NO813759L - Plasmid, fremgangsmaate for fremstilling av et slikt produkt, samt anvendelse derav - Google Patents

Plasmid, fremgangsmaate for fremstilling av et slikt produkt, samt anvendelse derav

Info

Publication number: NO813759L
Authority: NO; Norway
Prior art keywords: site; hind iii; pst; pwt; ecori
Prior art date: 1980-11-10

Application number

NO813759A

Other languages

English (en)

Norwegian (no)

Inventor

William Charlse Albert Tacon

John Spencer Emtage

Andrew George Stewart

Norman Henry Carey

Michael Houghton

Original Assignee

Searle & Co

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.)

1980-11-10

Filing date

1981-11-06

Publication date

1982-05-11

1981-11-06 Application filed by Searle & Co filed Critical Searle & Co

1982-05-11 Publication of NO813759L publication Critical patent/NO813759L/no

Links

239000013612 plasmid Substances 0.000 title claims description 150
238000000034 method Methods 0.000 title description 37
238000004519 manufacturing process Methods 0.000 title description 22
239000012634 fragment Substances 0.000 claims description 168
108020004414 DNA Proteins 0.000 claims description 70
230000001580 bacterial effect Effects 0.000 claims description 18
238000003780 insertion Methods 0.000 claims description 17
230000037431 insertion Effects 0.000 claims description 17
108091081024 Start codon Proteins 0.000 claims description 8
125000002707 L-tryptophyl group Chemical group [H]C1=C([H])C([H])=C2C(C([C@](N([H])[H])(C(=O)[*])[H])([H])[H])=C([H])N([H])C2=C1[H] 0.000 description 114
108090000623 proteins and genes Proteins 0.000 description 72
QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 51
QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 51
108090000765 processed proteins & peptides Proteins 0.000 description 51
229960004799 tryptophan Drugs 0.000 description 51
230000014509 gene expression Effects 0.000 description 31
238000005520 cutting process Methods 0.000 description 30
230000035897 transcription Effects 0.000 description 30
238000013518 transcription Methods 0.000 description 30
210000004027 cell Anatomy 0.000 description 28
239000004098 Tetracycline Substances 0.000 description 26
229960002180 tetracycline Drugs 0.000 description 26
229930101283 tetracycline Natural products 0.000 description 26
235000019364 tetracycline Nutrition 0.000 description 26
150000003522 tetracyclines Chemical class 0.000 description 26
238000010367 cloning Methods 0.000 description 24
102000004169 proteins and genes Human genes 0.000 description 22
102000004594 DNA Polymerase I Human genes 0.000 description 21
108010017826 DNA Polymerase I Proteins 0.000 description 21
238000011144 upstream manufacturing Methods 0.000 description 19
LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 18
241001646716 Escherichia coli K-12 Species 0.000 description 17
150000001413 amino acids Chemical class 0.000 description 17
230000015572 biosynthetic process Effects 0.000 description 17
239000012071 phase Substances 0.000 description 17
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 16
229960000723 ampicillin Drugs 0.000 description 16
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 16
239000000499 gel Substances 0.000 description 16
229920001184 polypeptide Polymers 0.000 description 16
102000004196 processed proteins & peptides Human genes 0.000 description 16
238000013519 translation Methods 0.000 description 16
HRPVXLWXLXDGHG-UHFFFAOYSA-N Acrylamide Chemical compound NC(=O)C=C HRPVXLWXLXDGHG-UHFFFAOYSA-N 0.000 description 14
241000588724 Escherichia coli Species 0.000 description 14
239000002773 nucleotide Substances 0.000 description 14
125000003729 nucleotide group Chemical group 0.000 description 14
239000000047 product Substances 0.000 description 13
238000006243 chemical reaction Methods 0.000 description 12
239000013613 expression plasmid Substances 0.000 description 12
230000008439 repair process Effects 0.000 description 12
