NO841130L - Ledersekvens for aa fremme sekresjon av genprodukter - Google Patents

Ledersekvens for aa fremme sekresjon av genprodukter

Info

Publication number: NO841130L
Authority: NO; Norway
Prior art keywords: transfer vector; stated; leader sequence; gene; structural gene
Prior art date: 1983-03-28

Application number

NO841130A

Other languages

English (en)

Norwegian (no)

Inventor

Anthony Atkinson

Nigel Peter Minton

Roger Franklin Sherwood

Original Assignee

Health Lab Service Board

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.)

1983-03-28

Filing date

1984-03-22

Publication date

1984-10-01

1984-03-22 Application filed by Health Lab Service Board filed Critical Health Lab Service Board

1984-10-01 Publication of NO841130L publication Critical patent/NO841130L/no

Links

230000001737 promoting effect Effects 0.000 title 1
108090000623 proteins and genes Proteins 0.000 claims description 110
239000013612 plasmid Substances 0.000 claims description 55
239000013598 vector Substances 0.000 claims description 47
238000012546 transfer Methods 0.000 claims description 44
229920001184 polypeptide Polymers 0.000 claims description 42
102000004196 processed proteins & peptides Human genes 0.000 claims description 42
108090000765 processed proteins & peptides Proteins 0.000 claims description 42
108091033319 polynucleotide Proteins 0.000 claims description 38
239000002157 polynucleotide Substances 0.000 claims description 38
102000040430 polynucleotide Human genes 0.000 claims description 38
241000588724 Escherichia coli Species 0.000 claims description 35
241000589516 Pseudomonas Species 0.000 claims description 22
239000002773 nucleotide Substances 0.000 claims description 11
240000004808 Saccharomyces cerevisiae Species 0.000 claims description 10
108020004511 Recombinant DNA Proteins 0.000 claims description 9
230000001580 bacterial effect Effects 0.000 claims description 8
238000011144 upstream manufacturing Methods 0.000 claims description 7
108010006303 Carboxypeptidases Proteins 0.000 claims description 4
102000005367 Carboxypeptidases Human genes 0.000 claims description 4
101000976075 Homo sapiens Insulin Proteins 0.000 claims description 3
102000002265 Human Growth Hormone Human genes 0.000 claims description 3
108010000521 Human Growth Hormone Proteins 0.000 claims description 3
239000000854 Human Growth Hormone Substances 0.000 claims description 3
102000004576 Placental Lactogen Human genes 0.000 claims description 3
108010003044 Placental Lactogen Proteins 0.000 claims description 3
239000000381 Placental Lactogen Substances 0.000 claims description 3
PBGKTOXHQIOBKM-FHFVDXKLSA-N insulin (human) Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@H]1CSSC[C@H]2C(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@H](C(=O)N[C@H](C(N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=3C=CC(O)=CC=3)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=3NC=NC=3)NC(=O)[C@H](CO)NC(=O)CNC1=O)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)NCC(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H]([C@@H](C)O)C(O)=O)C(=O)N[C@@H](CC(N)=O)C(O)=O)=O)CSSC[C@@H](C(N2)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@@H](NC(=O)CN)[C@@H](C)CC)[C@@H](C)CC)[C@@H](C)O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](NC(=O)[C@@H](N)CC=1C=CC=CC=1)C(C)C)C1=CN=CN1 PBGKTOXHQIOBKM-FHFVDXKLSA-N 0.000 claims description 2
102000004169 proteins and genes Human genes 0.000 description 48
235000018102 proteins Nutrition 0.000 description 47
239000012634 fragment Substances 0.000 description 36
101000624947 Homo sapiens Nesprin-1 Proteins 0.000 description 31
102100023306 Nesprin-1 Human genes 0.000 description 31
210000004027 cell Anatomy 0.000 description 30
244000005700 microbiome Species 0.000 description 24
OVBPIULPVIDEAO-LBPRGKRZSA-N folic acid Chemical compound C=1N=C2NC(N)=NC(=O)C2=NC=1CNC1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 OVBPIULPVIDEAO-LBPRGKRZSA-N 0.000 description 19
108020004414 DNA Proteins 0.000 description 18
102000004190 Enzymes Human genes 0.000 description 18
108090000790 Enzymes Proteins 0.000 description 18
