NO811119L - Forbedrede baerere, samt fremgangsmaate ved fremstilling av disse og for aa uttrykke klonede gener - Google Patents
Forbedrede baerere, samt fremgangsmaate ved fremstilling av disse og for aa uttrykke klonede generInfo
- Publication number
- NO811119L NO811119L NO811119A NO811119A NO811119L NO 811119 L NO811119 L NO 811119L NO 811119 A NO811119 A NO 811119A NO 811119 A NO811119 A NO 811119A NO 811119 L NO811119 L NO 811119L
- Authority
- NO
- Norway
- Prior art keywords
- promoter
- fragment
- gene
- dna
- bamhi
- Prior art date
Links
- 108090000623 proteins and genes Proteins 0.000 title claims description 166
- 238000000034 method Methods 0.000 title claims description 36
- 238000004519 manufacturing process Methods 0.000 title claims description 10
- 239000000969 carrier Substances 0.000 title description 6
- 239000012634 fragment Substances 0.000 claims description 137
- 239000013598 vector Substances 0.000 claims description 91
- 102000004169 proteins and genes Human genes 0.000 claims description 57
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 37
- 108020004511 Recombinant DNA Proteins 0.000 claims description 18
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 18
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 18
- 102000004190 Enzymes Human genes 0.000 claims description 17
- 108090000790 Enzymes Proteins 0.000 claims description 17
- 229920001184 polypeptide Polymers 0.000 claims description 17
- 241001515965 unidentified phage Species 0.000 claims description 15
- 102000053602 DNA Human genes 0.000 claims description 12
- 239000000427 antigen Substances 0.000 claims description 12
- 102000036639 antigens Human genes 0.000 claims description 12
- 108091007433 antigens Proteins 0.000 claims description 12
- 108010026228 mRNA guanylyltransferase Proteins 0.000 claims description 11
- 108010042407 Endonucleases Proteins 0.000 claims description 10
- 241000709744 Enterobacterio phage MS2 Species 0.000 claims description 7
- 150000001413 amino acids Chemical class 0.000 claims description 7
- 102000003996 Interferon-beta Human genes 0.000 claims description 5
- 108090000467 Interferon-beta Proteins 0.000 claims description 5
- 239000005556 hormone Substances 0.000 claims description 4
- 229940088597 hormone Drugs 0.000 claims description 4
- NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 claims description 4
- 230000003612 virological effect Effects 0.000 claims description 4
- 241001465754 Metazoa Species 0.000 claims description 3
- 241000700605 Viruses Species 0.000 claims description 3
- 102000004877 Insulin Human genes 0.000 claims description 2
- 108090001061 Insulin Proteins 0.000 claims description 2
- 102000006992 Interferon-alpha Human genes 0.000 claims description 2
- 108010047761 Interferon-alpha Proteins 0.000 claims description 2
- 102000008070 Interferon-gamma Human genes 0.000 claims description 2
- 108010038988 Peptide Hormones Proteins 0.000 claims description 2
- 102000015731 Peptide Hormones Human genes 0.000 claims description 2
- 208000006454 hepatitis Diseases 0.000 claims description 2
- 231100000283 hepatitis Toxicity 0.000 claims description 2
- 229940125396 insulin Drugs 0.000 claims description 2
- 102100031780 Endonuclease Human genes 0.000 claims 5
- 108010067390 Viral Proteins Proteins 0.000 claims 2
- 208000007212 Foot-and-Mouth Disease Diseases 0.000 claims 1
- 241000710198 Foot-and-mouth disease virus Species 0.000 claims 1
- 108010051696 Growth Hormone Proteins 0.000 claims 1
- 108010074328 Interferon-gamma Proteins 0.000 claims 1
- 102100038803 Somatotropin Human genes 0.000 claims 1
- 239000000122 growth hormone Substances 0.000 claims 1
- 239000013612 plasmid Substances 0.000 description 64
- 108020004414 DNA Proteins 0.000 description 61
- 210000004027 cell Anatomy 0.000 description 52
- 241000588724 Escherichia coli Species 0.000 description 50
- 235000018102 proteins Nutrition 0.000 description 49
- 230000014509 gene expression Effects 0.000 description 47
- 239000000047 product Substances 0.000 description 33
- 230000014616 translation Effects 0.000 description 33
- 238000013518 transcription Methods 0.000 description 27
- 230000035897 transcription Effects 0.000 description 27
- 238000001243 protein synthesis Methods 0.000 description 23
- 230000029087 digestion Effects 0.000 description 22
- 239000002773 nucleotide Substances 0.000 description 22
- 125000003729 nucleotide group Chemical group 0.000 description 22
- 230000015572 biosynthetic process Effects 0.000 description 21
- 230000006698 induction Effects 0.000 description 21
- 101150054175 cro gene Proteins 0.000 description 20
- 238000003786 synthesis reaction Methods 0.000 description 20
- 241000702208 Shigella phage SfX Species 0.000 description 19
- 238000010276 construction Methods 0.000 description 18
- 239000000203 mixture Substances 0.000 description 16
- 229930027917 kanamycin Natural products 0.000 description 15
- 229960000318 kanamycin Drugs 0.000 description 15
- 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 15
- 229930182823 kanamycin A Natural products 0.000 description 15
- 238000010367 cloning Methods 0.000 description 14
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 12
- 239000011543 agarose gel Substances 0.000 description 12
- 230000003115 biocidal effect Effects 0.000 description 12
- 230000000694 effects Effects 0.000 description 12
- 108020004999 messenger RNA Proteins 0.000 description 12
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 10
- 230000012010 growth Effects 0.000 description 10