230000029087 digestion Effects 0.000 description 11
FPPNZSSZRUTDAP-UWFZAAFLSA-N carbenicillin Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)C(C(O)=O)C1=CC=CC=C1 FPPNZSSZRUTDAP-UWFZAAFLSA-N 0.000 description 10
229960003669 carbenicillin Drugs 0.000 description 10
239000000203 mixture Substances 0.000 description 10
238000003786 synthesis reaction Methods 0.000 description 10
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 9
102000004163 DNA-directed RNA polymerases Human genes 0.000 description 9
108090000626 DNA-directed RNA polymerases Proteins 0.000 description 9
238000001962 electrophoresis Methods 0.000 description 9
239000006916 nutrient agar Substances 0.000 description 9
HEDRZPFGACZZDS-UHFFFAOYSA-N Chloroform Chemical compound ClC(Cl)Cl HEDRZPFGACZZDS-UHFFFAOYSA-N 0.000 description 8
ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 8
239000000427 antigen Substances 0.000 description 8
108091007433 antigens Proteins 0.000 description 8
102000036639 antigens Human genes 0.000 description 8
210000003705 ribosome Anatomy 0.000 description 8
239000011780 sodium chloride Substances 0.000 description 8
229920001817 Agar Polymers 0.000 description 7
108020004774 Alkaline Phosphatase Proteins 0.000 description 7
108020004705 Codon Proteins 0.000 description 7
239000008272 agar Substances 0.000 description 7
239000006166 lysate Substances 0.000 description 7
238000012360 testing method Methods 0.000 description 7
108091032973 (ribonucleotides)n+m Proteins 0.000 description 6
102000002260 Alkaline Phosphatase Human genes 0.000 description 6
TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 6
230000008901 benefit Effects 0.000 description 6
238000000338 in vitro Methods 0.000 description 6
238000001727 in vivo Methods 0.000 description 6
239000002609 medium Substances 0.000 description 6
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 6
108091026890 Coding region Proteins 0.000 description 5
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 5
102000004190 Enzymes Human genes 0.000 description 5
108090000790 Enzymes Proteins 0.000 description 5
101710163270 Nuclease Proteins 0.000 description 5
108091028043 Nucleic acid sequence Proteins 0.000 description 5
239000002253 acid Substances 0.000 description 5
150000007513 acids Chemical class 0.000 description 5
238000010276 construction Methods 0.000 description 5
VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 5
229940088598 enzyme Drugs 0.000 description 5
230000004927 fusion Effects 0.000 description 5
238000005304 joining Methods 0.000 description 5
230000035945 sensitivity Effects 0.000 description 5
239000013598 vector Substances 0.000 description 5
101150039660 HA gene Proteins 0.000 description 4
DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 4
229920004890 Triton X-100 Polymers 0.000 description 4
239000013504 Triton X-100 Substances 0.000 description 4
238000005119 centrifugation Methods 0.000 description 4
238000003776 cleavage reaction Methods 0.000 description 4
239000002131 composite material Substances 0.000 description 4
239000012153 distilled water Substances 0.000 description 4
230000000694 effects Effects 0.000 description 4
238000009585 enzyme analysis Methods 0.000 description 4
239000003999 initiator Substances 0.000 description 4
230000001788 irregular Effects 0.000 description 4
108020004999 messenger RNA Proteins 0.000 description 4
239000002243 precursor Substances 0.000 description 4
238000002360 preparation method Methods 0.000 description 4
238000011084 recovery Methods 0.000 description 4
108091008146 restriction endonucleases Proteins 0.000 description 4
230000007017 scission Effects 0.000 description 4
230000005030 transcription termination Effects 0.000 description 4
DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 4
102000016928 DNA-directed DNA polymerase Human genes 0.000 description 3
108010014303 DNA-directed DNA polymerase Proteins 0.000 description 3