229940088598 enzyme Drugs 0.000 description 18
235000019152 folic acid Nutrition 0.000 description 15
238000000034 method Methods 0.000 description 15
101100021402 Caenorhabditis elegans lis-1 gene Proteins 0.000 description 14
239000011724 folic acid Substances 0.000 description 14
230000000694 effects Effects 0.000 description 13
239000002609 medium Substances 0.000 description 12
108091008146 restriction endonucleases Proteins 0.000 description 12
238000003776 cleavage reaction Methods 0.000 description 10
230000007017 scission Effects 0.000 description 10
210000000170 cell membrane Anatomy 0.000 description 9
229940014144 folate Drugs 0.000 description 9
239000012528 membrane Substances 0.000 description 9
125000003729 nucleotide group Chemical group 0.000 description 9
239000000047 product Substances 0.000 description 9
235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 8
150000001413 amino acids Chemical group 0.000 description 8
210000000805 cytoplasm Anatomy 0.000 description 8
210000001322 periplasm Anatomy 0.000 description 8
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 7
238000002955 isolation Methods 0.000 description 7
230000009466 transformation Effects 0.000 description 7
235000001014 amino acid Nutrition 0.000 description 6
101150071119 cpg-2 gene Proteins 0.000 description 6
230000001086 cytosolic effect Effects 0.000 description 6
238000002474 experimental method Methods 0.000 description 6
239000000284 extract Substances 0.000 description 6
238000002360 preparation method Methods 0.000 description 6
OVBPIULPVIDEAO-UHFFFAOYSA-N N-Pteroyl-L-glutaminsaeure Natural products C=1N=C2NC(N)=NC(=O)C2=NC=1CNC1=CC=C(C(=O)NC(CCC(O)=O)C(O)=O)C=C1 OVBPIULPVIDEAO-UHFFFAOYSA-N 0.000 description 5
108010076504 Protein Sorting Signals Proteins 0.000 description 5
239000002253 acid Substances 0.000 description 5
108010005774 beta-Galactosidase Proteins 0.000 description 5
238000005119 centrifugation Methods 0.000 description 5
239000013611 chromosomal DNA Substances 0.000 description 5
229960000304 folic acid Drugs 0.000 description 5
230000004927 fusion Effects 0.000 description 5
238000004519 manufacturing process Methods 0.000 description 5
102000002260 Alkaline Phosphatase Human genes 0.000 description 4
108020004774 Alkaline Phosphatase Proteins 0.000 description 4
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 4
102000005936 beta-Galactosidase Human genes 0.000 description 4
239000000872 buffer Substances 0.000 description 4
230000004807 localization Effects 0.000 description 4
229920001817 Agar Polymers 0.000 description 3
OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 3
108010054576 Deoxyribonuclease EcoRI Proteins 0.000 description 3
FBOZXECLQNJBKD-ZDUSSCGKSA-N L-methotrexate Chemical compound C=1N=C2N=C(N)N=C(N)C2=NC=1CN(C)C1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 FBOZXECLQNJBKD-ZDUSSCGKSA-N 0.000 description 3
239000008272 agar Substances 0.000 description 3
229910052799 carbon Inorganic materials 0.000 description 3
230000001413 cellular effect Effects 0.000 description 3
239000001963 growth medium Substances 0.000 description 3
238000003780 insertion Methods 0.000 description 3
230000037431 insertion Effects 0.000 description 3
239000007788 liquid Substances 0.000 description 3
229960000485 methotrexate Drugs 0.000 description 3
238000000746 purification Methods 0.000 description 3
230000028327 secretion Effects 0.000 description 3
KDCGOANMDULRCW-UHFFFAOYSA-N 7H-purine Chemical compound N1=CNC2=NC=NC2=C1 KDCGOANMDULRCW-UHFFFAOYSA-N 0.000 description 2
241000894006 Bacteria Species 0.000 description 2
108020004705 Codon Proteins 0.000 description 2
WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 2
CSNNHWWHGAXBCP-UHFFFAOYSA-L Magnesium sulfate Chemical compound [Mg+2].[O-][S+2]([O-])([O-])[O-] CSNNHWWHGAXBCP-UHFFFAOYSA-L 0.000 description 2
206010028980 Neoplasm Diseases 0.000 description 2
229910019142 PO4 Inorganic materials 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
229960000723 ampicillin Drugs 0.000 description 2
AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 2
