description 24
- 108020004414 DNA Proteins 0.000 claims description 171
- 239000002773 nucleotide Substances 0.000 claims description 29
- 125000003729 nucleotide group Chemical group 0.000 claims description 29
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 claims description 20
- 108090000723 Insulin-Like Growth Factor I Proteins 0.000 claims description 20
- 210000005253 yeast cell Anatomy 0.000 claims description 20
- 108020004445 glyceraldehyde-3-phosphate dehydrogenase Proteins 0.000 claims description 15
- XYWBJDRHGNULKG-OUMQNGNKSA-N desirudin Chemical compound C([C@@H](C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(O)=O)NC(=O)[C@H](CC(O)=O)NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CCCCN)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](NC(=O)CNC(=O)[C@H](CCC(O)=O)NC(=O)CNC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H]1NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCC(O)=O)NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CO)NC(=O)CNC(=O)[C@H](CC(C)C)NC(=O)[C@H]([C@@H](C)CC)NC(=O)[C@@H]2CSSC[C@@H](C(=O)N[C@@H](CCC(O)=O)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@H](C(=O)N[C@H](C(NCC(=O)N[C@@H](CCC(N)=O)C(=O)NCC(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCCCN)C(=O)N2)=O)CSSC1)C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H]1NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)CNC(=O)[C@H](CO)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CC=2C=CC(O)=CC=2)NC(=O)[C@@H](NC(=O)[C@@H](N)C(C)C)C(C)C)[C@@H](C)O)CSSC1)C(C)C)[C@@H](C)O)[C@@H](C)O)C1=CC=CC=C1 XYWBJDRHGNULKG-OUMQNGNKSA-N 0.000 claims description 12
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 claims description 10
- 241000235070 Saccharomyces Species 0.000 claims description 10
- 229910052799 carbon Inorganic materials 0.000 claims description 10
- 108010073652 desirudin Proteins 0.000 claims description 10
- 229940079322 interferon Drugs 0.000 claims description 10
- 229910052757 nitrogen Inorganic materials 0.000 claims description 10
- 230000035897 transcription Effects 0.000 claims description 10
- 238000013518 transcription Methods 0.000 claims description 10
- 108091026908 Downstream promoter element Proteins 0.000 claims description 9
- 102000014150 Interferons Human genes 0.000 claims description 9
- 108010050904 Interferons Proteins 0.000 claims description 9
- 150000003839 salts Chemical class 0.000 claims description 7
- 102000013275 Somatomedins Human genes 0.000 claims description 3
- 230000000977 initiatory effect Effects 0.000 claims description 3
- 239000007788 liquid Substances 0.000 claims description 3
- 239000003630 growth substance Substances 0.000 claims description 2
- 101000801481 Homo sapiens Tissue-type plasminogen activator Proteins 0.000 claims 1
- 102000047823 human PLAT Human genes 0.000 claims 1
- 108700009124 Transcription Initiation Site Proteins 0.000 abstract description 8
- 238000004519 manufacturing process Methods 0.000 abstract description 6
- 230000022532 regulation of transcription, DNA-dependent Effects 0.000 abstract description 6
- 101150012394 PHO5 gene Proteins 0.000 abstract description 4
- 239000012634 fragment Substances 0.000 description 174
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 119
- 239000013612 plasmid Substances 0.000 description 88
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 64
- 210000004027 cell Anatomy 0.000 description 55
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 44
- 108091026890 Coding region Proteins 0.000 description 33
- 206010033733 Papule Diseases 0.000 description 28
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 28
- 239000000872 buffer Substances 0.000 description 26
- 230000014509 gene expression Effects 0.000 description 24
- 239000002609 medium Substances 0.000 description 24
- 108091008146 restriction endonucleases Proteins 0.000 description 23
- 239000000203 mixture Substances 0.000 description 22
- 108091034117 Oligonucleotide Proteins 0.000 description 21
- 238000012217 deletion Methods 0.000 description 21
- 230000037430 deletion Effects 0.000 description 21
- HEDRZPFGACZZDS-UHFFFAOYSA-N Chloroform Chemical compound ClC(Cl)Cl HEDRZPFGACZZDS-UHFFFAOYSA-N 0.000 description 20
- 239000011543 agarose gel Substances 0.000 description 20
- 229940024606 amino acid Drugs 0.000 description 20
- 150000001413 amino acids Chemical class 0.000 description 20
- 230000009466 transformation Effects 0.000 description 19
- 238000010276 construction Methods 0.000 description 18
- 238000002955 isolation Methods 0.000 description 18
- 102000004218 Insulin-Like Growth Factor I Human genes 0.000 description 17
- 108010076504 Protein Sorting Signals Proteins 0.000 description 17
- 239000000499 gel Substances 0.000 description 17
- 108091028043 Nucleic acid sequence Proteins 0.000 description 16
- 230000000694 effects Effects 0.000 description 16
- 238000012869 ethanol precipitation Methods 0.000 description 16
- 239000000047 product Substances 0.000 description 16
- 102000004169 proteins and genes Human genes 0.000 description 16
- 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 15
- 230000029087 digestion Effects 0.000 description 15
- 239000011780 sodium chloride Substances 0.000 description 14
- 241000588724 Escherichia coli Species 0.000 description 13
- 102100031181 Glyceraldehyde-3-phosphate dehydrogenase Human genes 0.000 description 13
- 238000004458 analytical method Methods 0.000 description 13
- 230000001580 bacterial effect Effects 0.000 description 13
- 238000003776 cleavage reaction Methods 0.000 description 13
- 238000000605 extraction Methods 0.000 description 13
- 230000007017 scission Effects 0.000 description 13
- 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 12
- 229960000723 ampicillin Drugs 0.000 description 12
- 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 12
- 239000008103 glucose Substances 0.000 description 12
- 230000008929 regeneration Effects 0.000 description 12
- 238000011069 regeneration method Methods 0.000 description 12
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 11
- 239000007983 Tris buffer Substances 0.000 description 11
- 230000004913 activation Effects 0.000 description 11
- 230000006870 function Effects 0.000 description 11
- 239000003550 marker Substances 0.000 description 11
- OSBLTNPMIGYQGY-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;2-[2-[bis(carboxymethyl)amino]ethyl-(carboxymethyl)amino]acetic acid;boric acid Chemical compound OB(O)O.OCC(N)(CO)CO.OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O OSBLTNPMIGYQGY-UHFFFAOYSA-N 0.000 description 10
- 102000012410 DNA Ligases Human genes 0.000 description 10
- 108010061982 DNA Ligases Proteins 0.000 description 10
- 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 10
- 210000002421 cell wall Anatomy 0.000 description 10
- 235000015097 nutrients Nutrition 0.000 description 10
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 10
- 102000004190 Enzymes Human genes 0.000 description 9
- 108090000790 Enzymes Proteins 0.000 description 9
- 229940088598 enzyme Drugs 0.000 description 9
- 108020004999 messenger RNA Proteins 0.000 description 9
- 230000001105 regulatory effect Effects 0.000 description 9
- 229920001817 Agar Polymers 0.000 description 8
- 108091081024 Start codon Proteins 0.000 description 8
- DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 8
- 239000008272 agar Substances 0.000 description 8
- 239000011575 calcium Substances 0.000 description 8
- 150000002500 ions Chemical class 0.000 description 8
- 238000000746 purification Methods 0.000 description 8
- 238000013519 translation Methods 0.000 description 8
- 108700039691 Genetic Promoter Regions Proteins 0.000 description 7
- 238000002844 melting Methods 0.000 description 7
- 230000010076 replication Effects 0.000 description 7
- 239000000243 solution Substances 0.000 description 7
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 6
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 6
- KFZMGEQAYNKOFK-UHFFFAOYSA-N Isopropanol Chemical compound CC(C)O KFZMGEQAYNKOFK-UHFFFAOYSA-N 0.000 description 6
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 6
- 102000003960 Ligases Human genes 0.000 description 6
- 108090000364 Ligases Proteins 0.000 description 6
- 108700026244 Open Reading Frames Proteins 0.000 description 6
- YGYAWVDWMABLBF-UHFFFAOYSA-N Phosgene Chemical compound ClC(Cl)=O YGYAWVDWMABLBF-UHFFFAOYSA-N 0.000 description 6
- 239000012190 activator Substances 0.000 description 6
- 229910052791 calcium Inorganic materials 0.000 description 6
- 210000000349 chromosome Anatomy 0.000 description 6
- 238000000855 fermentation Methods 0.000 description 6
- 230000004151 fermentation Effects 0.000 description 6
- 230000002068 genetic effect Effects 0.000 description 6
- 239000001963 growth medium Substances 0.000 description 6
- GZCWLCBFPRFLKL-UHFFFAOYSA-N 1-prop-2-ynoxypropan-2-ol Chemical compound CC(O)COCC#C GZCWLCBFPRFLKL-UHFFFAOYSA-N 0.000 description 5
- 102000013563 Acid Phosphatase Human genes 0.000 description 5
- 108010051457 Acid Phosphatase Proteins 0.000 description 5
- 108060002716 Exonuclease Proteins 0.000 description 5
- 108010007267 Hirudins Proteins 0.000 description 5
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 5
- 108091036060 Linker DNA Proteins 0.000 description 5
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 5
- 238000000246 agarose gel electrophoresis Methods 0.000 description 5
- 238000006243 chemical reaction Methods 0.000 description 5
- 238000010367 cloning Methods 0.000 description 5
- 102000013165 exonuclease Human genes 0.000 description 5
- 230000004927 fusion Effects 0.000 description 5
- 238000000338 in vitro Methods 0.000 description 5
- 230000008018 melting Effects 0.000 description 5
- 238000012545 processing Methods 0.000 description 5
- 239000001632 sodium acetate Substances 0.000 description 5
- 235000017281 sodium acetate Nutrition 0.000 description 5
- 102000004594 DNA Polymerase I Human genes 0.000 description 4
- 108010017826 DNA Polymerase I Proteins 0.000 description 4
- 238000001712 DNA sequencing Methods 0.000 description 4
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 description 4
- 102000016928 DNA-directed DNA polymerase Human genes 0.000 description 4
- 102000007625 Hirudins Human genes 0.000 description 4
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 4
- 241000700605 Viruses Species 0.000 description 4
- 239000000427 antigen Substances 0.000 description 4
- 108091007433 antigens Proteins 0.000 description 4
- 102000036639 antigens Human genes 0.000 description 4
- 230000001419 dependent effect Effects 0.000 description 4
- 238000000502 dialysis Methods 0.000 description 4
- 230000012010 growth Effects 0.000 description 4
- 239000003102 growth factor Substances 0.000 description 4
- 229940006607 hirudin Drugs 0.000 description 4
- WQPDUTSPKFMPDP-OUMQNGNKSA-N hirudin Chemical compound C([C@@H](C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC=1C=CC(OS(O)(=O)=O)=CC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(O)=O)NC(=O)[C@H](CC(O)=O)NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CCCCN)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](NC(=O)CNC(=O)[C@H](CCC(O)=O)NC(=O)CNC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H]1NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCC(O)=O)NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CO)NC(=O)CNC(=O)[C@H](CC(C)C)NC(=O)[C@H]([C@@H](C)CC)NC(=O)[C@@H]2CSSC[C@@H](C(=O)N[C@@H](CCC(O)=O)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@H](C(=O)N[C@H](C(NCC(=O)N[C@@H](CCC(N)=O)C(=O)NCC(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCCCN)C(=O)N2)=O)CSSC1)C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H]1NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)CNC(=O)[C@H](CO)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CC=2C=CC(O)=CC=2)NC(=O)[C@@H](NC(=O)[C@@H](N)C(C)C)C(C)C)[C@@H](C)O)CSSC1)C(C)C)[C@@H](C)O)[C@@H](C)O)C1=CC=CC=C1 WQPDUTSPKFMPDP-OUMQNGNKSA-N 0.000 description 4
- 238000011534 incubation Methods 0.000 description 4
- NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 4
- 230000037361 pathway Effects 0.000 description 4
- 230000009467 reduction Effects 0.000 description 4
- 238000004007 reversed phase HPLC Methods 0.000 description 4
- 238000012163 sequencing technique Methods 0.000 description 4
- 239000000126 substance Substances 0.000 description 4
- 230000014621 translational initiation Effects 0.000 description 4
- -1 vaccines Proteins 0.000 description 4
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 4
- 102000053602 DNA Human genes 0.000 description 3
- 102100031780 Endonuclease Human genes 0.000 description 3
- 108010042407 Endonucleases Proteins 0.000 description 3
- 101001011019 Gallus gallus Gallinacin-10 Proteins 0.000 description 3
- 101001011021 Gallus gallus Gallinacin-12 Proteins 0.000 description 3
- 101150112014 Gapdh gene Proteins 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- 101150009006 HIS3 gene Proteins 0.000 description 3
- XEEYBQQBJWHFJM-UHFFFAOYSA-N Iron Chemical compound [Fe] XEEYBQQBJWHFJM-UHFFFAOYSA-N 0.000 description 3
- 229910019142 PO4 Inorganic materials 0.000 description 3
- 239000002202 Polyethylene glycol Substances 0.000 description 3
- 108010021757 Polynucleotide 5'-Hydroxyl-Kinase Proteins 0.000 description 3
- 102000008422 Polynucleotide 5'-hydroxyl-kinase Human genes 0.000 description 3
- 108020005091 Replication Origin Proteins 0.000 description 3
- 101100394989 Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) hisI gene Proteins 0.000 description 3
- 238000009825 accumulation Methods 0.000 description 3
- 239000002253 acid Substances 0.000 description 3
- 230000003213 activating effect Effects 0.000 description 3
- 229960001230 asparagine Drugs 0.000 description 3
- 239000011324 bead Substances 0.000 description 3
- 238000004587 chromatography analysis Methods 0.000 description 3
- 238000010586 diagram Methods 0.000 description 3
- 108010031145 eglin proteinase inhibitors Proteins 0.000 description 3
- 238000001962 electrophoresis Methods 0.000 description 3
- 239000000284 extract Substances 0.000 description 3
- 239000012530 fluid Substances 0.000 description 3
- 238000001502 gel electrophoresis Methods 0.000 description 3
- 238000010353 genetic engineering Methods 0.000 description 3
- 239000011521 glass Substances 0.000 description 3
- 230000002414 glycolytic effect Effects 0.000 description 3
- 229960002885 histidine Drugs 0.000 description 3
- 229910052816 inorganic phosphate Inorganic materials 0.000 description 3
- 238000005342 ion exchange Methods 0.000 description 3