108010010803 Gelatin Proteins 0.000 description 3
108700039691 Genetic Promoter Regions Proteins 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
108010050904 Interferons Proteins 0.000 description 3
239000007836 KH2PO4 Substances 0.000 description 3
102000016943 Muramidase Human genes 0.000 description 3
108010014251 Muramidase Proteins 0.000 description 3
108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 3
HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
MZVQCMJNVPIDEA-UHFFFAOYSA-N [CH2]CN(CC)CC Chemical compound [CH2]CN(CC)CC MZVQCMJNVPIDEA-UHFFFAOYSA-N 0.000 description 3
230000015556 catabolic process Effects 0.000 description 3
230000008859 change Effects 0.000 description 3
239000007795 chemical reaction product Substances 0.000 description 3
239000000539 dimer Substances 0.000 description 3
238000001502 gel electrophoresis Methods 0.000 description 3
239000008273 gelatin Substances 0.000 description 3
229920000159 gelatin Polymers 0.000 description 3
235000019322 gelatine Nutrition 0.000 description 3
235000011852 gelatine desserts Nutrition 0.000 description 3
239000008103 glucose Substances 0.000 description 3
230000006698 induction Effects 0.000 description 3
230000005764 inhibitory process Effects 0.000 description 3
230000001665 lethal effect Effects 0.000 description 3
229960000274 lysozyme Drugs 0.000 description 3
239000004325 lysozyme Substances 0.000 description 3
235000010335 lysozyme Nutrition 0.000 description 3
229910001629 magnesium chloride Inorganic materials 0.000 description 3
229910000402 monopotassium phosphate Inorganic materials 0.000 description 3
235000019796 monopotassium phosphate Nutrition 0.000 description 3
235000015097 nutrients Nutrition 0.000 description 3
GNSKLFRGEWLPPA-UHFFFAOYSA-M potassium dihydrogen phosphate Chemical compound [K+].OP(O)([O-])=O GNSKLFRGEWLPPA-UHFFFAOYSA-M 0.000 description 3
230000001105 regulatory effect Effects 0.000 description 3
239000000523 sample Substances 0.000 description 3
238000012163 sequencing technique Methods 0.000 description 3
230000009466 transformation Effects 0.000 description 3
239000011534 wash buffer Substances 0.000 description 3
108020004465 16S ribosomal RNA Proteins 0.000 description 2
102100039986 Apoptosis inhibitor 5 Human genes 0.000 description 2
108091003079 Bovine Serum Albumin Proteins 0.000 description 2
239000004971 Cross linker Substances 0.000 description 2
101710204837 Envelope small membrane protein Proteins 0.000 description 2
108060002716 Exonuclease Proteins 0.000 description 2
108020005004 Guide RNA Proteins 0.000 description 2
101150017040 I gene Proteins 0.000 description 2
102000014150 Interferons Human genes 0.000 description 2
108010054278 Lac Repressors Proteins 0.000 description 2
101710145006 Lysis protein Proteins 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
LRHPLDYGYMQRHN-UHFFFAOYSA-N N-Butanol Chemical compound CCCCO LRHPLDYGYMQRHN-UHFFFAOYSA-N 0.000 description 2
108091034117 Oligonucleotide Proteins 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
241000700605 Viruses Species 0.000 description 2
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 2
125000003275 alpha amino acid group Chemical group 0.000 description 2
238000004458 analytical method Methods 0.000 description 2
238000003556 assay Methods 0.000 description 2
230000033228 biological regulation Effects 0.000 description 2
229940098773 bovine serum albumin Drugs 0.000 description 2
239000000872 buffer Substances 0.000 description 2
230000001413 cellular effect Effects 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
230000008878 coupling Effects 0.000 description 2
238000010168 coupling process Methods 0.000 description 2
238000005859 coupling reaction Methods 0.000 description 2
238000004132 cross linking Methods 0.000 description 2
239000011243 crosslinked material Substances 0.000 description 2
230000009089 cytolysis Effects 0.000 description 2
