DK175331B1 - Ekspressionskontrol-DNA-sekvenser, ekspressionsvektorer, som indeholder disse DNA-sekvenser, transformanter som bærer disse ekspressionsvektorer, og fremgangsmåder til fremstilling af pro- og eukaryote proteiner under anvendelse af de - Google Patents

Ekspressionskontrol-DNA-sekvenser, ekspressionsvektorer, som indeholder disse DNA-sekvenser, transformanter som bærer disse ekspressionsvektorer, og fremgangsmåder til fremstilling af pro- og eukaryote proteiner under anvendelse af de Download PDF

Info

Publication number: DK175331B1
Authority: DK; Denmark
Prior art keywords: plasmid; expression; promoter; dna; expression vector
Prior art date: 1984-12-17

Application number

DK198505843A

Other languages

Danish (da)

English (en)

Other versions

DK584385D0 (da

DK584385A (da

Inventor

Dietrich Stueber

Hermann Bujard

Original Assignee

Hoffmann La Roche

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.)

1984-12-17

Filing date

1985-12-16

Publication date

2004-08-30

1985-12-16 Application filed by Hoffmann La Roche filed Critical Hoffmann La Roche

1985-12-16 Publication of DK584385D0 publication Critical patent/DK584385D0/da

1986-06-18 Publication of DK584385A publication Critical patent/DK584385A/da

2004-08-30 Application granted granted Critical

2004-08-30 Publication of DK175331B1 publication Critical patent/DK175331B1/da

Links

230000014509 gene expression Effects 0.000 title claims abstract description 42
108091028043 Nucleic acid sequence Proteins 0.000 title claims abstract description 39
239000013604 expression vector Substances 0.000 title claims abstract description 21
238000000034 method Methods 0.000 title claims abstract description 14
108090000623 proteins and genes Proteins 0.000 title abstract description 52
102000004169 proteins and genes Human genes 0.000 title abstract description 16
238000002360 preparation method Methods 0.000 title description 4
229920001184 polypeptide Polymers 0.000 claims abstract description 10
102000004196 processed proteins & peptides Human genes 0.000 claims abstract description 10
108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 10
239000013612 plasmid Substances 0.000 claims description 76
241000588724 Escherichia coli Species 0.000 claims description 23
108010035563 Chloramphenicol O-acetyltransferase Proteins 0.000 claims description 17
239000013598 vector Substances 0.000 claims description 9
239000002773 nucleotide Substances 0.000 claims description 8
125000003729 nucleotide group Chemical group 0.000 claims description 8
235000014469 Bacillus subtilis Nutrition 0.000 claims description 4
241001596967 Escherichia coli M15 Species 0.000 claims description 4
230000003362 replicative effect Effects 0.000 claims 6
241000192125 Firmicutes Species 0.000 claims 2
230000000694 effects Effects 0.000 abstract description 6
238000004519 manufacturing process Methods 0.000 abstract description 2
108020004414 DNA Proteins 0.000 description 34
239000012634 fragment Substances 0.000 description 33
210000004027 cell Anatomy 0.000 description 20
230000004927 fusion Effects 0.000 description 18
239000000872 buffer Substances 0.000 description 17
LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 16
RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 14
235000018102 proteins Nutrition 0.000 description 14
108091008146 restriction endonucleases Proteins 0.000 description 14
ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 12
238000010276 construction Methods 0.000 description 12
239000000499 gel Substances 0.000 description 12
102000004190 Enzymes Human genes 0.000 description 11
108090000790 Enzymes Proteins 0.000 description 11
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 10
229960000723 ampicillin Drugs 0.000 description 10
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 10
238000000605 extraction Methods 0.000 description 10
108091026890 Coding region Proteins 0.000 description 9
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 9
BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 9
230000001105 regulatory effect Effects 0.000 description 9
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 8
238000001962 electrophoresis Methods 0.000 description 8
239000000243 solution Substances 0.000 description 8
108010034634 Repressor Proteins Proteins 0.000 description 7
102000009661 Repressor Proteins Human genes 0.000 description 7
229960005091 chloramphenicol Drugs 0.000 description 7
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 7