230000003115 biocidal effect Effects 0.000 description 2
201000011510 cancer Diseases 0.000 description 2
229940041514 candida albicans extract Drugs 0.000 description 2
238000006243 chemical reaction Methods 0.000 description 2
238000002512 chemotherapy Methods 0.000 description 2
239000013599 cloning vector Substances 0.000 description 2
125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 2
238000001962 electrophoresis Methods 0.000 description 2
108010062699 gamma-Glutamyl Hydrolase Proteins 0.000 description 2
239000000499 gel Substances 0.000 description 2
239000008103 glucose Substances 0.000 description 2
102000006602 glyceraldehyde-3-phosphate dehydrogenase Human genes 0.000 description 2
108020004445 glyceraldehyde-3-phosphate dehydrogenase Proteins 0.000 description 2
230000012010 growth Effects 0.000 description 2
230000007062 hydrolysis Effects 0.000 description 2
238000006460 hydrolysis reaction Methods 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
150000002500 ions Chemical class 0.000 description 2
239000003550 marker Substances 0.000 description 2
239000000463 material Substances 0.000 description 2
239000008188 pellet Substances 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
239000011780 sodium chloride Substances 0.000 description 2
239000005720 sucrose Substances 0.000 description 2
238000011426 transformation method Methods 0.000 description 2
239000012137 tryptone Substances 0.000 description 2
241001515965 unidentified phage Species 0.000 description 2
239000012138 yeast extract Substances 0.000 description 2
108091032973 (ribonucleotides)n+m Proteins 0.000 description 1
KDELTXNPUXUBMU-UHFFFAOYSA-N 2-[2-[bis(carboxymethyl)amino]ethyl-(carboxymethyl)amino]acetic acid boric acid Chemical compound OB(O)O.OB(O)O.OB(O)O.OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KDELTXNPUXUBMU-UHFFFAOYSA-N 0.000 description 1
OPIFSICVWOWJMJ-AEOCFKNESA-N 5-bromo-4-chloro-3-indolyl beta-D-galactoside Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1OC1=CNC2=CC=C(Br)C(Cl)=C12 OPIFSICVWOWJMJ-AEOCFKNESA-N 0.000 description 1
VVIAGPKUTFNRDU-UHFFFAOYSA-N 6S-folinic acid Natural products C1NC=2NC(N)=NC(=O)C=2N(C=O)C1CNC1=CC=C(C(=O)NC(CCC(O)=O)C(O)=O)C=C1 VVIAGPKUTFNRDU-UHFFFAOYSA-N 0.000 description 1
229920000936 Agarose Polymers 0.000 description 1
241000193830 Bacillus <bacterium> Species 0.000 description 1
UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 1
201000009030 Carcinoma Diseases 0.000 description 1
241000557626 Corvus corax Species 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
102000053602 DNA Human genes 0.000 description 1
102000012410 DNA Ligases Human genes 0.000 description 1
108010061982 DNA Ligases Proteins 0.000 description 1
238000001712 DNA sequencing Methods 0.000 description 1
102000004163 DNA-directed RNA polymerases Human genes 0.000 description 1
108090000626 DNA-directed RNA polymerases Proteins 0.000 description 1
101710088194 Dehydrogenase Proteins 0.000 description 1
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 1
108091029865 Exogenous DNA Proteins 0.000 description 1
MPJKWIXIYCLVCU-UHFFFAOYSA-N Folinic acid Natural products NC1=NC2=C(N(C=O)C(CNc3ccc(cc3)C(=O)NC(CCC(=O)O)CC(=O)O)CN2)C(=O)N1 MPJKWIXIYCLVCU-UHFFFAOYSA-N 0.000 description 1
101150019793 G2 gene Proteins 0.000 description 1
102000002464 Galactosidases Human genes 0.000 description 1
108010093031 Galactosidases Proteins 0.000 description 1
108700039691 Genetic Promoter Regions Proteins 0.000 description 1
102100036263 Glutamyl-tRNA(Gln) amidotransferase subunit C, mitochondrial Human genes 0.000 description 1
101001001786 Homo sapiens Glutamyl-tRNA(Gln) amidotransferase subunit C, mitochondrial Proteins 0.000 description 1
102000004877 Insulin Human genes 0.000 description 1
102100034343 Integrase Human genes 0.000 description 1
WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 1
241000124008 Mammalia Species 0.000 description 1
102000016943 Muramidase Human genes 0.000 description 1
108010014251 Muramidase Proteins 0.000 description 1
101100293261 Mus musculus Naa15 gene Proteins 0.000 description 1
