DD254212A5 - Verfahren zur herstellung eines hefehybrivectors, der einen oder mehrere DNS-inserts enthalt - Google Patents

Verfahren zur herstellung eines hefehybrivectors, der einen oder mehrere DNS-inserts enthalt Download PDF

Info

Publication number: DD254212A5
Authority: DD; German Democratic Republic
Prior art keywords: dna; yeast; hybrid; promoter; pho5
Prior art date: 1985-08-29

Application number

DD29389486A

Other languages

German (de)

English (en)

Inventor

Albert Hinnen

Bernd Meyhack

Original Assignee

Ciba Geigy Ag

Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)

1985-08-29

Filing date

1986-08-27

Publication date

1988-02-17

1986-08-27 Application filed by Ciba Geigy Ag filed Critical Ciba Geigy Ag

1988-02-17 Publication of DD254212A5 publication Critical patent/DD254212A5/de

Links

238000004519 manufacturing process Methods 0.000 title claims description 9
240000004808 Saccharomyces cerevisiae Species 0.000 claims abstract description 195
108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 75
102000004196 processed proteins & peptides Human genes 0.000 claims abstract description 74
229920001184 polypeptide Polymers 0.000 claims abstract description 73
238000011144 upstream manufacturing Methods 0.000 claims abstract description 50
108091026890 Coding region Proteins 0.000 claims abstract description 36
101150012394 PHO5 gene Proteins 0.000 claims abstract description 29
230000035897 transcription Effects 0.000 claims abstract description 11
238000013518 transcription Methods 0.000 claims abstract description 11
239000012634 fragment Substances 0.000 claims description 188
108090000623 proteins and genes Proteins 0.000 claims description 115
239000013612 plasmid Substances 0.000 claims description 109
239000013598 vector Substances 0.000 claims description 95
238000000034 method Methods 0.000 claims description 66
239000002773 nucleotide Substances 0.000 claims description 35
125000003729 nucleotide group Chemical group 0.000 claims description 35
108700026226 TATA Box Proteins 0.000 claims description 28
108020004445 glyceraldehyde-3-phosphate dehydrogenase Proteins 0.000 claims description 23
108010076504 Protein Sorting Signals Proteins 0.000 claims description 20
108020004414 DNA Proteins 0.000 claims description 19
108091028043 Nucleic acid sequence Proteins 0.000 claims description 19
108091026908 Downstream promoter element Proteins 0.000 claims description 14
108700009124 Transcription Initiation Site Proteins 0.000 claims description 13
101150112014 Gapdh gene Proteins 0.000 claims description 10
102000004190 Enzymes Human genes 0.000 claims description 9
108090000790 Enzymes Proteins 0.000 claims description 9
238000013519 translation Methods 0.000 claims description 9
230000022532 regulation of transcription, DNA-dependent Effects 0.000 claims description 6
230000002414 glycolytic effect Effects 0.000 claims description 5
230000004913 activation Effects 0.000 abstract description 18
230000001939 inductive effect Effects 0.000 abstract description 3
239000013604 expression vector Substances 0.000 abstract description 2
235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 130
LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 64
210000004027 cell Anatomy 0.000 description 57
ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 48
239000002609 medium Substances 0.000 description 33
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 31
206010033733 Papule Diseases 0.000 description 30
108091008146 restriction endonucleases Proteins 0.000 description 29
230000014509 gene expression Effects 0.000 description 27
230000009466 transformation Effects 0.000 description 27
239000000872 buffer Substances 0.000 description 26
238000012217 deletion Methods 0.000 description 26
239000000203 mixture Substances 0.000 description 26
230000037430 deletion Effects 0.000 description 25
108091034117 Oligonucleotide Proteins 0.000 description 24
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 description 24
239000011543 agarose gel Substances 0.000 description 22
108090000723 Insulin-Like Growth Factor I Proteins 0.000 description 21
101000702488 Rattus norvegicus High affinity cationic amino acid transporter 1 Proteins 0.000 description 21
229940024606 amino acid Drugs 0.000 description 21
150000001413 amino acids Chemical class 0.000 description 21
108010073652 desirudin Proteins 0.000 description 21
HEDRZPFGACZZDS-UHFFFAOYSA-N Chloroform Chemical compound ClC(Cl)Cl HEDRZPFGACZZDS-UHFFFAOYSA-N 0.000 description 20
241000588724 Escherichia coli Species 0.000 description 20
102000004218 Insulin-Like Growth Factor I Human genes 0.000 description 20
102100031181 Glyceraldehyde-3-phosphate dehydrogenase Human genes 0.000 description 19
210000005253 yeast cell Anatomy 0.000 description 19
IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 18
238000010276 construction Methods 0.000 description 18
238000002955 isolation Methods 0.000 description 18
239000007983 Tris buffer Substances 0.000 description 17
238000012869 ethanol precipitation Methods 0.000 description 17
239000000499 gel Substances 0.000 description 17
LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 17
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 16
230000029087 digestion Effects 0.000 description 16
239000000047 product Substances 0.000 description 16
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 15
102000012410 DNA Ligases Human genes 0.000 description 15
108010061982 DNA Ligases Proteins 0.000 description 15
238000004458 analytical method Methods 0.000 description 15
230000000694 effects Effects 0.000 description 15
238000000605 extraction Methods 0.000 description 15
102000004169 proteins and genes Human genes 0.000 description 15
239000011780 sodium chloride Substances 0.000 description 15
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 13
102000003978 Tissue Plasminogen Activator Human genes 0.000 description 13