239000000203 mixture Substances 0.000 description 7
229920002401 polyacrylamide Polymers 0.000 description 7
238000011534 incubation Methods 0.000 description 6
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 6
238000013518 transcription Methods 0.000 description 6
230000035897 transcription Effects 0.000 description 6
230000002103 transcriptional effect Effects 0.000 description 6
102000004163 DNA-directed RNA polymerases Human genes 0.000 description 5
108090000626 DNA-directed RNA polymerases Proteins 0.000 description 5
230000027455 binding Effects 0.000 description 5
238000010367 cloning Methods 0.000 description 5
230000000977 initiatory effect Effects 0.000 description 5
239000011780 sodium chloride Substances 0.000 description 5
102000012410 DNA Ligases Human genes 0.000 description 4
108010061982 DNA Ligases Proteins 0.000 description 4
WCUXLLCKKVVCTQ-UHFFFAOYSA-M Potassium chloride Chemical compound [Cl-].[K+] WCUXLLCKKVVCTQ-UHFFFAOYSA-M 0.000 description 4
229920005654 Sephadex Polymers 0.000 description 4
239000012507 Sephadex™ Substances 0.000 description 4
108010022394 Threonine synthase Proteins 0.000 description 4
238000004458 analytical method Methods 0.000 description 4
101150055766 cat gene Proteins 0.000 description 4
238000006243 chemical reaction Methods 0.000 description 4
238000003776 cleavage reaction Methods 0.000 description 4
102000004419 dihydrofolate reductase Human genes 0.000 description 4
230000010354 integration Effects 0.000 description 4
SCVFZCLFOSHCOH-UHFFFAOYSA-M potassium acetate Chemical compound [K+].CC([O-])=O SCVFZCLFOSHCOH-UHFFFAOYSA-M 0.000 description 4
239000000047 product Substances 0.000 description 4
230000007017 scission Effects 0.000 description 4
230000014616 translation Effects 0.000 description 4
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 3
UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 3
101150074155 DHFR gene Proteins 0.000 description 3
230000004543 DNA replication Effects 0.000 description 3
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 3
PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
102000004877 Insulin Human genes 0.000 description 3
108090001061 Insulin Proteins 0.000 description 3
101710163270 Nuclease Proteins 0.000 description 3
230000001580 bacterial effect Effects 0.000 description 3
239000001110 calcium chloride Substances 0.000 description 3
229910001628 calcium chloride Inorganic materials 0.000 description 3
235000011148 calcium chloride Nutrition 0.000 description 3
239000005018 casein Substances 0.000 description 3
BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 3
235000021240 caseins Nutrition 0.000 description 3
238000002474 experimental method Methods 0.000 description 3
239000008103 glucose Substances 0.000 description 3
238000000338 in vitro Methods 0.000 description 3
230000002779 inactivation Effects 0.000 description 3
229940125396 insulin Drugs 0.000 description 3
230000003993 interaction Effects 0.000 description 3
239000011777 magnesium Substances 0.000 description 3
108020004999 messenger RNA Proteins 0.000 description 3
238000010561 standard procedure Methods 0.000 description 3
238000013519 translation Methods 0.000 description 3
241000894006 Bacteria Species 0.000 description 2
102000004594 DNA Polymerase I Human genes 0.000 description 2
108010017826 DNA Polymerase I Proteins 0.000 description 2
241000701959 Escherichia virus Lambda Species 0.000 description 2
TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 2
239000000427 antigen Substances 0.000 description 2
108091007433 antigens Proteins 0.000 description 2
102000036639 antigens Human genes 0.000 description 2
230000015572 biosynthetic process Effects 0.000 description 2
238000005119 centrifugation Methods 0.000 description 2
239000002299 complementary DNA Substances 0.000 description 2
238000004108 freeze drying Methods 0.000 description 2
239000000122 growth hormone Substances 0.000 description 2
238000001727 in vivo Methods 0.000 description 2
101150066555 lacZ gene Proteins 0.000 description 2
230000035772 mutation Effects 0.000 description 2
239000013600 plasmid vector Substances 0.000 description 2
235000011056 potassium acetate Nutrition 0.000 description 2
239000001103 potassium chloride Substances 0.000 description 2
235000011164 potassium chloride Nutrition 0.000 description 2
238000001556 precipitation Methods 0.000 description 2
238000010186 staining Methods 0.000 description 2
238000003860 storage Methods 0.000 description 2