230000002950 deficient Effects 0.000 description 2
238000006731 degradation reaction Methods 0.000 description 2
229910000397 disodium phosphate Inorganic materials 0.000 description 2
238000009826 distribution Methods 0.000 description 2
108010052305 exodeoxyribonuclease III Proteins 0.000 description 2
102000013165 exonuclease Human genes 0.000 description 2
238000000605 extraction Methods 0.000 description 2
239000012467 final product Substances 0.000 description 2
238000011534 incubation Methods 0.000 description 2
230000000977 initiatory effect Effects 0.000 description 2
229940079322 interferon Drugs 0.000 description 2
238000002955 isolation Methods 0.000 description 2
231100000518 lethal Toxicity 0.000 description 2
239000000463 material Substances 0.000 description 2
125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 2
238000006386 neutralization reaction Methods 0.000 description 2
108020004707 nucleic acids Proteins 0.000 description 2
102000039446 nucleic acids Human genes 0.000 description 2
150000007523 nucleic acids Chemical class 0.000 description 2
238000012261 overproduction Methods 0.000 description 2
239000013600 plasmid vector Substances 0.000 description 2
239000011541 reaction mixture Substances 0.000 description 2
150000003839 salts Chemical class 0.000 description 2
239000000126 substance Substances 0.000 description 2
239000005720 sucrose Substances 0.000 description 2
229960003495 thiamine Drugs 0.000 description 2
RWQNBRDOKXIBIV-UHFFFAOYSA-N thymine Chemical compound CC1=CNC(=O)NC1=O RWQNBRDOKXIBIV-UHFFFAOYSA-N 0.000 description 2
230000001131 transforming effect Effects 0.000 description 2
BHNQPLPANNDEGL-UHFFFAOYSA-N 2-(4-octylphenoxy)ethanol Chemical compound CCCCCCCCC1=CC=C(OCCO)C=C1 BHNQPLPANNDEGL-UHFFFAOYSA-N 0.000 description 1
102100025677 Alkaline phosphatase, germ cell type Human genes 0.000 description 1
101000640990 Arabidopsis thaliana Tryptophan-tRNA ligase, chloroplastic/mitochondrial Proteins 0.000 description 1
241000894006 Bacteria Species 0.000 description 1
108700003860 Bacterial Genes Proteins 0.000 description 1
UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 1
241000283707 Capra Species 0.000 description 1
241000282693 Cercopithecidae Species 0.000 description 1
108090000317 Chymotrypsin Proteins 0.000 description 1
108050006400 Cyclin Proteins 0.000 description 1
102000012410 DNA Ligases Human genes 0.000 description 1
108010061982 DNA Ligases Proteins 0.000 description 1
102100033195 DNA ligase 4 Human genes 0.000 description 1
229920001425 Diethylaminoethyl cellulose Polymers 0.000 description 1
QXNVGIXVLWOKEQ-UHFFFAOYSA-N Disodium Chemical class [Na][Na] QXNVGIXVLWOKEQ-UHFFFAOYSA-N 0.000 description 1
101150013191 E gene Proteins 0.000 description 1
102100031780 Endonuclease Human genes 0.000 description 1
108010042407 Endonucleases Proteins 0.000 description 1
BRLQWZUYTZBJKN-UHFFFAOYSA-N Epichlorohydrin Chemical compound ClCC1CO1 BRLQWZUYTZBJKN-UHFFFAOYSA-N 0.000 description 1
241001302584 Escherichia coli str. K-12 substr. W3110 Species 0.000 description 1
229920001917 Ficoll Polymers 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
102000006992 Interferon-alpha Human genes 0.000 description 1
108010047761 Interferon-alpha Proteins 0.000 description 1
241001625930 Luria Species 0.000 description 1
241000283973 Oryctolagus cuniculus Species 0.000 description 1
108091005804 Peptidases Proteins 0.000 description 1
241000276498 Pollachius virens Species 0.000 description 1
239000004793 Polystyrene Substances 0.000 description 1
102100036691 Proliferating cell nuclear antigen Human genes 0.000 description 1
239000004365 Protease Substances 0.000 description 1
101100408135 Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) phnA gene Proteins 0.000 description 1
102000001218 Rec A Recombinases Human genes 0.000 description 1
108010055016 Rec A Recombinases Proteins 0.000 description 1