108090000373 Tissue Plasminogen Activator Proteins 0.000 description 13
239000003550 marker Substances 0.000 description 13
229960000187 tissue plasminogen activator Drugs 0.000 description 13
241001131785 Escherichia coli HB101 Species 0.000 description 12
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
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 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
230000001580 bacterial effect Effects 0.000 description 12
239000008103 glucose Substances 0.000 description 12
235000015097 nutrients Nutrition 0.000 description 12
230000008929 regeneration Effects 0.000 description 12
238000011069 regeneration method Methods 0.000 description 12
210000002421 cell wall Anatomy 0.000 description 11
230000006870 function Effects 0.000 description 11
229910052799 carbon Inorganic materials 0.000 description 10
238000003776 cleavage reaction Methods 0.000 description 10
230000007017 scission Effects 0.000 description 10
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 10
OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 9
108020004999 messenger RNA Proteins 0.000 description 9
229910052757 nitrogen Inorganic materials 0.000 description 9
230000001105 regulatory effect Effects 0.000 description 9
229920001817 Agar Polymers 0.000 description 8
HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 8
108700026244 Open Reading Frames Proteins 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
238000000246 agarose gel electrophoresis Methods 0.000 description 8
229940088598 enzyme Drugs 0.000 description 8
238000000746 purification Methods 0.000 description 8
108060002716 Exonuclease Proteins 0.000 description 7
108700039691 Genetic Promoter Regions Proteins 0.000 description 7
239000011575 calcium Substances 0.000 description 7
102000013165 exonuclease Human genes 0.000 description 7
229940079322 interferon Drugs 0.000 description 7
238000002844 melting Methods 0.000 description 7
238000002360 preparation method Methods 0.000 description 7
230000010076 replication Effects 0.000 description 7
150000003839 salts Chemical class 0.000 description 7
239000000243 solution Substances 0.000 description 7
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
102000003960 Ligases Human genes 0.000 description 6
108090000364 Ligases Proteins 0.000 description 6
229910052791 calcium Inorganic materials 0.000 description 6
238000000855 fermentation Methods 0.000 description 6
230000004151 fermentation Effects 0.000 description 6
230000004927 fusion Effects 0.000 description 6
230000008018 melting Effects 0.000 description 6
230000008569 process Effects 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
108020005065 3' Flanking Region Proteins 0.000 description 5
102000013563 Acid Phosphatase Human genes 0.000 description 5
108010051457 Acid Phosphatase Proteins 0.000 description 5
108010014303 DNA-directed DNA polymerase Proteins 0.000 description 5
102000016928 DNA-directed DNA polymerase Human genes 0.000 description 5
108010007267 Hirudins Proteins 0.000 description 5
ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 5
108091036060 Linker DNA Proteins 0.000 description 5
108010021757 Polynucleotide 5'-Hydroxyl-Kinase Proteins 0.000 description 5
102000008422 Polynucleotide 5'-hydroxyl-kinase Human genes 0.000 description 5
VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 5
239000000427 antigen Substances 0.000 description 5
108091007433 antigens Proteins 0.000 description 5
102000036639 antigens Human genes 0.000 description 5
238000006243 chemical reaction Methods 0.000 description 5
210000000349 chromosome Anatomy 0.000 description 5
238000010367 cloning Methods 0.000 description 5
239000001963 growth medium Substances 0.000 description 5
238000004255 ion exchange chromatography Methods 0.000 description 5
238000001556 precipitation Methods 0.000 description 5
238000012545 processing Methods 0.000 description 5
238000004007 reversed phase HPLC Methods 0.000 description 5
239000001632 sodium acetate Substances 0.000 description 5
235000017281 sodium acetate Nutrition 0.000 description 5
239000000758 substrate Substances 0.000 description 5
-1 vaccines Proteins 0.000 description 5
102000053602 DNA Human genes 0.000 description 4
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
102000007625 Hirudins Human genes 0.000 description 4
102000014150 Interferons Human genes 0.000 description 4
108010050904 Interferons Proteins 0.000 description 4
DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 4
229910019142 PO4 Inorganic materials 0.000 description 4
108020005091 Replication Origin Proteins 0.000 description 4
239000011324 bead Substances 0.000 description 4
230000001419 dependent effect Effects 0.000 description 4
238000000502 dialysis Methods 0.000 description 4
239000000284 extract Substances 0.000 description 4
230000002068 genetic effect Effects 0.000 description 4
239000011521 glass 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
229960002885 histidine Drugs 0.000 description 4
238000000338 in vitro Methods 0.000 description 4
238000011534 incubation Methods 0.000 description 4
150000002500 ions Chemical class 0.000 description 4
229940046166 oligodeoxynucleotide Drugs 0.000 description 4
230000036961 partial effect Effects 0.000 description 4
230000009467 reduction Effects 0.000 description 4
239000000126 substance Substances 0.000 description 4
230000005026 transcription initiation Effects 0.000 description 4
WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 3
108010054576 Deoxyribonuclease EcoRI Proteins 0.000 description 3
PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
239000002202 Polyethylene glycol Substances 0.000 description 3
238000012300 Sequence Analysis Methods 0.000 description 3
239000008051 TBE buffer Substances 0.000 description 3
241000700605 Viruses Species 0.000 description 3
244000309466 calf Species 0.000 description 3
239000013611 chromosomal DNA Substances 0.000 description 3