108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
108010007843 NADH oxidase Proteins 0.000 description 1
101150082943 NAT1 gene Proteins 0.000 description 1
102000004316 Oxidoreductases Human genes 0.000 description 1
108090000854 Oxidoreductases Proteins 0.000 description 1
108091005804 Peptidases Proteins 0.000 description 1
102000035195 Peptidases Human genes 0.000 description 1
108010090127 Periplasmic Proteins Proteins 0.000 description 1
101150059178 Plec gene Proteins 0.000 description 1
108010076039 Polyproteins Proteins 0.000 description 1
ZKQOUHVVXABNDG-IUCAKERBSA-N Pro-Leu Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)[C@@H]1CCCN1 ZKQOUHVVXABNDG-IUCAKERBSA-N 0.000 description 1
241000589776 Pseudomonas putida Species 0.000 description 1
241000589774 Pseudomonas sp. Species 0.000 description 1
CZPWVGJYEJSRLH-UHFFFAOYSA-N Pyrimidine Chemical compound C1=CN=CN=C1 CZPWVGJYEJSRLH-UHFFFAOYSA-N 0.000 description 1
108010092799 RNA-directed DNA polymerase Proteins 0.000 description 1
108020004682 Single-Stranded DNA Proteins 0.000 description 1
108091081024 Start codon Proteins 0.000 description 1
239000004098 Tetracycline Substances 0.000 description 1
238000002835 absorbance Methods 0.000 description 1
238000010521 absorption reaction Methods 0.000 description 1
150000007513 acids Chemical class 0.000 description 1
239000011543 agarose gel Substances 0.000 description 1
101150115889 al gene Proteins 0.000 description 1
230000003698 anagen phase Effects 0.000 description 1
238000004458 analytical method Methods 0.000 description 1
239000005557 antagonist Substances 0.000 description 1
230000015572 biosynthetic process Effects 0.000 description 1
229910052792 caesium Inorganic materials 0.000 description 1
TVFDJXOCXUVLDH-UHFFFAOYSA-N caesium atom Chemical compound [Cs] TVFDJXOCXUVLDH-UHFFFAOYSA-N 0.000 description 1
239000001110 calcium chloride Substances 0.000 description 1
235000011148 calcium chloride Nutrition 0.000 description 1
229910001628 calcium chloride Inorganic materials 0.000 description 1
230000010261 cell growth Effects 0.000 description 1
210000002421 cell wall Anatomy 0.000 description 1
229960005091 chloramphenicol Drugs 0.000 description 1
WIIZWVCIJKGZOK-RKDXNWHRSA-N chloramphenicol Chemical compound ClC(Cl)C(=O)N[C@H](CO)[C@H](O)C1=CC=C([N+]([O-])=O)C=C1 WIIZWVCIJKGZOK-RKDXNWHRSA-N 0.000 description 1
210000000349 chromosome Anatomy 0.000 description 1
238000010367 cloning Methods 0.000 description 1
238000012790 confirmation Methods 0.000 description 1
230000009089 cytolysis Effects 0.000 description 1
238000000432 density-gradient centrifugation Methods 0.000 description 1
239000005547 deoxyribonucleotide Substances 0.000 description 1
125000002637 deoxyribonucleotide group Chemical group 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
239000000539 dimer Substances 0.000 description 1
238000005516 engineering process Methods 0.000 description 1
229960005542 ethidium bromide Drugs 0.000 description 1
239000012530 fluid Substances 0.000 description 1
150000002224 folic acids Chemical class 0.000 description 1
235000008191 folinic acid Nutrition 0.000 description 1
239000011672 folinic acid Substances 0.000 description 1
VVIAGPKUTFNRDU-ABLWVSNPSA-N folinic acid Chemical compound C1NC=2NC(N)=NC(=O)C=2N(C=O)C1CNC1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 VVIAGPKUTFNRDU-ABLWVSNPSA-N 0.000 description 1
238000005194 fractionation Methods 0.000 description 1
108020001507 fusion proteins Proteins 0.000 description 1
102000037865 fusion proteins Human genes 0.000 description 1
230000002068 genetic effect Effects 0.000 description 1
229930195712 glutamate Natural products 0.000 description 1
XLYOFNOQVPJJNP-ZSJDYOACSA-N heavy water Substances [2H]O[2H] XLYOFNOQVPJJNP-ZSJDYOACSA-N 0.000 description 1
230000002209 hydrophobic effect Effects 0.000 description 1
230000001900 immune effect Effects 0.000 description 1
238000001727 in vivo Methods 0.000 description 1
238000011534 incubation Methods 0.000 description 1
230000006698 induction Effects 0.000 description 1
229940125396 insulin Drugs 0.000 description 1