108020004511 Recombinant DNA Proteins 0.000 description 1
108700005075 Regulator Genes Proteins 0.000 description 1
108010034634 Repressor Proteins Proteins 0.000 description 1
102000009661 Repressor Proteins Human genes 0.000 description 1
102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 1
102000006382 Ribonucleases Human genes 0.000 description 1
108010083644 Ribonucleases Proteins 0.000 description 1
229920005654 Sephadex Polymers 0.000 description 1
239000012507 Sephadex™ Substances 0.000 description 1
JZRWCGZRTZMZEH-UHFFFAOYSA-N Thiamine Natural products CC1=C(CCO)SC=[N+]1CC1=CN=C(C)N=C1N JZRWCGZRTZMZEH-UHFFFAOYSA-N 0.000 description 1
239000007984 Tris EDTA buffer Substances 0.000 description 1
QJIOKZXDGFZQJP-OYDLWJJNSA-N Trp-Trp-Arg Chemical group [H]N[C@@H](CC1=CNC2=C1C=CC=C2)C(=O)N[C@@H](CC1=CNC2=C1C=CC=C2)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O QJIOKZXDGFZQJP-OYDLWJJNSA-N 0.000 description 1
108090000631 Trypsin Proteins 0.000 description 1
102000004142 Trypsin Human genes 0.000 description 1
102000002501 Tryptophan-tRNA Ligase Human genes 0.000 description 1
229930003451 Vitamin B1 Natural products 0.000 description 1
108091060592 XDNA Proteins 0.000 description 1
XPAOKCSHUNYPBS-XSBNNCSWSA-N [(2r,3s,5r)-5-(6-aminopurin-9-yl)-3-hydroxyoxolan-2-yl]methyl [(2r,3r,5s)-3-(hydroxymethyl)-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl] hydrogen phosphate Chemical compound O=C1NC(=O)C(C)=CN1[C@H]1O[C@H](OP(O)(=O)OC[C@@H]2[C@H](C[C@@H](O2)N2C3=NC=NC(N)=C3N=C2)O)[C@@H](CO)C1 XPAOKCSHUNYPBS-XSBNNCSWSA-N 0.000 description 1
239000000654 additive Substances 0.000 description 1
GFFGJBXGBJISGV-UHFFFAOYSA-N adenyl group Chemical class N1=CN=C2N=CNC2=C1N GFFGJBXGBJISGV-UHFFFAOYSA-N 0.000 description 1
238000000246 agarose gel electrophoresis Methods 0.000 description 1
238000012870 ammonium sulfate precipitation Methods 0.000 description 1
230000000840 anti-viral effect Effects 0.000 description 1
230000009286 beneficial effect Effects 0.000 description 1
102000005936 beta-Galactosidase Human genes 0.000 description 1
108010005774 beta-Galactosidase Proteins 0.000 description 1
UDSAIICHUKSCKT-UHFFFAOYSA-N bromophenol blue Chemical compound C1=C(Br)C(O)=C(Br)C=C1C1(C=2C=C(Br)C(O)=C(Br)C=2)C2=CC=CC=C2S(=O)(=O)O1 UDSAIICHUKSCKT-UHFFFAOYSA-N 0.000 description 1
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
229940041514 candida albicans extract Drugs 0.000 description 1
239000001913 cellulose Substances 0.000 description 1
229920002678 cellulose Polymers 0.000 description 1
210000000349 chromosome Anatomy 0.000 description 1
229960002376 chymotrypsin Drugs 0.000 description 1
238000012790 confirmation Methods 0.000 description 1
230000001276 controlling effect Effects 0.000 description 1
229920001577 copolymer Polymers 0.000 description 1
238000012937 correction Methods 0.000 description 1
230000000120 cytopathologic effect Effects 0.000 description 1
SUYVUBYJARFZHO-RRKCRQDMSA-N dATP Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@H]1C[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 SUYVUBYJARFZHO-RRKCRQDMSA-N 0.000 description 1
SUYVUBYJARFZHO-UHFFFAOYSA-N dATP Natural products C1=NC=2C(N)=NC=NC=2N1C1CC(O)C(COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 SUYVUBYJARFZHO-UHFFFAOYSA-N 0.000 description 1
RGWHQCVHVJXOKC-SHYZEUOFSA-J dCTP(4-) Chemical compound O=C1N=C(N)C=CN1[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)C1 RGWHQCVHVJXOKC-SHYZEUOFSA-J 0.000 description 1
HAAZLUGHYHWQIW-KVQBGUIXSA-N dGTP Chemical compound C1=NC=2C(=O)NC(N)=NC=2N1[C@H]1C[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 HAAZLUGHYHWQIW-KVQBGUIXSA-N 0.000 description 1
NHVNXKFIZYSCEB-XLPZGREQSA-N dTTP Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)[C@@H](O)C1 NHVNXKFIZYSCEB-XLPZGREQSA-N 0.000 description 1
230000007812 deficiency Effects 0.000 description 1
239000007857 degradation product Substances 0.000 description 1