- 238000004255 ion exchange chromatography Methods 0.000 description 3
- 229940046166 oligodeoxynucleotide Drugs 0.000 description 3
- 230000036961 partial effect Effects 0.000 description 3
- 235000021317 phosphate Nutrition 0.000 description 3
- 229920001223 polyethylene glycol Polymers 0.000 description 3
- 239000011541 reaction mixture Substances 0.000 description 3
- 230000002829 reductive effect Effects 0.000 description 3
- 230000003362 replicative effect Effects 0.000 description 3
- 230000003248 secreting effect Effects 0.000 description 3
- 239000007787 solid Substances 0.000 description 3
- 239000000758 substrate Substances 0.000 description 3
- 239000006228 supernatant Substances 0.000 description 3
- 230000005026 transcription initiation Effects 0.000 description 3
- 230000005030 transcription termination Effects 0.000 description 3
- 230000002103 transcriptional effect Effects 0.000 description 3
- 230000001131 transforming effect Effects 0.000 description 3
- CYNAPIVXKRLDER-LBPRGKRZSA-N (2s)-2-benzamido-3-(4-hydroxy-3-nitrophenyl)propanoic acid Chemical compound C([C@@H](C(=O)O)NC(=O)C=1C=CC=CC=1)C1=CC=C(O)C([N+]([O-])=O)=C1 CYNAPIVXKRLDER-LBPRGKRZSA-N 0.000 description 2
- 108020005065 3' Flanking Region Proteins 0.000 description 2
- OSJPPGNTCRNQQC-UWTATZPHSA-N 3-phospho-D-glyceric acid Chemical compound OC(=O)[C@H](O)COP(O)(O)=O OSJPPGNTCRNQQC-UWTATZPHSA-N 0.000 description 2
- QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical compound CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 description 2
- NLXLAEXVIDQMFP-UHFFFAOYSA-N Ammonia chloride Chemical compound [NH4+].[Cl-] NLXLAEXVIDQMFP-UHFFFAOYSA-N 0.000 description 2
- 108010039209 Blood Coagulation Factors Proteins 0.000 description 2
- 102000015081 Blood Coagulation Factors Human genes 0.000 description 2
- 102000055006 Calcitonin Human genes 0.000 description 2
- 108060001064 Calcitonin Proteins 0.000 description 2
- 241000222120 Candida <Saccharomycetales> Species 0.000 description 2
- 108010001498 Galectin 1 Proteins 0.000 description 2
- 102100021736 Galectin-1 Human genes 0.000 description 2
- 102100024637 Galectin-10 Human genes 0.000 description 2
- 241000700721 Hepatitis B virus Species 0.000 description 2
- 108060003951 Immunoglobulin Proteins 0.000 description 2
- 102000004877 Insulin Human genes 0.000 description 2
- 108090001061 Insulin Proteins 0.000 description 2
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 2
- 239000006142 Luria-Bertani Agar Substances 0.000 description 2
- 206010028980 Neoplasm Diseases 0.000 description 2
- 101100062121 Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) cyc-1 gene Proteins 0.000 description 2
- 102000004160 Phosphoric Monoester Hydrolases Human genes 0.000 description 2
- 108090000608 Phosphoric Monoester Hydrolases Proteins 0.000 description 2
- 241000496314 Pyrrhobryum medium Species 0.000 description 2
- 238000012300 Sequence Analysis Methods 0.000 description 2
- 229930006000 Sucrose Natural products 0.000 description 2
- 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 2
- 239000008051 TBE buffer Substances 0.000 description 2
- 102000003978 Tissue Plasminogen Activator Human genes 0.000 description 2
- 108090000373 Tissue Plasminogen Activator Proteins 0.000 description 2
- 102000003990 Urokinase-type plasminogen activator Human genes 0.000 description 2
- 108090000435 Urokinase-type plasminogen activator Proteins 0.000 description 2
- 235000011130 ammonium sulphate Nutrition 0.000 description 2
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 2
- 230000003115 biocidal effect Effects 0.000 description 2
- 239000003114 blood coagulation factor Substances 0.000 description 2
- KGBXLFKZBHKPEV-UHFFFAOYSA-N boric acid Chemical compound OB(O)O KGBXLFKZBHKPEV-UHFFFAOYSA-N 0.000 description 2
- 239000004327 boric acid Substances 0.000 description 2
- 239000007853 buffer solution Substances 0.000 description 2
- BBBFJLBPOGFECG-VJVYQDLKSA-N calcitonin Chemical compound N([C@H](C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(N)=O)C(C)C)C(=O)[C@@H]1CSSC[C@H](N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1 BBBFJLBPOGFECG-VJVYQDLKSA-N 0.000 description 2
- 229960004015 calcitonin Drugs 0.000 description 2
- 244000309466 calf Species 0.000 description 2
- 229940041514 candida albicans extract Drugs 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 238000012512 characterization method Methods 0.000 description 2
- 239000003795 chemical substances by application Substances 0.000 description 2
- 230000000295 complement effect Effects 0.000 description 2
- 238000007796 conventional method Methods 0.000 description 2
- 238000001816 cooling Methods 0.000 description 2
- YPHMISFOHDHNIV-FSZOTQKASA-N cycloheximide Chemical compound C1[C@@H](C)C[C@H](C)C(=O)[C@@H]1[C@H](O)CC1CC(=O)NC(=O)C1 YPHMISFOHDHNIV-FSZOTQKASA-N 0.000 description 2
- 238000013461 design Methods 0.000 description 2
- 230000002255 enzymatic effect Effects 0.000 description 2
- 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 2
- 229960005542 ethidium bromide Drugs 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 238000004992 fast atom bombardment mass spectroscopy Methods 0.000 description 2
- 238000009472 formulation Methods 0.000 description 2
- 102000034356 gene-regulatory proteins Human genes 0.000 description 2
- 108091006104 gene-regulatory proteins Proteins 0.000 description 2
- 125000003147 glycosyl group Chemical group 0.000 description 2
- 238000004128 high performance liquid chromatography Methods 0.000 description 2
- 229940088597 hormone Drugs 0.000 description 2
- 239000005556 hormone Substances 0.000 description 2
- 238000009396 hybridization Methods 0.000 description 2
- 210000004408 hybridoma Anatomy 0.000 description 2
- 102000018358 immunoglobulin Human genes 0.000 description 2
- 230000001976 improved effect Effects 0.000 description 2
- 230000002779 inactivation Effects 0.000 description 2
- 238000010348 incorporation Methods 0.000 description 2
- 230000001939 inductive effect Effects 0.000 description 2
- 230000005764 inhibitory process Effects 0.000 description 2
- 229940125396 insulin Drugs 0.000 description 2
- 239000000543 intermediate Substances 0.000 description 2
- 244000005700 microbiome Species 0.000 description 2
- 230000035772 mutation Effects 0.000 description 2
- 239000003921 oil Substances 0.000 description 2
- 210000001322 periplasm Anatomy 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 2
- 239000010452 phosphate Substances 0.000 description 2
- 238000007747 plating Methods 0.000 description 2
- 108091033319 polynucleotide Proteins 0.000 description 2
- 102000040430 polynucleotide Human genes 0.000 description 2
- 239000002157 polynucleotide Substances 0.000 description 2
- 238000001556 precipitation Methods 0.000 description 2
- 230000006798 recombination Effects 0.000 description 2
- 238000005215 recombination Methods 0.000 description 2
- 230000000717 retained effect Effects 0.000 description 2
- 230000002441 reversible effect Effects 0.000 description 2
- 238000007480 sanger sequencing Methods 0.000 description 2
- 241000894007 species Species 0.000 description 2
- 230000007480 spreading Effects 0.000 description 2
- 238000003892 spreading Methods 0.000 description 2