238000010586 diagram Methods 0.000 description 3
108010031145 eglin proteinase inhibitors Proteins 0.000 description 3
230000002255 enzymatic effect Effects 0.000 description 3
238000010353 genetic engineering Methods 0.000 description 3
230000012010 growth Effects 0.000 description 3
230000001976 improved effect Effects 0.000 description 3
229910052816 inorganic phosphate Inorganic materials 0.000 description 3
238000005342 ion exchange Methods 0.000 description 3
239000007788 liquid Substances 0.000 description 3
230000037361 pathway Effects 0.000 description 3
239000010452 phosphate Substances 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
230000003362 replicative effect Effects 0.000 description 3
230000003248 secreting effect Effects 0.000 description 3
238000012163 sequencing technique Methods 0.000 description 3
239000006228 supernatant Substances 0.000 description 3
230000005030 transcription termination Effects 0.000 description 3
230000001131 transforming effect Effects 0.000 description 3
230000014621 translational initiation Effects 0.000 description 3
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
229920000936 Agarose Polymers 0.000 description 2
102000002260 Alkaline Phosphatase Human genes 0.000 description 2
108020004774 Alkaline Phosphatase Proteins 0.000 description 2
NLXLAEXVIDQMFP-UHFFFAOYSA-N Ammonia chloride Chemical compound [NH4+].[Cl-] NLXLAEXVIDQMFP-UHFFFAOYSA-N 0.000 description 2
102000015081 Blood Coagulation Factors Human genes 0.000 description 2
108010039209 Blood Coagulation Factors Proteins 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
108020004705 Codon Proteins 0.000 description 2
108010042407 Endonucleases Proteins 0.000 description 2
241000701959 Escherichia virus Lambda Species 0.000 description 2
101150077230 GAL4 gene Proteins 0.000 description 2
108010056771 Glucosidases Proteins 0.000 description 2
102000004366 Glucosidases Human genes 0.000 description 2
241000700721 Hepatitis B virus Species 0.000 description 2
108060003951 Immunoglobulin Proteins 0.000 description 2
XEEYBQQBJWHFJM-UHFFFAOYSA-N Iron Chemical compound [Fe] XEEYBQQBJWHFJM-UHFFFAOYSA-N 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
101710163270 Nuclease Proteins 0.000 description 2
102000004160 Phosphoric Monoester Hydrolases Human genes 0.000 description 2
108090000608 Phosphoric Monoester Hydrolases Proteins 0.000 description 2
101100173636 Rattus norvegicus Fhl2 gene Proteins 0.000 description 2
229920005654 Sephadex Polymers 0.000 description 2
239000012507 Sephadex™ Substances 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
102000003990 Urokinase-type plasminogen activator Human genes 0.000 description 2
108090000435 Urokinase-type plasminogen activator Proteins 0.000 description 2
238000009825 accumulation Methods 0.000 description 2
239000002253 acid Substances 0.000 description 2
230000003213 activating effect Effects 0.000 description 2
150000003863 ammonium salts Chemical class 0.000 description 2
235000011130 ammonium sulphate Nutrition 0.000 description 2
229960001230 asparagine Drugs 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
229940041514 candida albicans extract Drugs 0.000 description 2
238000005119 centrifugation Methods 0.000 description 2
238000012512 characterization method Methods 0.000 description 2
238000004587 chromatography analysis Methods 0.000 description 2
230000000295 complement effect Effects 0.000 description 2
238000007796 conventional method 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
230000006378 damage Effects 0.000 description 2
238000013461 design Methods 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
239000012530 fluid Substances 0.000 description 2
238000009472 formulation Methods 0.000 description 2
238000001502 gel electrophoresis Methods 0.000 description 2
102000034356 gene-regulatory proteins Human genes 0.000 description 2
108091006104 gene-regulatory proteins Proteins 0.000 description 2
230000013595 glycosylation Effects 0.000 description 2
238000006206 glycosylation reaction Methods 0.000 description 2
239000003102 growth factor Substances 0.000 description 2
239000007952 growth promoter Substances 0.000 description 2
238000009396 hybridization Methods 0.000 description 2
102000018358 immunoglobulin Human genes 0.000 description 2
238000001727 in vivo Methods 0.000 description 2
230000002779 inactivation Effects 0.000 description 2
NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 2
239000000543 intermediate Substances 0.000 description 2
210000000936 intestine Anatomy 0.000 description 2
238000007069 methylation reaction Methods 0.000 description 2
244000005700 microbiome Species 0.000 description 2
230000035772 mutation Effects 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
239000002243 precursor Substances 0.000 description 2
230000006798 recombination Effects 0.000 description 2
238000005215 recombination Methods 0.000 description 2
230000002829 reductive effect Effects 0.000 description 2
238000011160 research 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
239000007787 solid Substances 0.000 description 2
239000005720 sucrose Substances 0.000 description 2
238000012360 testing method Methods 0.000 description 2
239000011573 trace mineral Substances 0.000 description 2
235000013619 trace mineral Nutrition 0.000 description 2
230000002103 transcriptional effect Effects 0.000 description 2
238000010361 transduction Methods 0.000 description 2
230000026683 transduction Effects 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
AZUYLZMQTIKGSC-UHFFFAOYSA-N 1-[6-[4-(5-chloro-6-methyl-1H-indazol-4-yl)-5-methyl-3-(1-methylindazol-5-yl)pyrazol-1-yl]-2-azaspiro[3.3]heptan-2-yl]prop-2-en-1-one Chemical compound ClC=1C(=C2C=NNC2=CC=1C)C=1C(=NN(C=1C)C1CC2(CN(C2)C(C=C)=O)C1)C=1C=C2C=NN(C2=CC=1)C AZUYLZMQTIKGSC-UHFFFAOYSA-N 0.000 description 1
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