230000000593 degrading effect Effects 0.000 description 1
230000001419 dependent effect Effects 0.000 description 1
239000003599 detergent Substances 0.000 description 1
230000002900 effect on cell Effects 0.000 description 1
239000012636 effector Substances 0.000 description 1
238000005516 engineering process Methods 0.000 description 1
230000002255 enzymatic effect Effects 0.000 description 1
238000006911 enzymatic reaction Methods 0.000 description 1
ZMMJGEGLRURXTF-UHFFFAOYSA-N ethidium bromide Chemical compound [Br-].C12=CC(N)=CC=C2C2=CC=C(N)C=C2[N+](CC)=C1C1=CC=CC=C1 ZMMJGEGLRURXTF-UHFFFAOYSA-N 0.000 description 1
229960005542 ethidium bromide Drugs 0.000 description 1
238000001400 expression cloning Methods 0.000 description 1
239000011536 extraction buffer Substances 0.000 description 1
239000000706 filtrate Substances 0.000 description 1
235000003642 hunger Nutrition 0.000 description 1
230000002209 hydrophobic effect Effects 0.000 description 1
230000002401 inhibitory effect Effects 0.000 description 1
238000011081 inoculation Methods 0.000 description 1
230000003993 interaction Effects 0.000 description 1
238000011031 large-scale manufacturing process Methods 0.000 description 1
239000007788 liquid Substances 0.000 description 1
238000011068 loading method Methods 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
239000012528 membrane Substances 0.000 description 1
230000004048 modification Effects 0.000 description 1
238000012986 modification Methods 0.000 description 1
229940056360 penicillin g Drugs 0.000 description 1
LQRJAEQXMSMEDP-XCHBZYMASA-N peptide a Chemical compound N([C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](C)C(=O)NCCCC[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](CC=1C2=CC=CC=C2NC=1)NC(=O)C(\NC(=O)[C@@H](CCCCN)NC(=O)CNC(C)=O)=C/C=1C=CC=CC=1)C(N)=O)C(=O)C(\NC(=O)[C@@H](CCCCN)NC(=O)CNC(C)=O)=C\C1=CC=CC=C1 LQRJAEQXMSMEDP-XCHBZYMASA-N 0.000 description 1
229920002223 polystyrene Polymers 0.000 description 1
230000012743 protein tagging Effects 0.000 description 1
238000003127 radioimmunoassay Methods 0.000 description 1
230000003134 recirculating effect Effects 0.000 description 1
230000009467 reduction Effects 0.000 description 1
238000011160 research Methods 0.000 description 1
230000004044 response Effects 0.000 description 1
210000002966 serum Anatomy 0.000 description 1
IFGCUJZIWBUILZ-UHFFFAOYSA-N sodium 2-[[2-[[hydroxy-(3,4,5-trihydroxy-6-methyloxan-2-yl)oxyphosphoryl]amino]-4-methylpentanoyl]amino]-3-(1H-indol-3-yl)propanoic acid Chemical compound [Na+].C=1NC2=CC=CC=C2C=1CC(C(O)=O)NC(=O)C(CC(C)C)NP(O)(=O)OC1OC(C)C(O)C(O)C1O IFGCUJZIWBUILZ-UHFFFAOYSA-N 0.000 description 1
159000000000 sodium salts Chemical class 0.000 description 1
239000007790 solid phase Substances 0.000 description 1
238000000527 sonication Methods 0.000 description 1
239000006228 supernatant Substances 0.000 description 1
KYMBYSLLVAOCFI-UHFFFAOYSA-N thiamine Chemical compound CC1=C(CCO)SCN1CC1=CN=C(C)N=C1N KYMBYSLLVAOCFI-UHFFFAOYSA-N 0.000 description 1
235000019157 thiamine Nutrition 0.000 description 1
239000011721 thiamine Substances 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
229940113082 thymine Drugs 0.000 description 1
210000001519 tissue Anatomy 0.000 description 1
230000005026 transcription initiation Effects 0.000 description 1
230000002463 transducing effect Effects 0.000 description 1
238000000844 transformation Methods 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
101150044170 trpE gene Proteins 0.000 description 1
239000012588 trypsin Substances 0.000 description 1
239000012137 tryptone Substances 0.000 description 1
230000007306 turnover Effects 0.000 description 1
230000035899 viability Effects 0.000 description 1
230000029812 viral genome replication Effects 0.000 description 1
239000011691 vitamin B1 Substances 0.000 description 1
235000010374 vitamin B1 Nutrition 0.000 description 1
239000012138 yeast extract Substances 0.000 description 1