229960000318 kanamycin Drugs 0.000 description 1
229930027917 kanamycin Natural products 0.000 description 1
SBUJHOSQTJFQJX-NOAMYHISSA-N kanamycin Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N SBUJHOSQTJFQJX-NOAMYHISSA-N 0.000 description 1
229930182823 kanamycin A Natural products 0.000 description 1
150000002597 lactoses Chemical class 0.000 description 1
101150025049 leuB gene Proteins 0.000 description 1
WQVJUBFKFCDYDQ-BBWFWOEESA-N leubethanol Natural products C1=C(C)C=C2[C@H]([C@H](CCC=C(C)C)C)CC[C@@H](C)C2=C1O WQVJUBFKFCDYDQ-BBWFWOEESA-N 0.000 description 1
229960001691 leucovorin Drugs 0.000 description 1
ZNOVTXRBGFNYRX-ABLWVSNPSA-N levomefolic acid Chemical compound C1NC=2NC(N)=NC(=O)C=2N(C)C1CNC1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 ZNOVTXRBGFNYRX-ABLWVSNPSA-N 0.000 description 1
235000007635 levomefolic acid Nutrition 0.000 description 1
239000011578 levomefolic acid Substances 0.000 description 1
XIXADJRWDQXREU-UHFFFAOYSA-M lithium acetate Chemical compound [Li+].CC([O-])=O XIXADJRWDQXREU-UHFFFAOYSA-M 0.000 description 1
230000007774 longterm Effects 0.000 description 1
229960000274 lysozyme Drugs 0.000 description 1
235000010335 lysozyme Nutrition 0.000 description 1
239000004325 lysozyme Substances 0.000 description 1
229910052943 magnesium sulfate Inorganic materials 0.000 description 1
235000019341 magnesium sulphate Nutrition 0.000 description 1
238000013507 mapping Methods 0.000 description 1
230000000813 microbial effect Effects 0.000 description 1
229930027945 nicotinamide-adenine dinucleotide Natural products 0.000 description 1
BOPGDPNILDQYTO-NNYOXOHSSA-N nicotinamide-adenine dinucleotide Chemical compound C1=CCC(C(=O)N)=CN1[C@H]1[C@H](O)[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OC[C@@H]2[C@H]([C@@H](O)[C@@H](O2)N2C3=NC=NC(N)=C3N=C2)O)O1 BOPGDPNILDQYTO-NNYOXOHSSA-N 0.000 description 1
235000015097 nutrients Nutrition 0.000 description 1
229940046166 oligodeoxynucleotide Drugs 0.000 description 1
230000003204 osmotic effect Effects 0.000 description 1
238000001556 precipitation Methods 0.000 description 1
239000002243 precursor Substances 0.000 description 1
108010090894 prolylleucine Proteins 0.000 description 1
230000000644 propagated effect Effects 0.000 description 1
229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 1
230000006798 recombination Effects 0.000 description 1
238000005215 recombination Methods 0.000 description 1
238000011160 research Methods 0.000 description 1
230000000717 retained effect Effects 0.000 description 1
239000012266 salt solution Substances 0.000 description 1
150000003839 salts Chemical class 0.000 description 1
239000013049 sediment Substances 0.000 description 1
238000004062 sedimentation Methods 0.000 description 1
238000000926 separation method Methods 0.000 description 1
238000012163 sequencing technique Methods 0.000 description 1
239000013605 shuttle vector Substances 0.000 description 1
238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
239000007787 solid Substances 0.000 description 1
238000000527 sonication Methods 0.000 description 1
239000000600 sorbitol Substances 0.000 description 1
239000003381 stabilizer Substances 0.000 description 1
238000010561 standard procedure Methods 0.000 description 1
239000000758 substrate Substances 0.000 description 1
239000006228 supernatant Substances 0.000 description 1
238000010189 synthetic method Methods 0.000 description 1
238000012360 testing method Methods 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
231100000331 toxic Toxicity 0.000 description 1
230000002588 toxic effect Effects 0.000 description 1
230000001131 transforming effect Effects 0.000 description 1
150000005691 triesters Chemical class 0.000 description 1
238000002604 ultrasonography Methods 0.000 description 1
210000005253 yeast cell Anatomy 0.000 description 1
239000011592 zinc chloride Substances 0.000 description 1
235000005074 zinc chloride Nutrition 0.000 description 1
JIAARYAFYJHUJI-UHFFFAOYSA-L zinc dichloride Chemical compound [Cl-].[Cl-].[Zn+2] JIAARYAFYJHUJI-UHFFFAOYSA-L 0.000 description 1