102100027324 2-hydroxyacyl-CoA lyase 1 Human genes 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
108020005029 5' Flanking Region Proteins 0.000 description 1
101710163881 5,6-dihydroxyindole-2-carboxylic acid oxidase 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
101000583086 Bunodosoma granuliferum Delta-actitoxin-Bgr2b Proteins 0.000 description 1
108091028026 C-DNA Proteins 0.000 description 1
108010072454 CTGCAG-specific type II deoxyribonucleases Proteins 0.000 description 1
101100011368 Caenorhabditis elegans egl-1 gene Proteins 0.000 description 1
101100011376 Caenorhabditis elegans egl-5 gene Proteins 0.000 description 1
102000005572 Cathepsin A Human genes 0.000 description 1
108010059081 Cathepsin A Proteins 0.000 description 1
108020004638 Circular DNA Proteins 0.000 description 1
108091062157 Cis-regulatory element Proteins 0.000 description 1
102100022641 Coagulation factor IX Human genes 0.000 description 1
108091033380 Coding strand Proteins 0.000 description 1
108010062580 Concanavalin A 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
108010005054 Deoxyribonuclease BamHI Proteins 0.000 description 1
102100031780 Endonuclease Human genes 0.000 description 1
102000004533 Endonucleases Human genes 0.000 description 1
102000005593 Endopeptidases Human genes 0.000 description 1
108010059378 Endopeptidases Proteins 0.000 description 1
108091092566 Extrachromosomal DNA Proteins 0.000 description 1
108010076282 Factor IX Proteins 0.000 description 1
108010054218 Factor VIII Proteins 0.000 description 1
102000001690 Factor VIII Human genes 0.000 description 1
101150094690 GAL1 gene Proteins 0.000 description 1
101150038242 GAL10 gene Proteins 0.000 description 1
102100028501 Galanin peptides Human genes 0.000 description 1
102100024637 Galectin-10 Human genes 0.000 description 1
102100039555 Galectin-7 Human genes 0.000 description 1
241000237858 Gastropoda Species 0.000 description 1
108010021582 Glucokinase Proteins 0.000 description 1
102000005731 Glucose-6-phosphate isomerase Human genes 0.000 description 1
108010070600 Glucose-6-phosphate isomerase Proteins 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
101001009252 Homo sapiens 2-hydroxyacyl-CoA lyase 1 Proteins 0.000 description 1
101100121078 Homo sapiens GAL gene Proteins 0.000 description 1
101000608772 Homo sapiens Galectin-7 Proteins 0.000 description 1
101000878605 Homo sapiens Low affinity immunoglobulin epsilon Fc receptor Proteins 0.000 description 1
101000950847 Homo sapiens Macrophage migration inhibitory factor Proteins 0.000 description 1
101000851058 Homo sapiens Neutrophil elastase Proteins 0.000 description 1
101100477520 Homo sapiens SHOX gene Proteins 0.000 description 1
108010000521 Human Growth Hormone 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
102000004877 Insulin Human genes 0.000 description 1
108090001061 Insulin Proteins 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
108010090665 Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase Proteins 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
101100285000 Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) his-3 gene Proteins 0.000 description 1
102100033174 Neutrophil elastase Human genes 0.000 description 1
NHNBFGGVMKEFGY-UHFFFAOYSA-N Nitrate Chemical compound [O-][N+]([O-])=O NHNBFGGVMKEFGY-UHFFFAOYSA-N 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
108010069341 Phosphofructokinases Proteins 0.000 description 1
102000001105 Phosphofructokinases Human genes 0.000 description 1
108091000080 Phosphotransferase Proteins 0.000 description 1
102000001938 Plasminogen Activators Human genes 0.000 description 1
108010001014 Plasminogen Activators Proteins 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
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
108090000783 Renin Proteins 0.000 description 1
102100028255 Renin Human genes 0.000 description 1
241000223252 Rhodotorula Species 0.000 description 1
241000235070 Saccharomyces Species 0.000 description 1
101100539892 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) USA1 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
102100032491 Serine protease 1 Human genes 0.000 description 1
102000048489 Short Stature Homeobox Human genes 0.000 description 1
108700025071 Short Stature Homeobox Proteins 0.000 description 1
108020004682 Single-Stranded DNA Proteins 0.000 description 1
102000013275 Somatomedins Human genes 0.000 description 1
102000005157 Somatostatin Human genes 0.000 description 1
108010056088 Somatostatin Proteins 0.000 description 1
101000895926 Streptomyces plicatus Endo-beta-N-acetylglucosaminidase H 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
101150006914 TRP1 gene Proteins 0.000 description 1
239000004098 Tetracycline Substances 0.000 description 1
108090000190 Thrombin 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
229920004890 Triton X-100 Polymers 0.000 description 1
239000013504 Triton X-100 Substances 0.000 description 1
108060008682 Tumor Necrosis Factor Proteins 0.000 description 1
108020005202 Viral DNA Proteins 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
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
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
230000003698 anagen phase Effects 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
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
229940019700 blood coagulation factors Drugs 0.000 description 1
108010006025 bovine growth hormone Proteins 0.000 description 1
238000009395 breeding Methods 0.000 description 1
230000001488 breeding effect Effects 0.000 description 1
210000004899 c-terminal region Anatomy 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
230000006037 cell lysis Effects 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
239000003795 chemical substances by application Substances 0.000 description 1
150000001805 chlorine compounds Chemical class 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