238000003786 synthesis reaction Methods 0.000 description 2
LWIHDJKSTIGBAC-UHFFFAOYSA-K tripotassium phosphate Chemical compound [K+].[K+].[K+].[O-]P([O-])([O-])=O LWIHDJKSTIGBAC-UHFFFAOYSA-K 0.000 description 2
239000011782 vitamin Substances 0.000 description 2
229940088594 vitamin Drugs 0.000 description 2
229930003231 vitamin Natural products 0.000 description 2
235000013343 vitamin Nutrition 0.000 description 2
150000003722 vitamin derivatives Chemical class 0.000 description 2
108091032973 (ribonucleotides)n+m Proteins 0.000 description 1
101150028074 2 gene Proteins 0.000 description 1
BCOSEZGCLGPUSL-UHFFFAOYSA-N 2,3,3-trichloroprop-2-enoyl chloride Chemical compound ClC(Cl)=C(Cl)C(Cl)=O BCOSEZGCLGPUSL-UHFFFAOYSA-N 0.000 description 1
HRPVXLWXLXDGHG-UHFFFAOYSA-N Acrylamide Chemical compound NC(=O)C=C HRPVXLWXLXDGHG-UHFFFAOYSA-N 0.000 description 1
229920001817 Agar Polymers 0.000 description 1
108700028369 Alleles Proteins 0.000 description 1
USFZMSVCRYTOJT-UHFFFAOYSA-N Ammonium acetate Chemical compound N.CC(O)=O USFZMSVCRYTOJT-UHFFFAOYSA-N 0.000 description 1
239000005695 Ammonium acetate Substances 0.000 description 1
108020004635 Complementary DNA Proteins 0.000 description 1
102000053602 DNA Human genes 0.000 description 1
230000004544 DNA amplification Effects 0.000 description 1
108090000204 Dipeptidase 1 Proteins 0.000 description 1
241000701533 Escherichia virus T4 Species 0.000 description 1
241000701988 Escherichia virus T5 Species 0.000 description 1
241000282326 Felis catus Species 0.000 description 1
IECPWNUMDGFDKC-UHFFFAOYSA-N Fusicsaeure Natural products C12C(O)CC3C(=C(CCC=C(C)C)C(O)=O)C(OC(C)=O)CC3(C)C1(C)CCC1C2(C)CCC(O)C1C IECPWNUMDGFDKC-UHFFFAOYSA-N 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
102000018997 Growth Hormone Human genes 0.000 description 1
108010051696 Growth Hormone Proteins 0.000 description 1
102000002265 Human Growth Hormone Human genes 0.000 description 1
108010000521 Human Growth Hormone Proteins 0.000 description 1
239000000854 Human Growth Hormone Substances 0.000 description 1
102000014150 Interferons Human genes 0.000 description 1
108010050904 Interferons Proteins 0.000 description 1
108010002350 Interleukin-2 Proteins 0.000 description 1
108010054278 Lac Repressors Proteins 0.000 description 1
108010074338 Lymphokines Proteins 0.000 description 1
102000008072 Lymphokines Human genes 0.000 description 1
101000966481 Mus musculus Dihydrofolate reductase Proteins 0.000 description 1
101150045515 O gene Proteins 0.000 description 1
102000004316 Oxidoreductases Human genes 0.000 description 1
108090000854 Oxidoreductases Proteins 0.000 description 1
102000015731 Peptide Hormones Human genes 0.000 description 1
108010038988 Peptide Hormones Proteins 0.000 description 1
230000006819 RNA synthesis Effects 0.000 description 1
108091030071 RNAI Proteins 0.000 description 1
238000012300 Sequence Analysis Methods 0.000 description 1
108020004682 Single-Stranded DNA Proteins 0.000 description 1
VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
102000005157 Somatostatin Human genes 0.000 description 1
108010056088 Somatostatin Proteins 0.000 description 1
239000007983 Tris buffer Substances 0.000 description 1
108010075344 Tryptophan synthase Proteins 0.000 description 1
229930003451 Vitamin B1 Natural products 0.000 description 1
238000009825 accumulation Methods 0.000 description 1
ZOIORXHNWRGPMV-UHFFFAOYSA-N acetic acid;zinc Chemical compound [Zn].CC(O)=O.CC(O)=O ZOIORXHNWRGPMV-UHFFFAOYSA-N 0.000 description 1
239000008272 agar Substances 0.000 description 1
235000019257 ammonium acetate Nutrition 0.000 description 1
229940043376 ammonium acetate Drugs 0.000 description 1
230000001093 anti-cancer Effects 0.000 description 1
230000000840 anti-viral effect Effects 0.000 description 1
230000000890 antigenic effect Effects 0.000 description 1
108010005774 beta-Galactosidase Proteins 0.000 description 1
102000006635 beta-lactamase Human genes 0.000 description 1
210000000941 bile Anatomy 0.000 description 1
238000010804 cDNA synthesis Methods 0.000 description 1
238000012512 characterization method Methods 0.000 description 1
210000000349 chromosome Anatomy 0.000 description 1
230000009918 complex formation Effects 0.000 description 1
108091036078 conserved sequence Proteins 0.000 description 1
238000007796 conventional method Methods 0.000 description 1