Classifications

- 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)
- C12Y304/17—Metallocarboxypeptidases (3.4.17)
- C12Y304/17011—Glutamate carboxypeptidase (3.4.17.11)
- 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
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
- C12N15/62—DNA sequences coding for fusion proteins
- C12N15/625—DNA sequences coding for fusion proteins containing a sequence coding for a signal sequence
- 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
- C12N15/74—Vectors or expression systems specially adapted for prokaryotic hosts other than E. coli, e.g. Lactobacillus, Micromonospora
- C12N15/78—Vectors or expression systems specially adapted for prokaryotic hosts other than E. coli, e.g. Lactobacillus, Micromonospora for Pseudomonas
- 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)
- C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
- C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
- C12N9/2468—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1) acting on beta-galactose-glycoside bonds, e.g. carrageenases (3.2.1.83; 3.2.1.157); beta-agarase (3.2.1.81)
- C12N9/2471—Beta-galactosidase (3.2.1.23), i.e. exo-(1-->4)-beta-D-galactanase
- 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)
- 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)
- C12N9/485—Exopeptidases (3.4.11-3.4.19)
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
- C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
- C12Y302/01023—Beta-galactosidase (3.2.1.23), i.e. exo-(1-->4)-beta-D-galactanase
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/01—Fusion polypeptide containing a localisation/targetting motif
- C07K2319/02—Fusion polypeptide containing a localisation/targetting motif containing a signal sequence
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/01—Fusion polypeptide containing a localisation/targetting motif
- C07K2319/034—Fusion polypeptide containing a localisation/targetting motif containing a motif for targeting to the periplasmic space of Gram negative bacteria as a soluble protein, i.e. signal sequence should be cleaved

Landscapes

Health & Medical Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
Genetics & Genomics (AREA)
Chemical & Material Sciences (AREA)
Engineering & Computer Science (AREA)
Organic Chemistry (AREA)
Zoology (AREA)
Wood Science & Technology (AREA)
Bioinformatics & Cheminformatics (AREA)
General Engineering & Computer Science (AREA)
Biomedical Technology (AREA)
General Health & Medical Sciences (AREA)
Biochemistry (AREA)
Biotechnology (AREA)
Molecular Biology (AREA)
Microbiology (AREA)
Medicinal Chemistry (AREA)
Biophysics (AREA)
Physics & Mathematics (AREA)
Plant Pathology (AREA)
Micro-Organisms Or Cultivation Processes Thereof (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)
Enzymes And Modification Thereof (AREA)
Management, Administration, Business Operations System, And Electronic Commerce (AREA)
Time Recorders, Dirve Recorders, Access Control (AREA)

NO841130A 1983-03-28 1984-03-22 Ledersekvens for aa fremme sekresjon av genprodukter NO841130L (no)

Applications Claiming Priority (1)

Application Number	Priority Date	Filing Date	Title
GB8308483A GB8308483D0 (en)	1983-03-28	1983-03-28	Secretion of gene products

Publications (1)

Publication Number	Publication Date
NO841130L true NO841130L (no)	1984-10-01

Family

ID=10540349

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
NO841130A NO841130L (no)	1983-03-28	1984-03-22	Ledersekvens for aa fremme sekresjon av genprodukter

Country Status (6)

Country	Link
EP (1)	EP0121352B1 (fr)
JP (1)	JPS6054686A (fr)
DE (1)	DE3468434D1 (fr)
DK (1)	DK167584A (fr)
GB (1)	GB8308483D0 (fr)
NO (1)	NO841130L (fr)