150000001875 compounds Chemical class 0.000 description 1
238000001816 cooling Methods 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
230000002498 deadly effect 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
230000003292 diminished effect Effects 0.000 description 1
238000009826 distribution Methods 0.000 description 1
101150057929 egl-4 gene Proteins 0.000 description 1
239000003480 eluent Substances 0.000 description 1
238000005516 engineering process Methods 0.000 description 1
239000003623 enhancer 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
230000001036 exonucleolytic effect Effects 0.000 description 1
239000013613 expression plasmid Substances 0.000 description 1
229960004222 factor ix Drugs 0.000 description 1
229960000301 factor viii Drugs 0.000 description 1
230000002349 favourable effect Effects 0.000 description 1
235000011389 fruit/vegetable juice Nutrition 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
108010087005 glusulase Proteins 0.000 description 1
125000003147 glycosyl group Chemical group 0.000 description 1
239000000122 growth hormone Substances 0.000 description 1
239000003630 growth substance Substances 0.000 description 1
208000006454 hepatitis Diseases 0.000 description 1
231100000283 hepatitis Toxicity 0.000 description 1
238000004128 high performance liquid chromatography Methods 0.000 description 1
210000003630 histaminocyte Anatomy 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
238000010348 incorporation Methods 0.000 description 1
230000002401 inhibitory effect Effects 0.000 description 1
230000005764 inhibitory process Effects 0.000 description 1
238000003780 insertion Methods 0.000 description 1
230000037431 insertion Effects 0.000 description 1
229940125396 insulin Drugs 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
230000000968 intestinal effect Effects 0.000 description 1
PGLTVOMIXTUURA-UHFFFAOYSA-N iodoacetamide Chemical compound NC(=O)CI PGLTVOMIXTUURA-UHFFFAOYSA-N 0.000 description 1
238000010849 ion bombardment Methods 0.000 description 1
229910052742 iron Inorganic materials 0.000 description 1
238000001155 isoelectric focusing Methods 0.000 description 1
238000002372 labelling Methods 0.000 description 1
239000008101 lactose Substances 0.000 description 1
238000011031 large-scale manufacturing process Methods 0.000 description 1
230000003902 lesion Effects 0.000 description 1
229920002521 macromolecule Polymers 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
230000002906 microbiologic effect 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
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
210000005036 nerve Anatomy 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
DDBREPKUVSBGFI-UHFFFAOYSA-N phenobarbital Chemical compound C=1C=CC=CC=1C1(CC)C(=O)NC(=O)NC1=O DDBREPKUVSBGFI-UHFFFAOYSA-N 0.000 description 1
150000003013 phosphoric acid derivatives Chemical class 0.000 description 1
102000020233 phosphotransferase Human genes 0.000 description 1
229940127126 plasminogen activator Drugs 0.000 description 1
238000002264 polyacrylamide gel electrophoresis Methods 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
230000002265 prevention Effects 0.000 description 1
210000001236 prokaryotic cell Anatomy 0.000 description 1
210000001938 protoplast Anatomy 0.000 description 1
238000003127 radioimmunoassay Methods 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
239000011347 resin Substances 0.000 description 1
229920005989 resin Polymers 0.000 description 1
238000004366 reverse phase liquid chromatography Methods 0.000 description 1
239000007320 rich medium Substances 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
238000010008 shearing Methods 0.000 description 1
238000004904 shortening Methods 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
239000007974 sodium acetate buffer Substances 0.000 description 1
239000012064 sodium phosphate buffer Substances 0.000 description 1
NHXLMOGPVYXJNR-ATOGVRKGSA-N somatostatin Chemical compound C([C@H]1C(=O)N[C@H](C(N[C@@H](CO)C(=O)N[C@@H](CSSC[C@@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@@H](CC=2C3=CC=CC=C3NC=2)C(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(=O)N1)[C@@H](C)O)NC(=O)CNC(=O)[C@H](C)N)C(O)=O)=O)[C@H](O)C)C1=CC=CC=C1 NHXLMOGPVYXJNR-ATOGVRKGSA-N 0.000 description 1
229960000553 somatostatin Drugs 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
241000894007 species Species 0.000 description 1
230000007480 spreading Effects 0.000 description 1
238000003892 spreading Methods 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
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
238000000844 transformation Methods 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
GPRLSGONYQIRFK-MNYXATJNSA-N triton Chemical compound [3H+] GPRLSGONYQIRFK-MNYXATJNSA-N 0.000 description 1
102000003390 tumor necrosis factor Human genes 0.000 description 1
238000009281 ultraviolet germicidal irradiation Methods 0.000 description 1
229960005486 vaccine Drugs 0.000 description 1
239000011782 vitamin Substances 0.000 description 1
229940088594 vitamin Drugs 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)
General Engineering & Computer Science (AREA)
Molecular Biology (AREA)
Biomedical Technology (AREA)
Biotechnology (AREA)
Microbiology (AREA)
Medicinal Chemistry (AREA)
Biophysics (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Mycology (AREA)
Gastroenterology & Hepatology (AREA)
Diabetes (AREA)
Tropical Medicine & Parasitology (AREA)
Physics & Mathematics (AREA)
Chemical Kinetics & Catalysis (AREA)
General Chemical & Material Sciences (AREA)
Endocrinology (AREA)
Toxicology (AREA)
Plant Pathology (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)
Gyroscopes (AREA)
Led Devices (AREA)
Graft Or Block Polymers (AREA)
Enzymes And Modification Thereof (AREA)
Acyclic And Carbocyclic Compounds In Medicinal Compositions (AREA)
Distillation Of Fermentation Liquor, Processing Of Alcohols, Vinegar And Beer (AREA)