- 239000005720 sucrose Substances 0.000 description 2
- 238000012360 testing method Methods 0.000 description 2
- 210000001519 tissue Anatomy 0.000 description 2
- 229960000187 tissue plasminogen activator Drugs 0.000 description 2
- 239000011573 trace mineral Substances 0.000 description 2
- 235000013619 trace mineral Nutrition 0.000 description 2
- 238000010361 transduction Methods 0.000 description 2
- 230000026683 transduction Effects 0.000 description 2
- GPRLSGONYQIRFK-MNYXATJNSA-N triton Chemical compound [3H+] GPRLSGONYQIRFK-MNYXATJNSA-N 0.000 description 2
- 239000012137 tryptone Substances 0.000 description 2
- 229960005356 urokinase Drugs 0.000 description 2
- 239000012138 yeast extract Substances 0.000 description 2
- OWEGMIWEEQEYGQ-UHFFFAOYSA-N 100676-05-9 Natural products OC1C(O)C(O)C(CO)OC1OCC1C(O)C(O)C(O)C(OC2C(OC(O)C(O)C2O)CO)O1 OWEGMIWEEQEYGQ-UHFFFAOYSA-N 0.000 description 1
- VTVWTPGLLAELLI-UHFFFAOYSA-N 4-[[4-(dimethylamino)phenyl]diazenyl]benzenesulfonyl chloride Chemical compound C1=CC(N(C)C)=CC=C1N=NC1=CC=C(S(Cl)(=O)=O)C=C1 VTVWTPGLLAELLI-UHFFFAOYSA-N 0.000 description 1
- MCNQUWLLXZZZAC-UHFFFAOYSA-N 4-cyano-1-(2,4-dichlorophenyl)-5-(4-methoxyphenyl)-n-piperidin-1-ylpyrazole-3-carboxamide Chemical compound C1=CC(OC)=CC=C1C1=C(C#N)C(C(=O)NN2CCCCC2)=NN1C1=CC=C(Cl)C=C1Cl MCNQUWLLXZZZAC-UHFFFAOYSA-N 0.000 description 1
- 101150096316 5 gene Proteins 0.000 description 1
- ODPOAESBSUKMHD-UHFFFAOYSA-L 6,7-dihydrodipyrido[1,2-b:1',2'-e]pyrazine-5,8-diium;dibromide Chemical compound [Br-].[Br-].C1=CC=[N+]2CC[N+]3=CC=CC=C3C2=C1 ODPOAESBSUKMHD-UHFFFAOYSA-L 0.000 description 1
- 229920000936 Agarose Polymers 0.000 description 1
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 1
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 1
- GUBGYTABKSRVRQ-XLOQQCSPSA-N Alpha-Lactose Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1O[C@@H]1[C@@H](CO)O[C@H](O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-XLOQQCSPSA-N 0.000 description 1
- 208000031295 Animal disease Diseases 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 241000270298 Boidae Species 0.000 description 1
- BTBUEUYNUDRHOZ-UHFFFAOYSA-N Borate Chemical compound [O-]B([O-])[O-] BTBUEUYNUDRHOZ-UHFFFAOYSA-N 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- NLZUEZXRPGMBCV-UHFFFAOYSA-N Butylhydroxytoluene Chemical compound CC1=CC(C(C)(C)C)=C(O)C(C(C)(C)C)=C1 NLZUEZXRPGMBCV-UHFFFAOYSA-N 0.000 description 1
- 108091028026 C-DNA Proteins 0.000 description 1
- 101150069146 C5 gene Proteins 0.000 description 1
- 108010072454 CTGCAG-specific type II deoxyribonucleases Proteins 0.000 description 1
- 102100022641 Coagulation factor IX Human genes 0.000 description 1
- 108091033380 Coding strand Proteins 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- FBPFZTCFMRRESA-FSIIMWSLSA-N D-Glucitol Natural products OC[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO FBPFZTCFMRRESA-FSIIMWSLSA-N 0.000 description 1
- FBPFZTCFMRRESA-KVTDHHQDSA-N D-Mannitol Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-KVTDHHQDSA-N 0.000 description 1
- 102000010567 DNA Polymerase II Human genes 0.000 description 1
- 108010063113 DNA Polymerase II Proteins 0.000 description 1
- 238000007399 DNA isolation Methods 0.000 description 1
- 108010066072 DNA modification methylase EcoRI Proteins 0.000 description 1
- 108010008286 DNA nucleotidylexotransferase Proteins 0.000 description 1
- 230000006820 DNA synthesis Effects 0.000 description 1
- 102100029764 DNA-directed DNA/RNA polymerase mu Human genes 0.000 description 1
- 101710088194 Dehydrogenase Proteins 0.000 description 1
- 101150105088 Dele1 gene Proteins 0.000 description 1
- 108010005054 Deoxyribonuclease BamHI Proteins 0.000 description 1
- 108010054576 Deoxyribonuclease EcoRI Proteins 0.000 description 1
- 239000005630 Diquat Substances 0.000 description 1
- 244000078127 Eleusine coracana Species 0.000 description 1
- 235000013499 Eleusine coracana subsp coracana Nutrition 0.000 description 1
- 102000004533 Endonucleases Human genes 0.000 description 1
- 108010059378 Endopeptidases Proteins 0.000 description 1
- 102000005593 Endopeptidases Human genes 0.000 description 1
- 101000885147 Enterococcus avium D-arabitol-phosphate dehydrogenase Proteins 0.000 description 1
- 241000588722 Escherichia Species 0.000 description 1
- 241001131785 Escherichia coli HB101 Species 0.000 description 1
- 108091092566 Extrachromosomal DNA Proteins 0.000 description 1
- 108010076282 Factor IX Proteins 0.000 description 1
- 101150004883 GRF10 gene Proteins 0.000 description 1
- 108010001515 Galectin 4 Proteins 0.000 description 1
- 102100039555 Galectin-7 Human genes 0.000 description 1
- 101000887163 Gallus gallus Gallinacin-4 Proteins 0.000 description 1
- 101000887166 Gallus gallus Gallinacin-7 Proteins 0.000 description 1
- 241000237858 Gastropoda Species 0.000 description 1
- 108010021582 Glucokinase Proteins 0.000 description 1
- 108010056771 Glucosidases Proteins 0.000 description 1
- 102000004366 Glucosidases Human genes 0.000 description 1
- 241000709721 Hepatovirus A Species 0.000 description 1
- 102000005548 Hexokinase Human genes 0.000 description 1
- 108700040460 Hexokinases Proteins 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 101000599951 Homo sapiens Insulin-like growth factor I Proteins 0.000 description 1
- 101000878605 Homo sapiens Low affinity immunoglobulin epsilon Fc receptor 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
- 102100037852 Insulin-like growth factor I Human genes 0.000 description 1
- 102000005755 Intercellular Signaling Peptides and Proteins Human genes 0.000 description 1
- 108010070716 Intercellular Signaling Peptides and Proteins Proteins 0.000 description 1
- 102000000589 Interleukin-1 Human genes 0.000 description 1
- 108010002352 Interleukin-1 Proteins 0.000 description 1
- 108010002350 Interleukin-2 Proteins 0.000 description 1
- 102000000588 Interleukin-2 Human genes 0.000 description 1
- 102000015696 Interleukins Human genes 0.000 description 1
- 108010063738 Interleukins Proteins 0.000 description 1
- 102100024319 Intestinal-type alkaline phosphatase Human genes 0.000 description 1
- 101710184243 Intestinal-type alkaline phosphatase Proteins 0.000 description 1
- 102000004195 Isomerases Human genes 0.000 description 1
- 108090000769 Isomerases Proteins 0.000 description 1
- 241000235649 Kluyveromyces Species 0.000 description 1
- LEVWYRKDKASIDU-IMJSIDKUSA-N L-cystine Chemical compound [O-]C(=O)[C@@H]([NH3+])CSSC[C@H]([NH3+])C([O-])=O LEVWYRKDKASIDU-IMJSIDKUSA-N 0.000 description 1
- JVTAAEKCZFNVCJ-UHFFFAOYSA-M Lactate Chemical compound CC(O)C([O-])=O JVTAAEKCZFNVCJ-UHFFFAOYSA-M 0.000 description 1
- 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 1
- 108700005090 Lethal Genes Proteins 0.000 description 1
- 102100038007 Low affinity immunoglobulin epsilon Fc receptor Human genes 0.000 description 1
- NPBGTPKLVJEOBE-IUCAKERBSA-N Lys-Arg Chemical group NCCCC[C@H](N)C(=O)N[C@H](C(O)=O)CCCNC(N)=N NPBGTPKLVJEOBE-IUCAKERBSA-N 0.000 description 1
- FYYHWMGAXLPEAU-UHFFFAOYSA-N Magnesium Chemical compound [Mg] FYYHWMGAXLPEAU-UHFFFAOYSA-N 0.000 description 1
- GUBGYTABKSRVRQ-PICCSMPSSA-N Maltose Natural products O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@@H](CO)OC(O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-PICCSMPSSA-N 0.000 description 1