Families Citing this family (37)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US4925919A (en) *	1984-04-25	1990-05-15	Roland Mertelsmann	Purified interleukin 2
US4853332A (en) *	1982-10-19	1989-08-01	Cetus Corporation	Structural genes, plasmids and transformed cells for producing cysteine depleted muteins of biologically active proteins
US4711844A (en) *	1983-03-09	1987-12-08	Cetus Corporation	Modified signal peptides
ATE220101T1 (de)	1983-04-25	2002-07-15	Chiron Corp	Hybrid-dns-synthesis von reifen insulinähnlichen wachstumsfaktoren
IL71991A (en)	1983-06-06	1994-05-30	Genentech Inc	Preparation of human FGI and FGE in their processed form through recombinant AND tranology in prokaryotes
US4569790A (en) *	1984-03-28	1986-02-11	Cetus Corporation	Process for recovering microbially produced interleukin-2 and purified recombinant interleukin-2 compositions
US4908433A (en) *	1984-04-25	1990-03-13	Sloan-Kettering Institute For Cancer Research	Uses of interleukin-2
US4908434A (en) *	1984-04-25	1990-03-13	Sloan-Kettering Institute For Cancer Research	Process for preparing purified interleukin-2
US4963495A (en) *	1984-10-05	1990-10-16	Genentech, Inc.	Secretion of heterologous proteins
US4569794A (en) *	1984-12-05	1986-02-11	Eli Lilly And Company	Process for purifying proteins and compounds useful in such process
US4935352A (en) *	1985-10-21	1990-06-19	Takeda Chemical Industries, Ltd.	Expression vector for animal cell line and use thereof
JPH07108224B2 (ja) *	1985-11-07	1995-11-22	重三鵜高	バチルス・ブレビスを用いる遺伝子の発現方法
JPH0669377B2 (ja) *	1985-11-25	1994-09-07	工業技術院長	Ｄｎａ塩基配列およびベクタ−
JPS6387975A (ja) *	1986-10-02	1988-04-19	Agency Of Ind Science & Technol	枯草菌菌株
DK175535B1 (da) *	1987-03-04	2004-11-29	Daiichi Suntory Pharma Co Ltd	Fremgangsmåde til fremstilling af et fysiologisk aktivt cysteinholdigt peptid
EP0499990B1 (fr) *	1991-02-19	1996-05-15	Takeda Chemical Industries, Ltd.	Procédé pour la production des peptides sans cystéine
GB9301553D0 (en) *	1993-01-27	1993-03-17	Univ Wales	Protein synthesis
GB9415167D0 (en) *	1994-07-27	1994-09-14	Springer Caroline J	Improvements relating to cancer therapy
US6410701B1 (en) *	1995-05-05	2002-06-25	Human Genome Sciences, Inc.	Human neuropeptide receptor
GB9601640D0 (en) *	1996-01-26	1996-03-27	Cancer Res Campaign Tech	Ligand directed enzyme prodrug therapy
US6656718B2 (en)	2000-07-07	2003-12-02	Cancer Research Technology Limited	Modified carboxypeptidase enzymes and their use
US9453251B2 (en)	2002-10-08	2016-09-27	Pfenex Inc.	Expression of mammalian proteins in Pseudomonas fluorescens
US7153666B2 (en)	2003-07-17	2006-12-26	General Atomics	Methods and compositions for determination of glycated proteins
US8187831B2 (en)	2003-09-19	2012-05-29	General Atomics	Determination of ions using ion-sensitive enzymes
US7022494B2 (en)	2003-09-19	2006-04-04	General Atomics	Detection of potassium ions using ion-sensitive enzymes
PL2336153T3 (pl)	2003-11-21	2016-08-31	Pfenex Inc	Udoskonalone systemy ekspresji z układem wydzielania SEC
US8101735B2 (en)	2004-06-16	2012-01-24	Health Protection Agency	Preparation of protective antigen
US7355027B2 (en) *	2004-06-16	2008-04-08	Dynport Vaccine Company Llc	Bacillus anthracis protective antigen
EP2412816B1 (fr)	2004-07-26	2014-12-03	Pfenex Inc.	Procédé permettant d'améliorer l'expression d'une protéine par mise au point d'une souche par génie génétique
WO2008013874A1 (fr)	2006-07-25	2008-01-31	General Atomics	Procédé de recherche du pourcentage d'hémoglobine glycatée
US7943385B2 (en)	2006-07-25	2011-05-17	General Atomics	Methods for assaying percentage of glycated hemoglobin
CA2677179C (fr)	2007-01-31	2016-02-16	Dow Global Technologies Inc.	Sequences leader bacteriennes pour augmenter l'expression
EP2142651B1 (fr)	2007-04-27	2013-05-22	Pfenex Inc.	Procédé pour rapidement cribler des hôtes microbiens et identifier certaines souches ayant un rendement et/ou une qualité d'expression des protéines hétérologues améliorés
US9580719B2 (en)	2007-04-27	2017-02-28	Pfenex, Inc.	Method for rapidly screening microbial hosts to identify certain strains with improved yield and/or quality in the expression of heterologous proteins
CN102076867A (zh)	2008-05-13	2011-05-25	通用原子公司	用于直接测定糖化血红蛋白百分比的电化学生物传感器
BR112015022181A8 (pt)	2013-03-12	2018-01-23	Massachusetts Eye & Ear Infirmary	proteínas da substância de inibição mulleriana (mis) e usos das mesmas para o tratamento de doenças
WO2015089321A2 (fr)	2013-12-11	2015-06-18	The General Hospital Corporation	Utilisation de protéines d'hormone anti-mullerienne (amh) pour la contraception et la préservation de la réserve ovarienne