NKLPQNGYXWVELD-UHFFFAOYSA-M coomassie brilliant blue Chemical compound [Na+].C1=CC(OCC)=CC=C1NC1=CC=C(C(=C2C=CC(C=C2)=[N+](CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=2C=CC(=CC=2)N(CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=C1 NKLPQNGYXWVELD-UHFFFAOYSA-M 0.000 description 1
238000012258 culturing Methods 0.000 description 1
238000012217 deletion Methods 0.000 description 1
230000037430 deletion Effects 0.000 description 1
OZRNSSUDZOLUSN-LBPRGKRZSA-N dihydrofolic acid Chemical compound N=1C=2C(=O)NC(N)=NC=2NCC=1CNC1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 OZRNSSUDZOLUSN-LBPRGKRZSA-N 0.000 description 1
230000002526 effect on cardiovascular system Effects 0.000 description 1
238000010218 electron microscopic analysis Methods 0.000 description 1
230000008030 elimination Effects 0.000 description 1
238000003379 elimination reaction Methods 0.000 description 1
230000002708 enhancing effect Effects 0.000 description 1
ZMMJGEGLRURXTF-UHFFFAOYSA-N ethidium bromide Chemical compound [Br-].C12=CC(N)=CC=C2C2=CC=C(N)C=C2[N+](CC)=C1C1=CC=CC=C1 ZMMJGEGLRURXTF-UHFFFAOYSA-N 0.000 description 1
229960005542 ethidium bromide Drugs 0.000 description 1
210000003527 eukaryotic cell Anatomy 0.000 description 1
230000001747 exhibiting effect Effects 0.000 description 1
238000011049 filling Methods 0.000 description 1
229960004675 fusidic acid Drugs 0.000 description 1
IECPWNUMDGFDKC-MZJAQBGESA-N fusidic acid Chemical compound O[C@@H]([C@@H]12)C[C@H]3\C(=C(/CCC=C(C)C)C(O)=O)[C@@H](OC(C)=O)C[C@]3(C)[C@@]2(C)CC[C@@H]2[C@]1(C)CC[C@@H](O)[C@H]2C IECPWNUMDGFDKC-MZJAQBGESA-N 0.000 description 1
229940088597 hormone Drugs 0.000 description 1
239000005556 hormone Substances 0.000 description 1
230000002519 immonomodulatory effect Effects 0.000 description 1
230000001771 impaired effect Effects 0.000 description 1
239000000411 inducer Substances 0.000 description 1
230000006698 induction Effects 0.000 description 1
206010022000 influenza Diseases 0.000 description 1
229940079322 interferon Drugs 0.000 description 1
238000011835 investigation Methods 0.000 description 1
238000002955 isolation Methods 0.000 description 1
101150009839 lacF gene Proteins 0.000 description 1
229910001629 magnesium chloride Inorganic materials 0.000 description 1
FYYHWMGAXLPEAU-OUBTZVSYSA-N magnesium-25 atom Chemical compound [25Mg] FYYHWMGAXLPEAU-OUBTZVSYSA-N 0.000 description 1
201000004792 malaria Diseases 0.000 description 1
238000013507 mapping Methods 0.000 description 1
244000005700 microbiome Species 0.000 description 1
238000010369 molecular cloning Methods 0.000 description 1
238000002703 mutagenesis Methods 0.000 description 1
231100000350 mutagenesis Toxicity 0.000 description 1
239000013642 negative control Substances 0.000 description 1
231100000252 nontoxic Toxicity 0.000 description 1
230000003000 nontoxic effect Effects 0.000 description 1
238000012261 overproduction Methods 0.000 description 1
229910000160 potassium phosphate Inorganic materials 0.000 description 1
235000011009 potassium phosphates Nutrition 0.000 description 1
239000002243 precursor Substances 0.000 description 1
210000001236 prokaryotic cell Anatomy 0.000 description 1
238000001243 protein synthesis Methods 0.000 description 1
230000010076 replication Effects 0.000 description 1
210000003705 ribosome Anatomy 0.000 description 1
239000012723 sample buffer Substances 0.000 description 1
239000001632 sodium acetate Substances 0.000 description 1
235000017281 sodium acetate Nutrition 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
239000006228 supernatant Substances 0.000 description 1
229960003495 thiamine Drugs 0.000 description 1
DPJRMOMPQZCRJU-UHFFFAOYSA-M thiamine hydrochloride Chemical compound Cl.[Cl-].CC1=C(CCO)SC=[N+]1CC1=CN=C(C)N=C1N DPJRMOMPQZCRJU-UHFFFAOYSA-M 0.000 description 1
231100000419 toxicity Toxicity 0.000 description 1
230000001988 toxicity Effects 0.000 description 1
230000009466 transformation Effects 0.000 description 1
230000001131 transforming effect Effects 0.000 description 1
239000001226 triphosphate Substances 0.000 description 1
235000011178 triphosphate Nutrition 0.000 description 1
125000002264 triphosphate group Chemical class [H]OP(=O)(O[H])OP(=O)(O[H])OP(=O)(O[H])O* 0.000 description 1
LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
241001515965 unidentified phage Species 0.000 description 1
229960005486 vaccine Drugs 0.000 description 1
239000011691 vitamin B1 Substances 0.000 description 1
235000010374 vitamin B1 Nutrition 0.000 description 1
239000004246 zinc acetate Substances 0.000 description 1
DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 1