- 229930195725 Mannitol Natural products 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 108060004795 Methyltransferase Proteins 0.000 description 1
- 229910002651 NO3 Inorganic materials 0.000 description 1
- NHNBFGGVMKEFGY-UHFFFAOYSA-N Nitrate Chemical compound [O-][N+]([O-])=O NHNBFGGVMKEFGY-UHFFFAOYSA-N 0.000 description 1
- 102000019040 Nuclear Antigens Human genes 0.000 description 1
- 108010051791 Nuclear Antigens Proteins 0.000 description 1
- 101710163270 Nuclease Proteins 0.000 description 1
- 101800004910 Nuclease A Proteins 0.000 description 1
- 108010067372 Pancreatic elastase Proteins 0.000 description 1
- 102000016387 Pancreatic elastase Human genes 0.000 description 1
- 102000015731 Peptide Hormones Human genes 0.000 description 1
- 108010038988 Peptide Hormones Proteins 0.000 description 1
- 239000001888 Peptone Substances 0.000 description 1
- 108010080698 Peptones Proteins 0.000 description 1
- OAICVXFJPJFONN-UHFFFAOYSA-N Phosphorus Chemical compound [P] OAICVXFJPJFONN-UHFFFAOYSA-N 0.000 description 1
- 229920002873 Polyethylenimine Polymers 0.000 description 1
- ZLMJMSJWJFRBEC-UHFFFAOYSA-N Potassium Chemical compound [K] ZLMJMSJWJFRBEC-UHFFFAOYSA-N 0.000 description 1
- 108020001991 Protoporphyrinogen Oxidase Proteins 0.000 description 1
- 102000005135 Protoporphyrinogen oxidase Human genes 0.000 description 1
- 108010011939 Pyruvate Decarboxylase Proteins 0.000 description 1
- 102000013009 Pyruvate Kinase Human genes 0.000 description 1
- 108020005115 Pyruvate Kinase Proteins 0.000 description 1
- 102000009572 RNA Polymerase II Human genes 0.000 description 1
- 108010009460 RNA Polymerase II Proteins 0.000 description 1
- 101100173636 Rattus norvegicus Fhl2 gene Proteins 0.000 description 1
- 108090000783 Renin Proteins 0.000 description 1
- 102100028255 Renin Human genes 0.000 description 1
- 241000223252 Rhodotorula Species 0.000 description 1
- 101100083256 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) PHO2 gene Proteins 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- SSJMZMUVNKEENT-IMJSIDKUSA-N Ser-Ala Chemical compound OC(=O)[C@H](C)NC(=O)[C@@H](N)CO SSJMZMUVNKEENT-IMJSIDKUSA-N 0.000 description 1
- 108020004682 Single-Stranded DNA Proteins 0.000 description 1
- QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 1
- 102000019197 Superoxide Dismutase Human genes 0.000 description 1
- 108010012715 Superoxide dismutase Proteins 0.000 description 1
- 239000004098 Tetracycline Substances 0.000 description 1
- 244000269722 Thea sinensis Species 0.000 description 1
- 108090000190 Thrombin Proteins 0.000 description 1
- 244000044283 Toxicodendron succedaneum Species 0.000 description 1
- 108700019146 Transgenes Proteins 0.000 description 1
- 102000005924 Triose-Phosphate Isomerase Human genes 0.000 description 1
- 108700015934 Triose-phosphate isomerases Proteins 0.000 description 1
- 208000026487 Triploidy Diseases 0.000 description 1
- 241000209140 Triticum Species 0.000 description 1
- 235000021307 Triticum Nutrition 0.000 description 1
- 101150058730 Ttpa gene Proteins 0.000 description 1
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 1
- 240000008042 Zea mays Species 0.000 description 1
- 235000005824 Zea mays ssp. parviglumis Nutrition 0.000 description 1
- 235000002017 Zea mays subsp mays Nutrition 0.000 description 1
- HCHKCACWOHOZIP-UHFFFAOYSA-N Zinc Chemical compound [Zn] HCHKCACWOHOZIP-UHFFFAOYSA-N 0.000 description 1
- 206010000210 abortion Diseases 0.000 description 1
- 231100000176 abortion Toxicity 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- PBCJIPOGFJYBJE-UHFFFAOYSA-N acetonitrile;hydrate Chemical compound O.CC#N PBCJIPOGFJYBJE-UHFFFAOYSA-N 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 239000000853 adhesive Substances 0.000 description 1
- 230000001070 adhesive effect Effects 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 235000001014 amino acid Nutrition 0.000 description 1
- 108010012543 amino-terminal parathyroid hormone Proteins 0.000 description 1
- 235000019270 ammonium chloride Nutrition 0.000 description 1
- 150000003863 ammonium salts Chemical class 0.000 description 1
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 1
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 1
- 239000001166 ammonium sulphate Substances 0.000 description 1
- 230000003321 amplification Effects 0.000 description 1
- 230000003698 anagen phase Effects 0.000 description 1
- 239000012491 analyte Substances 0.000 description 1
- 238000005349 anion exchange Methods 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 230000000259 anti-tumor effect Effects 0.000 description 1
- 230000000840 anti-viral effect Effects 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 239000008346 aqueous phase Substances 0.000 description 1
- 230000002716 ataractic effect Effects 0.000 description 1
- 238000000376 autoradiography Methods 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 108010051210 beta-Fructofuranosidase Proteins 0.000 description 1
- GUBGYTABKSRVRQ-QUYVBRFLSA-N beta-maltose Chemical compound OC[C@H]1O[C@H](O[C@H]2[C@H](O)[C@@H](O)[C@H](O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@@H]1O GUBGYTABKSRVRQ-QUYVBRFLSA-N 0.000 description 1
- 230000033228 biological regulation Effects 0.000 description 1
- 230000001851 biosynthetic effect Effects 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 201000011510 cancer Diseases 0.000 description 1
- 239000004202 carbamide Substances 0.000 description 1
- 150000001720 carbohydrates Chemical group 0.000 description 1
- 150000004649 carbonic acid derivatives Chemical class 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 210000000170 cell membrane Anatomy 0.000 description 1
- 239000006285 cell suspension Substances 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 230000019522 cellular metabolic process Effects 0.000 description 1
- 230000003196 chaotropic effect Effects 0.000 description 1
- 239000013043 chemical agent Substances 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 150000001805 chlorine compounds Chemical class 0.000 description 1
- 239000013611 chromosomal DNA Substances 0.000 description 1
- 230000002759 chromosomal effect Effects 0.000 description 1
- 230000005757 colony formation Effects 0.000 description 1
- 230000002860 competitive effect Effects 0.000 description 1
- 239000012141 concentrate Substances 0.000 description 1
- 235000005822 corn Nutrition 0.000 description 1
- 239000013601 cosmid vector Substances 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- 229960003067 cystine Drugs 0.000 description 1
- 230000006378 damage Effects 0.000 description 1
- 230000002498 deadly effect Effects 0.000 description 1
- 230000007423 decrease Effects 0.000 description 1
- 230000002950 deficient Effects 0.000 description 1
- 230000006735 deficit Effects 0.000 description 1
- 239000007857 degradation product Substances 0.000 description 1
- 230000002939 deleterious effect Effects 0.000 description 1
- 238000011033 desalting Methods 0.000 description 1
- 239000003599 detergent Substances 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 230000018109 developmental process Effects 0.000 description 1
- 238000009792 diffusion process Methods 0.000 description 1
- 229940124568 digestive agent Drugs 0.000 description 1