Classifications

- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/005—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from viruses
- 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
- C12N15/66—General methods for inserting a gene into a vector to form a recombinant vector using cleavage and ligation; Use of non-functional linkers or adaptors, e.g. linkers containing the sequence for a restriction endonuclease
- 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
- C12N15/71—Expression systems using regulatory sequences derived from the trp-operon
- 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
- C12N2760/00—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA ssRNA viruses negative-sense
- C12N2760/00011—Details
- C12N2760/16011—Orthomyxoviridae
- C12N2760/16111—Influenzavirus A, i.e. influenza A virus
- C12N2760/16122—New viral proteins or individual genes, new structural or functional aspects of known viral proteins or genes

Landscapes

Health & Medical Sciences (AREA)
Genetics & Genomics (AREA)
Life Sciences & Earth Sciences (AREA)
Chemical & Material Sciences (AREA)
Engineering & Computer Science (AREA)
Organic Chemistry (AREA)
Wood Science & Technology (AREA)
Biomedical Technology (AREA)
Biotechnology (AREA)
General Engineering & Computer Science (AREA)
Molecular Biology (AREA)
Bioinformatics & Cheminformatics (AREA)
Zoology (AREA)
Biophysics (AREA)
Biochemistry (AREA)
General Health & Medical Sciences (AREA)
Microbiology (AREA)
Plant Pathology (AREA)
Physics & Mathematics (AREA)
Virology (AREA)
Gastroenterology & Hepatology (AREA)
Medicinal Chemistry (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Saccharide Compounds (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)
Micro-Organisms Or Cultivation Processes Thereof (AREA)

NO813759A 1980-11-10 1981-11-06 Plasmid, fremgangsmaate for fremstilling av et slikt produkt, samt anvendelse derav NO813759L (no)

Applications Claiming Priority (1)

Application Number	Priority Date	Filing Date	Title
GB8036080		1980-11-10

Publications (1)

Publication Number	Publication Date
NO813759L true NO813759L (no)	1982-05-11

Family

ID=10517203

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
NO813759A NO813759L (no)	1980-11-10	1981-11-06	Plasmid, fremgangsmaate for fremstilling av et slikt produkt, samt anvendelse derav

Country Status (8)

Country	Link
EP (1)	EP0052002A3 (fr)
JP (1)	JPS57163396A (fr)
AU (1)	AU7731281A (fr)
DK (1)	DK489481A (fr)
ES (1)	ES506994A0 (fr)
NO (1)	NO813759L (fr)
PT (1)	PT73945B (fr)
ZA (1)	ZA817735B (fr)

Families Citing this family (15)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
ZA811368B (en) *	1980-03-24	1982-04-28	Genentech Inc	Bacterial polypedtide expression employing tryptophan promoter-operator
US5833975A (en) *	1989-03-08	1998-11-10	Virogenetics Corporation	Canarypox virus expressing cytokine and/or tumor-associated antigen DNA sequence
US5174993A (en) *	1981-12-24	1992-12-29	Health Research Inc.	Recombinant avipox virus and immunological use thereof
US7767449B1 (en)	1981-12-24	2010-08-03	Health Research Incorporated	Methods using modified vaccinia virus
US4582800A (en) *	1982-07-12	1986-04-15	Hoffmann-La Roche Inc.	Novel vectors and method for controlling interferon expression
WO1984000380A1 (fr) *	1982-07-13	1984-02-02	Celltech Ltd	Vecteur
AU575301B2 (en) *	1982-10-08	1988-07-28	Juridical Foundation, Japanese Foundation For Cancer Research	Novel vector
US4559300A (en) *	1983-01-18	1985-12-17	Eli Lilly And Company	Method for using an homologous bacillus promoter and associated natural or modified ribosome binding site-containing DNA sequence in streptomyces
EP0147178B1 (fr) *	1983-12-23	1991-08-14	Pfizer Inc.	Plasmides d'expression pour la produciton de protéines héterologues dans des bactéries
US4935370A (en) *	1983-12-23	1990-06-19	Pfizer Inc.	Expression plasmids for improved production of heterologous protein in bacteria
US4663281A (en) *	1984-03-22	1987-05-05	Mass Institute Of Technology	Enhanced production of proteinaceous materials in eucaryotic cells
CA1338664C (fr) *	1985-04-10	1996-10-22	Cetus Oncology Corporation	Hotes recombinants
AU582288B2 (en) *	1986-03-07	1989-03-16	Damon Biotech Inc.	Vector and method for achieving high level expression in eukaryotic cells
DE10399032I1 (de) *	1987-08-28	2004-01-29	Health Research Inc	Rekombinante Viren.
US7049102B1 (en)	1989-09-22	2006-05-23	Board Of Trustees Of Leland Stanford University	Multi-gene expression profile

Family Cites Families (5)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
GB2068970B (en) *	1980-02-06	1983-06-22	Searle & Co	Recombinant dna technique for the preparation of a protein resembling human interferon
ZA811368B (en) *	1980-03-24	1982-04-28	Genentech Inc	Bacterial polypedtide expression employing tryptophan promoter-operator
CH651308A5 (de) *	1980-07-01	1985-09-13	Hoffmann La Roche	Interferone und deren herstellung.
NZ198445A (en) *	1980-09-25	1984-05-31	Genentech Inc	Production of human fibroblast interferon by recombinant dna technology
BR8108074A (pt) *	1980-12-12	1982-09-21	Unilever Nv	Sequencia de dna,plasmidio recombinante,ligadores de dna,cultura bacterial e processo para produzir taumatina