DD29389486A 1985-08-29 1986-08-27 Verfahren zur herstellung eines hefehybrivectors, der einen oder mehrere DNS-inserts enthalt DD254212A5 (de)

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
DD254212A5 true DD254212A5 (de)	1988-02-17

Family

ID=10584428

Family Applications (2)

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
DD31325586A DD267739A5 (de)	1985-08-29	1986-08-27	Verfahren zur Herstellung eines zu Hefe heterologen Poly-Peptids

Family Applications After (1)

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

Country Status (22)

Country	Link
US (1)	US5436136A (fr)
EP (1)	EP0213593B1 (fr)
JP (1)	JPH07110233B2 (fr)
AT (1)	ATE62510T1 (fr)
AU (1)	AU599329B2 (fr)
CA (1)	CA1318616C (fr)
DD (2)	DD254212A5 (fr)
DE (1)	DE3678647D1 (fr)
DK (1)	DK175093B1 (fr)
ES (3)	ES2001618A6 (fr)
FI (1)	FI91280C (fr)
GB (1)	GB8521496D0 (fr)
GR (1)	GR862209B (fr)
HU (1)	HU211207B (fr)
IE (1)	IE58844B1 (fr)
IL (1)	IL79837A (fr)
NO (1)	NO175871C (fr)
NZ (1)	NZ217388A (fr)
PH (1)	PH24715A (fr)
PT (1)	PT83273B (fr)
SU (1)	SU1630616A3 (fr)
ZA (1)	ZA866535B (fr)