Classifications

- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/70—Vectors or expression systems specially adapted for E. coli

Landscapes

Genetics & Genomics (AREA)
Health & Medical Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
Engineering & Computer Science (AREA)
Wood Science & Technology (AREA)
Organic Chemistry (AREA)
Biomedical Technology (AREA)
Biotechnology (AREA)
General Engineering & Computer Science (AREA)
Chemical & Material Sciences (AREA)
Zoology (AREA)
Bioinformatics & Cheminformatics (AREA)
Biophysics (AREA)
Plant Pathology (AREA)
Molecular Biology (AREA)
Biochemistry (AREA)
General Health & Medical Sciences (AREA)
Physics & Mathematics (AREA)
Microbiology (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)
Micro-Organisms Or Cultivation Processes Thereof (AREA)
Saccharide Compounds (AREA)
Selective Calling Equipment (AREA)
Enzymes And Modification Thereof (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Medicines Containing Material From Animals Or Micro-Organisms (AREA)

DK198505843A 1984-12-17 1985-12-16 Ekspressionskontrol-DNA-sekvenser, ekspressionsvektorer, som indeholder disse DNA-sekvenser, transformanter som bærer disse ekspressionsvektorer, og fremgangsmåder til fremstilling af pro- og eukaryote proteiner under anvendelse af de DK175331B1 (da)

Applications Claiming Priority (2)