1981
- 1981-11-04 DK DK489481A patent/DK489481A/da not_active Application Discontinuation
- 1981-11-06 NO NO813759A patent/NO813759L/no unknown
- 1981-11-09 PT PT73945A patent/PT73945B/pt unknown
- 1981-11-09 EP EP81305308A patent/EP0052002A3/fr not_active Withdrawn
- 1981-11-09 AU AU77312/81A patent/AU7731281A/en not_active Abandoned
- 1981-11-09 ZA ZA817735A patent/ZA817735B/xx unknown
- 1981-11-10 JP JP56180262A patent/JPS57163396A/ja active Pending
- 1981-11-10 ES ES506994A patent/ES506994A0/es active Granted

Also Published As

Publication number	Publication date
ES8304199A1 (es)	1983-02-16
ES506994A0 (es)	1983-02-16
EP0052002A3 (fr)	1983-03-16
PT73945B (en)	1983-04-18
DK489481A (da)	1982-05-11
AU7731281A (en)	1982-05-20
ZA817735B (en)	1982-10-27
JPS57163396A (en)	1982-10-07
PT73945A (en)	1981-12-01
EP0052002A2 (fr)	1982-05-19

Publication	Publication Date	Title
US5082783A (en)	1992-01-21	Enhanced secretion of heterologous proteins by hosts using substituted promoters
Chang et al.	1987	High-level secretion of human growth hormone by Escherichia coli
DK173092B1 (da)	2000-01-10	Rekombinant plasmid, fremgangsmåde til fremstilling af plasmidet, bakterie indeholdende plasmidet, samt fremgangsmåde til f
Kaster et al.	1983	Analysis of a bacterial hygromycin B resistance gene by transcriptional and translational fusions and by DNA sequencing
AU625554B2 (en)	1992-07-16	CKS method of protein synthesis
CA2122135C (fr)	1999-12-21	Streptavidine recombinante
NO830780L (no)	1983-09-09	Uttrykking, behandling og sekresjon av heterologt protein av gjaer
JPH0776596A (ja)	1995-03-20	ペプチド、融合ペプチド、発現ベクター及び組換えタンパク質の製造方法
NO158880B (no)	1988-08-01	Fremgangsmaate for fremstilling av et spesifikt pattedyrhormon.
IE63126B1 (en)	1995-03-22	Improved vectors and methods for making such vectors and for expressing cloned genes
JPH09135691A (ja)	1997-05-27	牛のプレ成長および成長ホルモンの製造方法
NO783724L (no)	1979-05-09	Syntetisk dna samt fremgangsmaate til dets fremstilling
AU607973B2 (en)	1991-03-21	Process for production of physiologically active peptide containing cysteine residue
EP0052002A2 (fr)	1982-05-19	Plasmides-vecteurs, leur production et utilisation
NO301285B1 (no)	1997-10-06	DNA-sekvens som koder for det regulatoriske område for alkoholoksidase II hos Pichia pastoris
NO175871B (fr)	1994-09-12
NO178035B (no)	1995-10-02	Ekspressjonsvektor, gjærcelle som er i stand til å utskille desulfatohirudin samt fremgangsmåte for fremstilling av et terapeutisk aktivt desulfatohirudin
AP80A (en)	1990-04-16	Expression of HIV binding proteins.
JPH0376580A (ja)	1991-04-02	大腸菌発現ベクターとそれを利用した抗ウイルス性タンパク質の製造方法
US5401642A (en)	1995-03-28	Vectors and methods for making such vectors and for expressing cloned genes
WO1991009952A1 (fr)	1991-07-11	Peptide a signal lipoproteique fusionne avec des polypeptides antigeniques
NZ207925A (en)	1988-05-30	Yeast expression vehicle consisting of a yeast promoter and signal peptide encoding region linked to a heterologus peptide coding region; expression and culture
EP1714972B1 (fr)	2011-10-19	Méthode pour produire un peptide avec un pI supérieur à 8 ou inférieur à 5
WO1999053033A1 (fr)	1999-10-21	Procedes et compositions de production a fort rendement de proteines eukaryotes
Maclntyre et al.	1991	Requirement of the SecB chaperone for export of a non-secretory polypeptide in Escherichia coli