- 230000001079 digestive effect Effects 0.000 description 1
- 230000003292 diminished effect Effects 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- 238000002592 echocardiography Methods 0.000 description 1
- 235000013601 eggs Nutrition 0.000 description 1
- 239000003480 eluent Substances 0.000 description 1
- 230000006862 enzymatic digestion Effects 0.000 description 1
- 238000006911 enzymatic reaction Methods 0.000 description 1
- 210000003527 eukaryotic cell Anatomy 0.000 description 1
- 230000029142 excretion Effects 0.000 description 1
- 239000013613 expression plasmid Substances 0.000 description 1
- 239000013604 expression vector Substances 0.000 description 1
- 238000001125 extrusion Methods 0.000 description 1
- 229960004222 factor ix Drugs 0.000 description 1
- 230000002349 favourable effect Effects 0.000 description 1
- RFHAOTPXVQNOHP-UHFFFAOYSA-N fluconazole Chemical compound C1=NC=NN1CC(C=1C(=CC(F)=CC=1)F)(O)CN1C=NC=N1 RFHAOTPXVQNOHP-UHFFFAOYSA-N 0.000 description 1
- 239000004459 forage Substances 0.000 description 1
- 238000010230 functional analysis Methods 0.000 description 1
- 238000012215 gene cloning Methods 0.000 description 1
- 229960001031 glucose Drugs 0.000 description 1
- 235000001727 glucose Nutrition 0.000 description 1
- 230000013595 glycosylation Effects 0.000 description 1
- 238000006206 glycosylation reaction Methods 0.000 description 1
- 239000000122 growth hormone Substances 0.000 description 1
- 239000007952 growth promoter Substances 0.000 description 1
- 208000006454 hepatitis Diseases 0.000 description 1
- 231100000283 hepatitis Toxicity 0.000 description 1
- 210000003630 histaminocyte Anatomy 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 229920001519 homopolymer Polymers 0.000 description 1
- 229930195733 hydrocarbon Natural products 0.000 description 1
- 150000002430 hydrocarbons Chemical class 0.000 description 1
- 230000002519 immonomodulatory effect Effects 0.000 description 1
- 108010008429 immunoglobulin-binding factors Proteins 0.000 description 1
- 229940072221 immunoglobulins Drugs 0.000 description 1
- 238000007901 in situ hybridization Methods 0.000 description 1
- 238000003017 in situ immunoassay Methods 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 238000001802 infusion Methods 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 239000003999 initiator Substances 0.000 description 1
- 230000002608 insulinlike Effects 0.000 description 1
- 230000010354 integration Effects 0.000 description 1
- 229940047124 interferons Drugs 0.000 description 1
- 210000000936 intestine Anatomy 0.000 description 1
- 229910052742 iron Inorganic materials 0.000 description 1
- 239000008101 lactose Substances 0.000 description 1
- 238000011031 large-scale manufacturing process Methods 0.000 description 1
- 229920002521 macromolecule Polymers 0.000 description 1
- 210000002540 macrophage Anatomy 0.000 description 1
- 239000011777 magnesium Substances 0.000 description 1
- 229910052749 magnesium Inorganic materials 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- WPBNNNQJVZRUHP-UHFFFAOYSA-L manganese(2+);methyl n-[[2-(methoxycarbonylcarbamothioylamino)phenyl]carbamothioyl]carbamate;n-[2-(sulfidocarbothioylamino)ethyl]carbamodithioate Chemical compound [Mn+2].[S-]C(=S)NCCNC([S-])=S.COC(=O)NC(=S)NC1=CC=CC=C1NC(=S)NC(=O)OC WPBNNNQJVZRUHP-UHFFFAOYSA-L 0.000 description 1
- 239000000594 mannitol Substances 0.000 description 1
- 235000010355 mannitol Nutrition 0.000 description 1
- 238000004949 mass spectrometry Methods 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 230000035800 maturation Effects 0.000 description 1
- 235000019988 mead Nutrition 0.000 description 1
- 235000013372 meat Nutrition 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 1
- 230000011987 methylation Effects 0.000 description 1
- 238000007069 methylation reaction Methods 0.000 description 1
- 230000002906 microbiologic effect Effects 0.000 description 1
- 238000013508 migration Methods 0.000 description 1
- 230000005012 migration Effects 0.000 description 1
- 230000011278 mitosis Effects 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- PJUIMOJAAPLTRJ-UHFFFAOYSA-N monothioglycerol Chemical compound OCC(O)CS PJUIMOJAAPLTRJ-UHFFFAOYSA-N 0.000 description 1
- 238000002703 mutagenesis Methods 0.000 description 1
- 231100000350 mutagenesis Toxicity 0.000 description 1
- 238000003199 nucleic acid amplification method Methods 0.000 description 1
- 235000016709 nutrition Nutrition 0.000 description 1
- 230000002018 overexpression Effects 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- 235000019319 peptone Nutrition 0.000 description 1
- 230000000144 pharmacologic effect Effects 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 150000003013 phosphoric acid derivatives Chemical class 0.000 description 1
- 229910052698 phosphorus Inorganic materials 0.000 description 1
- 239000011574 phosphorus Substances 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 230000008488 polyadenylation Effects 0.000 description 1
- 238000006116 polymerization reaction Methods 0.000 description 1
- 239000011591 potassium Substances 0.000 description 1
- 229910052700 potassium Inorganic materials 0.000 description 1
- ZNNZYHKDIALBAK-UHFFFAOYSA-M potassium thiocyanate Chemical compound [K+].[S-]C#N ZNNZYHKDIALBAK-UHFFFAOYSA-M 0.000 description 1
- 230000003389 potentiating effect Effects 0.000 description 1
- 230000001376 precipitating effect Effects 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 230000002265 prevention Effects 0.000 description 1
- 210000001236 prokaryotic cell Anatomy 0.000 description 1
- 230000000644 propagated effect Effects 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 238000003127 radioimmunoassay Methods 0.000 description 1
- 235000002079 ragi Nutrition 0.000 description 1
- 101150079601 recA gene Proteins 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 230000001172 regenerating effect Effects 0.000 description 1
- 230000009711 regulatory function Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 239000011347 resin Substances 0.000 description 1
- 229920005989 resin Polymers 0.000 description 1
- 239000007320 rich medium Substances 0.000 description 1
- 238000005096 rolling process Methods 0.000 description 1
- 238000012216 screening Methods 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- 238000003998 size exclusion chromatography high performance liquid chromatography Methods 0.000 description 1
- 238000001542 size-exclusion chromatography Methods 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 239000002689 soil Substances 0.000 description 1
- 239000000600 sorbitol Substances 0.000 description 1
- 238000001179 sorption measurement Methods 0.000 description 1
- 125000006850 spacer group Chemical group 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 239000003774 sulfhydryl reagent Substances 0.000 description 1
- 150000003467 sulfuric acid derivatives Chemical class 0.000 description 1
- 229910021653 sulphate ion Inorganic materials 0.000 description 1
- 239000013589 supplement Substances 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 230000002194 synthesizing effect Effects 0.000 description 1
- 229960002180 tetracycline Drugs 0.000 description 1
- 229930101283 tetracycline Natural products 0.000 description 1