Application Number	Priority Date	Filing Date	Title
GB8431818		1984-12-17
GB848431818A GB8431818D0 (en)	1984-12-17	1984-12-17	Expression control sequence

Publications (3)

Publication Number	Publication Date
DK584385D0 DK584385D0 (da)	1985-12-16
DK584385A DK584385A (da)	1986-06-18
DK175331B1 true DK175331B1 (da)	2004-08-30

Family

ID=10571310

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
DK198505843A DK175331B1 (da)	1984-12-17	1985-12-16	Ekspressionskontrol-DNA-sekvenser, ekspressionsvektorer, som indeholder disse DNA-sekvenser, transformanter som bærer disse ekspressionsvektorer, og fremgangsmåder til fremstilling af pro- og eukaryote proteiner under anvendelse af de

Country Status (13)

Country	Link
EP (1)	EP0186069B1 (de)
JP (2)	JP2552650B2 (de)
AT (1)	ATE72677T1 (de)
AU (1)	AU589151B2 (de)
CA (1)	CA1318271C (de)
DE (1)	DE3585406D1 (de)
DK (1)	DK175331B1 (de)
GB (1)	GB8431818D0 (de)
IE (1)	IE58915B1 (de)
IL (1)	IL77330A (de)
NZ (1)	NZ214549A (de)
PH (1)	PH22137A (de)
ZA (1)	ZA859577B (de)

Families Citing this family (7)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US5232840A (en) *	1986-03-27	1993-08-03	Monsanto Company	Enhanced protein production in bacteria by employing a novel ribosome binding site
JPS63123383A (ja) *	1986-11-11	1988-05-27	Mitsubishi Kasei Corp	ハイブリツドプロモ−タ−、発現調節ｄｎａ配列および発現ベクタ−
DK443288A (da) *	1987-08-17	1989-02-18	Hoffmann La Roche	Ekspressionskontrolsekvenser
US7049102B1 (en)	1989-09-22	2006-05-23	Board Of Trustees Of Leland Stanford University	Multi-gene expression profile
US5246857A (en) *	1990-10-11	1993-09-21	Nitto Chemical Industry Co., Ltd.	Circular plasmids derived from the genus rhodococcus
WO2002051982A2 (en) *	2000-12-27	2002-07-04	Elitra Pharmaceuticals, Inc.	Bacterial promoters and methods of use
RU2225442C2 (ru)	2001-02-22	2004-03-10	Закрытое акционерное общество "Научно-исследовательский институт Аджиномото-Генетика"	Рекомбинантная днк для контроля экспрессии, способ контроля экспрессии целевого гена, способ получения целевого вещества

Family Cites Families (2)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
IL65775A (en) *	1981-05-18	1985-05-31	Genentech Inc	Microbial hybrid promotors and plasmids and e.coli comprising them
WO1985000831A1 (en) *	1983-08-10	1985-02-28	Amgen	Microbial expression of insulin-like growth factor

1984
- 1984-12-17 GB GB848431818A patent/GB8431818D0/en active Pending
1985
- 1985-12-13 NZ NZ214549A patent/NZ214549A/en unknown
- 1985-12-13 CA CA000497592A patent/CA1318271C/en not_active Expired - Lifetime
- 1985-12-13 DE DE8585115921T patent/DE3585406D1/de not_active Expired - Lifetime
- 1985-12-13 IL IL77330A patent/IL77330A/xx not_active IP Right Cessation
- 1985-12-13 ZA ZA859577A patent/ZA859577B/xx unknown
- 1985-12-13 EP EP85115921A patent/EP0186069B1/de not_active Expired - Lifetime
- 1985-12-13 AT AT85115921T patent/ATE72677T1/de not_active IP Right Cessation
- 1985-12-16 IE IE317785A patent/IE58915B1/en not_active IP Right Cessation
- 1985-12-16 DK DK198505843A patent/DK175331B1/da not_active IP Right Cessation
- 1985-12-16 JP JP60282699A patent/JP2552650B2/ja not_active Expired - Lifetime
- 1985-12-16 AU AU51257/85A patent/AU589151B2/en not_active Expired
- 1985-12-17 PH PH33185A patent/PH22137A/en unknown
1994
- 1994-05-09 JP JP6095174A patent/JP2515488B2/ja not_active Expired - Lifetime