Families Citing this family (23)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
AU621277B2 (en) *	1985-11-13	1992-03-12	Xoma Corporation	Shortened phosphoglycerate kinase promoter
GB8530631D0 (en)	1985-12-12	1986-01-22	Ciba Geigy Ag	Thrombin inhibitors
MY101203A (en) *	1985-12-12	1991-08-17	Ucp Gen Pharma Ag	Production of thrombin iinhibitors.
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
JPH06500470A (ja) *	1990-09-04	1994-01-20	メルク　エンド　カンパニー　インコーポレーテッド	メチロトローフ酵母細胞におけるインスリン様成長因子の産生
US5612198A (en) *	1990-09-04	1997-03-18	The Salk Institute	Production of insulin-like growth factor-1 in methylotrophic yeast cells
ATE220105T1 (de) *	1991-04-01	2002-07-15	Merck & Co Inc	Gene, die die proteolytische aktivitaet von pichia beeinflussen und deren verwendung
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
ATE284972T1 (de) *	1996-09-24	2005-01-15	Cadus Pharmaceutical Corp	Verfahren und zusammensetzungen für die identifizierung von receptor effectoren
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
EP2571991A1 (fr)	2010-05-20	2013-03-27	Evolva SA	Procédé de fabrication de composés isoprénoïdes dans une levure
PE20231212A1 (es)	2020-04-20	2023-08-17	Vestaron Corp	Polipeptidos variantes proteoliticamente estables de u1-agatoxina-ta1b para el control de plagas
TW202205956A (zh)	2020-05-01	2022-02-16	美商韋斯塔隆公司	殺蟲組合
CA3215602A1 (fr)	2021-04-01	2022-10-06	Vestaron Corporation	Polypeptides mutants av3 destines a la lutte antiparasitaire
WO2023122805A1 (fr)	2021-12-20	2023-06-29	Vestaron Corporation	Procédé de pression de sélection par sorbitol
WO2023225555A1 (fr)	2022-05-18	2023-11-23	Vestaron Corporation	Variants peptidiques d'actx pesticides
WO2023245100A1 (fr)	2022-06-17	2023-12-21	Vestaron Corporation	Peptides variants de ncr13 antimicrobiens
WO2024026406A2 (fr)	2022-07-29	2024-02-01	Vestaron Corporation	Peptides actx de nouvelle génération

Family Cites Families (10)

* Cited by examiner, † Cited by third party
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
DE3479520D1 (en) *	1983-11-21	1989-09-28	Ciba Geigy Ag	Synthesis of tissue plasminogen activator(tpa) by yeast
EP0164556B1 (fr) *	1984-05-11	1994-03-02	Chiron Corporation	Transcription augmentée dans les levures par usage d'une construction hybride de la région du promoteur
EP0164566A3 (fr) *	1984-05-11	1986-10-29	LGA Gastechnik GmbH	Dispositif de sécurité pour réservoirs de gaz liquéfié
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 FI FI863430A patent/FI91280C/fi not_active IP Right Cessation
- 1986-08-25 IL IL79837A patent/IL79837A/xx not_active IP Right Cessation
- 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
- 1986-08-26 EP EP86111820A patent/EP0213593B1/fr not_active Expired - Lifetime
- 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/fr not_active Expired - Lifetime
- 1986-08-27 DD DD31325586A patent/DD267739A5/de unknown
- 1986-08-28 PT PT83273A patent/PT83273B/pt unknown
- 1986-08-28 NZ NZ217388A patent/NZ217388A/xx unknown
- 1986-08-28 PH PH34192A patent/PH24715A/en unknown
- 1986-08-28 NO NO863458A patent/NO175871C/no not_active IP Right Cessation
- 1986-08-28 ZA ZA866535A patent/ZA866535B/xx unknown
- 1986-08-28 IE IE230786A patent/IE58844B1/en not_active IP Right Cessation
- 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 AU AU62032/86A patent/AU599329B2/en not_active Expired
- 1986-08-28 SU SU864028035A patent/SU1630616A3/ru active
- 1986-08-29 ES ES8601490A patent/ES2001618A6/es not_active Expired
- 1986-08-29 JP JP61201924A patent/JPH07110233B2/ja not_active Expired - Lifetime
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