- 235000019364 tetracycline Nutrition 0.000 description 1
- 150000003522 tetracyclines Chemical class 0.000 description 1
- 229940035024 thioglycerol Drugs 0.000 description 1
- 229960004072 thrombin Drugs 0.000 description 1
- 231100000331 toxic Toxicity 0.000 description 1
- 230000002588 toxic effect Effects 0.000 description 1
- YNJBWRMUSHSURL-UHFFFAOYSA-N trichloroacetic acid Chemical compound OC(=O)C(Cl)(Cl)Cl YNJBWRMUSHSURL-UHFFFAOYSA-N 0.000 description 1
- 230000001960 triggered effect Effects 0.000 description 1
- 238000009281 ultraviolet germicidal irradiation Methods 0.000 description 1
- 241001515965 unidentified phage Species 0.000 description 1
- 230000003827 upregulation Effects 0.000 description 1
- 229960005486 vaccine Drugs 0.000 description 1
- 239000004474 valine Substances 0.000 description 1
- 125000002987 valine group Chemical group [H]N([H])C([H])(C(*)=O)C([H])(C([H])([H])[H])C([H])([H])[H] 0.000 description 1
- 229940088594 vitamin Drugs 0.000 description 1
- 239000011782 vitamin Substances 0.000 description 1
- 229930003231 vitamin Natural products 0.000 description 1
- 235000013343 vitamin Nutrition 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 229910052724 xenon Inorganic materials 0.000 description 1
- FHNFHKCVQCLJFQ-UHFFFAOYSA-N xenon atom Chemical compound [Xe] FHNFHKCVQCLJFQ-UHFFFAOYSA-N 0.000 description 1
- 239000011701 zinc Substances 0.000 description 1
- 229910052725 zinc Inorganic materials 0.000 description 1
- 108010082737 zymolyase Proteins 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
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/64—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6421—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
- C12N9/6424—Serine endopeptidases (3.4.21)
- C12N9/6456—Plasminogen activators
- C12N9/6459—Plasminogen activators t-plasminogen activator (3.4.21.68), i.e. tPA
-
- 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
- C07K14/65—Insulin-like growth factors, i.e. somatomedins, e.g. IGF-1, IGF-2
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/81—Protease inhibitors
- C07K14/815—Protease inhibitors from leeches, e.g. hirudin, eglin
-
- 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
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/79—Vectors or expression systems specially adapted for eukaryotic hosts
- C12N15/80—Vectors or expression systems specially adapted for eukaryotic hosts for fungi
- C12N15/81—Vectors or expression systems specially adapted for eukaryotic hosts for fungi for yeasts
-
- 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
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/16—Hydrolases (3) acting on ester bonds (3.1)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/02—Preparation of peptides or proteins having a known sequence of two or more amino acids, e.g. glutathione
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y304/00—Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
- C12Y304/21—Serine endopeptidases (3.4.21)
- C12Y304/21069—Protein C activated (3.4.21.69)
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Genetics & Genomics (AREA)
- Engineering & Computer Science (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Molecular Biology (AREA)
- General Engineering & Computer Science (AREA)
- Biotechnology (AREA)
- Biomedical Technology (AREA)
- Microbiology (AREA)
- Medicinal Chemistry (AREA)
- Biophysics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Mycology (AREA)
- Gastroenterology & Hepatology (AREA)
- General Chemical & Material Sciences (AREA)
- Physics & Mathematics (AREA)
- Endocrinology (AREA)
- Diabetes (AREA)
- Plant Pathology (AREA)
- Tropical Medicine & Parasitology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Toxicology (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Alcoholic Beverages (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Coloring Foods And Improving Nutritive Qualities (AREA)
- Enzymes And Modification Thereof (AREA)
- Graft Or Block Polymers (AREA)
- Led Devices (AREA)
- Gyroscopes (AREA)
- Distillation Of Fermentation Liquor, Processing Of Alcohols, Vinegar And Beer (AREA)
- Acyclic And Carbocyclic Compounds In Medicinal Compositions (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GB858521496A GB8521496D0 (en) | 1985-08-29 | 1985-08-29 | Repressible yeast promoters |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| DD267739A5 true DD267739A5 (de) | 1989-05-10 |
Family
ID=10584428
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| DD31325586A DD267739A5 (de) | 1985-08-29 | 1986-08-27 | Verfahren zur Herstellung eines zu Hefe heterologen Poly-Peptids |
| DD29389486A DD254212A5 (de) | 1985-08-29 | 1986-08-27 | Verfahren zur herstellung eines hefehybrivectors, der einen oder mehrere DNS-inserts enthalt |
Family Applications After (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| DD29389486A DD254212A5 (de) | 1985-08-29 | 1986-08-27 | Verfahren zur herstellung eines hefehybrivectors, der einen oder mehrere DNS-inserts enthalt |
Country Status (22)
| Country | Link |
|---|---|
| US (1) | US5436136A (en:Method) |
| EP (1) | EP0213593B1 (en:Method) |
| JP (1) | JPH07110233B2 (en:Method) |
| AT (1) | ATE62510T1 (en:Method) |
| AU (1) | AU599329B2 (en:Method) |
| CA (1) | CA1318616C (en:Method) |
| DD (2) | DD267739A5 (en:Method) |
| DE (1) | DE3678647D1 (en:Method) |
| DK (1) | DK175093B1 (en:Method) |
| ES (3) | ES2001618A6 (en:Method) |
| FI (1) | FI91280C (en:Method) |
| GB (1) | GB8521496D0 (en:Method) |
| GR (1) | GR862209B (en:Method) |
| HU (1) | HU211207B (en:Method) |
| IE (1) | IE58844B1 (en:Method) |
| IL (1) | IL79837A (en:Method) |
| NO (1) | NO175871C (en:Method) |
| NZ (1) | NZ217388A (en:Method) |
| PH (1) | PH24715A (en:Method) |
| PT (1) | PT83273B (en:Method) |
| SU (1) | SU1630616A3 (en:Method) |
| ZA (1) | ZA866535B (en:Method) |
Families Citing this family (26)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| AU621277B2 (en) * | 1985-11-13 | 1992-03-12 | Xoma Corporation | Shortened phosphoglycerate kinase promoter |
| MY101203A (en) * | 1985-12-12 | 1991-08-17 | Ucp Gen Pharma Ag | Production of thrombin iinhibitors. |
| GB8530631D0 (en) | 1985-12-12 | 1986-01-22 | Ciba Geigy Ag | Thrombin inhibitors |
| GB8620926D0 (en) * | 1986-08-29 | 1986-10-08 | Delta Biotechnology Ltd | Yeast promoter |
| GB8907110D0 (en) * | 1988-05-04 | 1989-05-10 | Ciba Geigy Ag | Improvements in the production of polypeptides |
| NO177065C (no) * | 1988-09-26 | 1995-07-12 | Labofina Sa | Framgangsmåte for framstilling av enzymatisk aktivt humant lysozym |
| US5612198A (en) * | 1990-09-04 | 1997-03-18 | The Salk Institute | Production of insulin-like growth factor-1 in methylotrophic yeast cells |
| WO1992004363A1 (en) * | 1990-09-04 | 1992-03-19 | The Salk Institute Biotechnology/Industrial Associates, Inc. | Production of insulin-like growth factor-1 in methylotrophic yeast cells |
| AU661844B2 (en) * | 1991-04-01 | 1995-08-10 | Merck Sharp & Dohme Corp. | Genes which influence (pichia) proteolytic activity, and uses therefor |
| US5674728A (en) * | 1993-11-03 | 1997-10-07 | Novartis Corporation | Aspergillus niger vacuolar aspartyl protease |
| JPH08173170A (ja) * | 1994-05-25 | 1996-07-09 | Kirin Brewery Co Ltd | キャンディダ・ユティリス酵母の形質転換系、およびそれによる異種遺伝子の発現 |