Also Published As

Publication number	Publication date
DE3585406D1 (de)	1992-03-26
DK584385D0 (da)	1985-12-16
IL77330A (en)	1991-05-12
EP0186069A3 (en)	1988-01-13
JP2552650B2 (ja)	1996-11-13
EP0186069A2 (de)	1986-07-02
EP0186069B1 (de)	1992-02-19
IE58915B1 (en)	1993-12-01
CA1318271C (en)	1993-05-25
JPS61181386A (ja)	1986-08-14
ATE72677T1 (de)	1992-03-15
GB8431818D0 (en)	1985-01-30
AU5125785A (en)	1986-06-26
AU589151B2 (en)	1989-10-05
IE853177L (en)	1986-06-17
PH22137A (en)	1988-06-01
JP2515488B2 (ja)	1996-07-10
NZ214549A (en)	1988-02-12
ZA859577B (en)	1986-08-27
DK584385A (da)	1986-06-18
JPH0746994A (ja)	1995-02-21

Legal Events

Date	Code	Title	Description
2006-01-09	PUP	Patent expired

Publication	Publication Date	Title
DK175206B1 (da)	2004-07-12	Ekspressionskontrolsekvenser
US5965443A (en)	1999-10-12	System for in vitro transposition
JP2645217B2 (ja)	1997-08-25	植物細胞内で発現するキメラ遺伝子
DK171301B1 (da)	1996-08-26	Plasmid-vektorer, fremgangsmåde til fremstilling deraf samt fremgangsmåde til fremstilling af polypeptid
Baty et al.	1987	Extracellular release of colicin A is non‐specific.
US5232840A (en)	1993-08-03	Enhanced protein production in bacteria by employing a novel ribosome binding site
EP1019487A1 (de)	2000-07-19	Expressionskontrollsequenzen
Baldus et al.	1995	Evidence that the transcriptional activator Spo0A interacts with two sigma factors in Bacillus subtilis
Wood et al.	1983	Complementation of argG and hisA mutations of Escherichia coli by DNA cloned from the archaebacterium Methanococcus voltae
DK175331B1 (da)	2004-08-30	Ekspressionskontrol-DNA-sekvenser, ekspressionsvektorer, som indeholder disse DNA-sekvenser, transformanter som bærer disse ekspressionsvektorer, og fremgangsmåder til fremstilling af pro- og eukaryote proteiner under anvendelse af de
JPH10503090A (ja)	1998-03-24	低温での組換え蛋白質産生のためのベクターおよび形質転換宿主細胞
JP2544602B2 (ja)	1996-10-16	新規プラスミドベクタ−
Boyd et al.	1995	The pCLIP plasmids: versatile cloning vectors based on the bacteriophage λ origin of replication
AU708080B2 (en)	1999-07-29	Process for producing recombinant proteins, plasmids and modified cells
HU201116B (en)	1990-09-28	Process for producing plasmids having uncontrolled replication conduct under given circumstances
WO1990003438A1 (en)	1990-04-05	Improved bacterial strains for heterologous gene expression
JP2905921B2 (ja)	1999-06-14	細菌中に含まれるプラスミドの安定化方法
Allet et al.	1988	Purification and characterization of the DNA-binding protein Ner of bacteriophage Mu
Dennis et al.	1985	Autogenous posttranscriptional regulation of RNA polymerase beta and beta'subunit synthesis in Escherichia coli
EP0134673B1 (de)	1991-10-09	Plasmidvektor und seine Verwendung
HU197937B (en)	1989-06-28	Process for producing new cloning carriers usable for the expression of polypeptides in microbiological host cells
US5654169A (en)	1997-08-05	Vectors and transformed host cells for recombinant protein production at reduced temperatures
US5932714A (en)	1999-08-03	Expression of gene products from genetically manipulated strains of Bordetella
WO2000060103A2 (en)	2000-10-12	Dna construct comprising a cyanophage of cyanobacteria promoter and its use
EP0105554A1 (de)	1984-04-18	DNS und Plasmide