Publication number	Publication date
US5436136A (en)	1995-07-25
FI863430A0 (fi)	1986-08-25
NO863458L (no)	1987-03-02
NO175871C (no)	1994-12-21
ATE62510T1 (de)	1991-04-15
FI91280B (fi)	1994-02-28
HU211207B (en)	1995-11-28
EP0213593B1 (fr)	1991-04-10
DK409686D0 (da)	1986-08-28
JPS6251995A (ja)	1987-03-06
PH24715A (en)	1990-10-01
NO863458D0 (no)	1986-08-28
DE3678647D1 (en)	1991-05-16
ES2006383A6 (es)	1989-04-16
ZA866535B (en)	1987-04-29
IE58844B1 (en)	1993-11-17
FI91280C (fi)	1994-06-10
GB8521496D0 (en)	1985-10-02
AU6203286A (en)	1987-03-05
EP0213593A1 (fr)	1987-03-11
FI863430A (fi)	1987-03-01
JPH07110233B2 (ja)	1995-11-29
CA1318616C (fr)	1993-06-01
DD267739A5 (de)	1989-05-10
GR862209B (en)	1986-12-31
PT83273A (en)	1986-09-01
IL79837A0 (en)	1986-11-30
IE862307L (en)	1987-02-28
NZ217388A (en)	1989-02-24
AU599329B2 (en)	1990-07-19
ES2006382A6 (es)	1989-04-16
HUT42525A (en)	1987-07-28
DK175093B1 (da)	2004-05-24
IL79837A (en)	1992-06-21
DK409686A (da)	1987-03-01
PT83273B (pt)	1989-05-12
NO175871B (fr)	1994-09-12
SU1630616A3 (ru)	1991-02-23
ES2001618A6 (es)	1988-06-01

Legal Events

Date	Code	Title	Description
2000-02-03	ENJ	Ceased due to non-payment of renewal fee

Publication	Publication Date	Title
DD254212A5 (de)	1988-02-17	Verfahren zur herstellung eines hefehybrivectors, der einen oder mehrere DNS-inserts enthalt
DE69011853T3 (de)	1998-06-25	System zur bearbeitung von hefe, welches eine zur bearbeitungsstelle benachbarte negativ geladene aminosäure beeinhaltet.
DE69018920T2 (de)	1995-09-07	Verwendung von dns-fragmenten, die ein signalpeptid kodieren zur sekretion von reifen proteinen in rekombinanten hefen, expressions-kassetten, transformierte hefen und verfahren zur herstellung dieser proteine.
DE3280422T2 (de)	1993-05-27	Verfahren und produkte zur leichten mikrobiologischen expression von dns-sequenzen.
DE68925893T2 (de)	1996-08-08	Sekretorische leader-sequenzen
DE68923123T2 (de)	1995-11-30	Herstellung von Proteinen.
DE3050722C2 (fr)	1987-09-24
DE3308215C2 (de)	1994-01-27	Expression, Processing und Sekretion von heterologem Protein durch Hefe
DE3886408T2 (de)	1994-05-11	Synthetische hefe-signalpeptide.
DD218118A5 (de)	1985-01-30	Verfahren zur herstellung eines hefe- oder nichthefepolypeptids
DE3686399T2 (de)	1993-01-14	Herstellung von thrombin-inhibitoren.
DE2848053A1 (de)	1979-05-10	Synthetische dna und verfahren zu ihrer herstellung
DE3752063T2 (de)	1997-12-04	Funktioneller DNS-Block und für Hirudin kodierendes Plasmid, transformierte Hefe aud Verfahren zur Herstellung von Hirudin.
JPH07222595A (ja)	1995-08-22	置換されたプロモーターを使用する宿主による異種起源蛋白質の製造方法
DE3854947T2 (de)	1996-11-14	Neues Expressionssystem
DE58907266T2 (de)	1994-09-29	Polypeptide mit einer die Koagulierung hemmenden Wirkung.
JP2834111B2 (ja)	1998-12-09	微生物によるヒト副甲状腺ホルモンの生産
DE69735242T2 (de)	2006-09-21	N-terminal verlängerte proteine exprimiert in hefe
DE3689918T2 (de)	1994-10-20	Verfahren zur Verwendung von BAR1 für die Fremdproteinsekretion.
DE3587205T2 (de)	1993-08-26	Verfahren zur herstellung eines proteins und dafuer zu verwendender vektor, rekombinante dns und transformierte zelle.
DE69634757T2 (de)	2006-02-02	Vektor zur expression von n-terminal verlängerten proteinen in hefezellen
DD210466A5 (de)	1984-06-13	Verfahren zur herstellung eines rekombinanten plasmids
DD274053A5 (de)	1989-12-06	Verfahren zur Produktion eines menschlichen, einkettigen Plasminogenaktivators
DE3878410T2 (de)	1993-06-03	Verfahren zur erhoehung von gen-expression.
DE69121489T2 (de)	1997-02-27	In vitro-Behandlung von Fusionsproteinen