Family Cites Families (2)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
CA1201668A (fr) *	1977-11-08	1986-03-11	Genentech, Inc.	Adn synthetique et methode de production
US4506013A (en) *	1980-10-03	1985-03-19	Eli Lilly And Company	Stabilizing and selecting recombinant DNA host cells

1983
- 1983-03-28 GB GB8308483A patent/GB8308483D0/en active Pending
1984
- 1984-03-06 EP EP19840301468 patent/EP0121352B1/fr not_active Expired
- 1984-03-06 DE DE8484301468T patent/DE3468434D1/de not_active Expired
- 1984-03-22 NO NO841130A patent/NO841130L/no unknown
- 1984-03-26 DK DK167584A patent/DK167584A/da not_active IP Right Cessation
- 1984-03-27 JP JP59059287A patent/JPS6054686A/ja active Pending

Also Published As

Publication number	Publication date
GB8308483D0 (en)	1983-05-05
JPS6054686A (ja)	1985-03-29
DE3468434D1 (en)	1988-02-11
DK167584A (da)	1984-09-29
EP0121352B1 (fr)	1988-01-07
DK167584D0 (da)	1984-03-26
EP0121352A1 (fr)	1984-10-10

Publication	Publication Date	Title
NO841130L (no)	1984-10-01	Ledersekvens for aa fremme sekresjon av genprodukter
EP0096430B1 (fr)	1990-01-10	Système de clônage pour espèces de Kluyveromyces
Minton et al.	1983	Molecular cloning of the Pseudomonas carboxypeptidase G2 gene and its expression in Escherichia coli and Pseudomonas putida
Shevchik et al.	1994	Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity.
Reverchon et al.	1994	pecS: a locus controlling pectinase, cellulase and blue pigment production in Erwinia chrysanthemi
CN111278852B (zh)	2024-07-16	重组欧氏杆菌天冬酰胺酶的生产方法
JP2963695B2 (ja)	1999-10-18	クローン化リゾスタフィン遺伝子の発現
JP7430189B2 (ja)	2024-02-09	外来遺伝子を発現させるためのピキア・パストリス変異株
JP2006068019A (ja)	2006-03-16	ｏｓｍＢプロモータで制御される発現プラスミド
NO840200L (no)	1984-07-30	Glukoamylase cdna.
EP0035384A2 (fr)	1981-09-09	Segment de désoxyribonucléotides destiné à être rattaché à une séquence codante clonée d'ADN
EP0889134A1 (fr)	1999-01-07	$g(b)-FRUCTOFURANNOSIDASE ET SON GENE, PROCEDE D'ISOLEMENT DU GENE DE $g(b)-FRUCTOFURANNOSIDASE, SYSTEME POUR LA PRODUCTION DE $g(b)-FRUCTOFURANNOSIDASE, ET VARIANT DE $g(b)-FRUCTOFURANNOSIDASE
EP0353188B1 (fr)	1994-03-16	Système d'expression
Beuve et al.	1990	Rhizobium meliloti adenylate cyclase is related to eucaryotic adenylate and guanylate cyclases
Delgado et al.	2003	Candida albicans TDH3 gene promotes secretion of internal invertase when expressed in Saccharomyces cerevisiae as a glyceraldehyde‐3‐phosphate dehydrogenase‐invertase fusion protein
Kahng et al.	2002	Enhanced detection and characterization of protocatechuate 3, 4-dioxygenase in Acinetobacter lwoffii K24 by proteomics using a column separation
EP0302838B1 (fr)	1994-06-29	Clonage du gène codant pour l'enzyme isoamylase et son utilisation pour la production de cette enzyme
JPH05284973A (ja)	1993-11-02	組換プラスミドおよびこれをベクターとして用いる異種蛋白質の分泌生産方法
WO1986000929A1 (fr)	1986-02-13	Molecule d'adn recombinant, microorganismes transformes et procede de production de penicilline v amidase
KR100420313B1 (ko)	2004-03-03	신규 레반슈크라제를 이용한 레반의 생산방법
CA1200775A (fr)	1986-02-18	Liens d'expression
Walker et al.	1990	Deletion analysis of domain independence in the TRP1 gene product of Neurospora crassa
JPH05500309A (ja)	1993-01-28	新規のポリガラクツロナーゼ遺伝子および利用方法
JPH06505873A (ja)	1994-07-07	キモシンの製造方法
JPH02219570A (ja)	1990-09-03	ヒト５―リポキシゲナーゼの製造方法