| AU733007B2 (en) * | 1996-09-24 | 2001-05-03 | Cadus Pharmaceutical Corporation | Methods and compositions for identifying receptor effectors |
| US6265186B1 (en) | 1997-04-11 | 2001-07-24 | Dsm N.V. | Yeast cells comprising at least two copies of a desired gene integrated into the chromosomal genome at more than one non-ribosomal RNA encoding domain, particularly with Kluyveromyces |
| US6890730B1 (en) | 1999-12-10 | 2005-05-10 | The Salk Institute | Sequence and method for increasing protein expression in cellular expression systems |
| US8008459B2 (en) * | 2001-01-25 | 2011-08-30 | Evolva Sa | Concatemers of differentially expressed multiple genes |
| US9476082B2 (en) | 2010-05-20 | 2016-10-25 | Evolva Sa | Method of producing isoprenoid compounds in yeast |
| EP2822963A2 (en) | 2012-03-09 | 2015-01-14 | Vestaron Corporation | Toxic peptide production, peptide expression in plants and combinations of cysteine rich peptides |
| PT4139334T (pt) | 2020-04-20 | 2024-11-27 | Vestaron Corp | Polipéptidos variantes de u1-agatoxina-ta1b proteoliticamente estáveis para controlo de pragas |
| WO2021222814A1 (en) | 2020-05-01 | 2021-11-04 | Vestaron Corporation | Insecticidal combinations |
| AR125258A1 (es) | 2021-04-01 | 2023-06-28 | Vestaron Corp | Polipéptidos con mutaciones de av3 para el control de plagas |
| WO2023122805A1 (en) | 2021-12-20 | 2023-06-29 | Vestaron Corporation | Sorbitol driven selection pressure method |
| TW202413392A (zh) | 2022-05-18 | 2024-04-01 | 美商韋斯塔隆公司 | 殺蟲ａｃｔｘ肽變異體 |
| WO2023245100A1 (en) | 2022-06-17 | 2023-12-21 | Vestaron Corporation | Antimicrobial ncr13 variant peptides |
| WO2024026406A2 (en) | 2022-07-29 | 2024-02-01 | Vestaron Corporation | Next Generation ACTX Peptides |
| WO2024259306A2 (en) | 2023-06-16 | 2024-12-19 | Vestaron Corporation | Pvd1 variant polypeptides for pest control |
| WO2025226701A1 (en) | 2024-04-23 | 2025-10-30 | Vestaron Corporation | Proteolytically stable u1-agatoxin-ta1b variant polypeptides for pest control |
Family Cites Families (10)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB2125047B (en) * | 1982-08-09 | 1986-02-19 | Ciba Geigy Ag | Yeast hybrid vectors and their use for the production of polypeptides |
| AU577259B2 (en) * | 1982-08-13 | 1988-09-22 | Zymogenetics Inc. | Glycolytic promters for regulated protein expression protease inhibitor |
| US4876197A (en) * | 1983-02-22 | 1989-10-24 | Chiron Corporation | Eukaryotic regulatable transcription |
| NZ207926A (en) * | 1983-04-25 | 1988-04-29 | Genentech Inc | Use of yeast #a#-factor to assist in expression of proteins heterologus to yeast |
| DE3485810T2 (de) * | 1983-05-27 | 1992-12-10 | Texas A & M University Syst | Verfahren zur herstellung eines rekombinanten baculovirus-expressionsvektors. |
| GB8314961D0 (en) * | 1983-05-31 | 1983-07-06 | Kingsman A J | Dna sequence |
| PH22337A (en) * | 1983-11-21 | 1988-08-12 | Ciba Geigy Ag | Synthesis of fibrinolytic agents by yeast |
| EP0480480A3 (en) * | 1984-05-11 | 1992-06-10 | Chiron Corporation | Enhanced yeast transcription employing hybrid promoter region constructs |
| EP0164566A3 (de) * | 1984-05-11 | 1986-10-29 | LGA Gastechnik GmbH | Sicherheitseinrichtung für Flüssiggastanks |
| US4895800A (en) * | 1985-11-26 | 1990-01-23 | Phillips Petroleum Company | Yeast production of hepatitis B surface antigen |
-
1985
- 1985-08-29 GB GB858521496A patent/GB8521496D0/en active Pending
-
1986
- 1986-08-25 IL IL79837A patent/IL79837A/xx not_active IP Right Cessation
- 1986-08-25 FI FI863430A patent/FI91280C/fi not_active IP Right Cessation
- 1986-08-26 EP EP86111820A patent/EP0213593B1/en not_active Expired - Lifetime
- 1986-08-26 AT AT86111820T patent/ATE62510T1/de not_active IP Right Cessation
- 1986-08-26 DE DE8686111820T patent/DE3678647D1/de not_active Expired - Lifetime
- 1986-08-27 DD DD31325586A patent/DD267739A5/de unknown
- 1986-08-27 GR GR862209A patent/GR862209B/el unknown
- 1986-08-27 DD DD29389486A patent/DD254212A5/de not_active IP Right Cessation
- 1986-08-27 CA CA000516879A patent/CA1318616C/en not_active Expired - Lifetime
- 1986-08-28 ZA ZA866535A patent/ZA866535B/xx unknown
- 1986-08-28 PH PH34192A patent/PH24715A/en unknown
- 1986-08-28 AU AU62032/86A patent/AU599329B2/en not_active Expired
- 1986-08-28 HU HU863720A patent/HU211207B/hu unknown
- 1986-08-28 DK DK198604096A patent/DK175093B1/da not_active IP Right Cessation
- 1986-08-28 PT PT83273A patent/PT83273B/pt unknown
- 1986-08-28 NO NO863458A patent/NO175871C/no not_active IP Right Cessation
- 1986-08-28 SU SU864028035A patent/SU1630616A3/ru active
- 1986-08-28 NZ NZ217388A patent/NZ217388A/xx unknown
- 1986-08-28 IE IE230786A patent/IE58844B1/en not_active IP Right Cessation
- 1986-08-29 JP JP61201924A patent/JPH07110233B2/ja not_active Expired - Lifetime
- 1986-08-29 ES ES8601490A patent/ES2001618A6/es not_active Expired
-
1988
- 1988-03-16 ES ES8800794A patent/ES2006382A6/es not_active Expired
- 1988-03-16 ES ES8800795A patent/ES2006383A6/es not_active Expired
-
1991
- 1991-12-20 US US07/811,898 patent/US5436136A/en not_active Expired - Lifetime
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| DD267739A5 (de) | Verfahren zur Herstellung eines zu Hefe heterologen Poly-Peptids | |
| DE3111405C2 (en:Method) | ||
| DE68929115T2 (de) | Verfahren zur Herstellung von menschlichem Serumalbumin in Hefe | |
| DE69011853T3 (de) | System zur bearbeitung von hefe, welches eine zur bearbeitungsstelle benachbarte negativ geladene aminosäure beeinhaltet. | |
| DE69028448T2 (de) | Herstellung von Hämoglobin und Analogen davon durch Bakterien oder Hefen | |
| DE3586889T2 (de) | Regulatorregion fuer die expression von heterologen genen in hefe. | |
| DE3486216T2 (de) | Hybrid-DNS-Synthesis von reifen insulinähnlichen Wachstumsfaktoren. | |
| DE69232666T2 (de) | Gene, die die proteolytische aktivitaet von pichia beeinflussen und deren verwendung | |
| DE68923123T2 (de) | Herstellung von Proteinen. | |
| DE3686399T2 (de) | Herstellung von thrombin-inhibitoren. | |
| DE69130544T2 (de) | Bakterielle Vektoren | |
| DD157343A5 (de) | Mikrobielle expression von quasi-synthetischen genen | |
| DE2848053A1 (de) | Synthetische dna und verfahren zu ihrer herstellung | |
| DE68927921T2 (de) | Expression von Hepatitis B S und preS2 Proteinen in methylotrophen Hefen | |
| DE2848051A1 (de) | Synthetische dna und verfahren zu ihrer herstellung | |
| DD216044A5 (de) | Verfahren zur herstellung eines rekombinierenden dna-klonierungsvektors | |
| DE3854947T2 (de) | Neues Expressionssystem | |
| DE69013811T2 (de) | Verfahren zur Herstellung von antiviralem Protein unter Benützung von E.coli-Transformant, das Gen, das für dieses Protein kodiert und E.coli-Vektor benützt in diesem Verfahren. | |
| EP1664306A2 (de) | Sekretion von proteinen aus hefen | |
| DE69222013T2 (de) | Endoplasmatisches Retikulum-ständige rekombinante dibasische Endoprotease und deren Verwendungen | |
| JP2834111B2 (ja) | 微生物によるヒト副甲状腺ホルモンの生産 | |
| DE3689918T2 (de) | Verfahren zur Verwendung von BAR1 für die Fremdproteinsekretion. | |
| DE69735242T2 (de) | N-terminal verlängerte proteine exprimiert in hefe | |
| DE3887856T2 (de) | Methode zur Herstellung von natürlichen, menschlichen Wachstumshormon in reiner Form. | |
| DE3751081T2 (de) | [Leu 13] Motilin, dessen kodierende DNS-Moleküle und Verfahren zu dessen Herstellung. |