- 238000013519 translation Methods 0.000 description 10
- 238000004458 analytical method Methods 0.000 description 9
- 239000000499 gel Substances 0.000 description 9
- 239000002609 medium Substances 0.000 description 9
- 230000010076 replication Effects 0.000 description 9
- 229960003669 carbenicillin Drugs 0.000 description 8
- 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 8
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 7
- 241000829100 Macaca mulatta polyomavirus 1 Species 0.000 description 7
- 101710185500 Small t antigen Proteins 0.000 description 7
- 239000004098 Tetracycline Substances 0.000 description 7
- 230000002759 chromosomal effect Effects 0.000 description 7
- 229960002180 tetracycline Drugs 0.000 description 7
- 229930101283 tetracycline Natural products 0.000 description 7
- 235000019364 tetracycline Nutrition 0.000 description 7
- 150000003522 tetracyclines Chemical class 0.000 description 7
- HEDRZPFGACZZDS-UHFFFAOYSA-N Chloroform Chemical compound ClC(Cl)Cl HEDRZPFGACZZDS-UHFFFAOYSA-N 0.000 description 6
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 6
- 230000000977 initiatory effect Effects 0.000 description 6
- 239000002243 precursor Substances 0.000 description 6
- 230000008569 process Effects 0.000 description 6
- 101800001076 17 kDa core protein A12L Proteins 0.000 description 5
- 102000004533 Endonucleases Human genes 0.000 description 5
- 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 5
- 101710163270 Nuclease Proteins 0.000 description 5
- 230000001580 bacterial effect Effects 0.000 description 5
- 238000012512 characterization method Methods 0.000 description 5
- 230000006870 function Effects 0.000 description 5
- 238000003780 insertion Methods 0.000 description 5
- 230000037431 insertion Effects 0.000 description 5
- 239000003550 marker Substances 0.000 description 5
- 102000039446 nucleic acids Human genes 0.000 description 5
- 108020004707 nucleic acids Proteins 0.000 description 5
- 150000007523 nucleic acids Chemical class 0.000 description 5
- 239000011780 sodium chloride Substances 0.000 description 5
- 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 4
- 238000006243 chemical reaction Methods 0.000 description 4
- 238000012217 deletion Methods 0.000 description 4
- 230000037430 deletion Effects 0.000 description 4
- 230000001419 dependent effect Effects 0.000 description 4
- 238000001962 electrophoresis Methods 0.000 description 4
- 238000000605 extraction Methods 0.000 description 4
- 238000002372 labelling Methods 0.000 description 4
- 230000035772 mutation Effects 0.000 description 4
- 230000002035 prolonged effect Effects 0.000 description 4
- 108091008146 restriction endonucleases Proteins 0.000 description 4
- 230000000717 retained effect Effects 0.000 description 4
- FRGKKTITADJNOE-UHFFFAOYSA-N sulfanyloxyethane Chemical compound CCOS FRGKKTITADJNOE-UHFFFAOYSA-N 0.000 description 4
- 229960004799 tryptophan Drugs 0.000 description 4
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
- 102000004594 DNA Polymerase I Human genes 0.000 description 3
- 108010017826 DNA Polymerase I Proteins 0.000 description 3
- 108090000626 DNA-directed RNA polymerases Proteins 0.000 description 3
- 102000004163 DNA-directed RNA polymerases Human genes 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 3
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 3
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 3
- 229960000723 ampicillin Drugs 0.000 description 3
- 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 3
- 238000005520 cutting process Methods 0.000 description 3
- 238000001514 detection method Methods 0.000 description 3
- 238000002474 experimental method Methods 0.000 description 3
- 230000002068 genetic effect Effects 0.000 description 3
- 238000001114 immunoprecipitation Methods 0.000 description 3
- 238000011534 incubation Methods 0.000 description 3
- 239000008101 lactose Substances 0.000 description 3
- 230000001320 lysogenic effect Effects 0.000 description 3
- 229960004452 methionine Drugs 0.000 description 3
- 238000012986 modification Methods 0.000 description 3
- 230000004048 modification Effects 0.000 description 3
- 150000002972 pentoses Chemical class 0.000 description 3
- 229920002401 polyacrylamide Polymers 0.000 description 3
- 230000009467 reduction Effects 0.000 description 3
- 239000006228 supernatant Substances 0.000 description 3
- HRPVXLWXLXDGHG-UHFFFAOYSA-N Acrylamide Chemical compound NC(=O)C=C HRPVXLWXLXDGHG-UHFFFAOYSA-N 0.000 description 2
- 229920000936 Agarose Polymers 0.000 description 2
- 241000894006 Bacteria Species 0.000 description 2
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 2
- 241000282552 Chlorocebus aethiops Species 0.000 description 2
- 108091026890 Coding region Proteins 0.000 description 2
- 241000699800 Cricetinae Species 0.000 description 2
- 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 2
- 241000196324 Embryophyta Species 0.000 description 2
- 241000710202 Foot-and-mouth disease virus - type A Species 0.000 description 2
- 241000710196 Foot-and-mouth disease virus - type C Species 0.000 description 2
- 108700039691 Genetic Promoter Regions 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
- 102000002265 Human Growth Hormone Human genes 0.000 description 2
- 108010000521 Human Growth Hormone Proteins 0.000 description 2
- 239000000854 Human Growth Hormone Substances 0.000 description 2
- -1 Is Highly Basic" Proteins 0.000 description 2
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 2
- NWIBSHFKIJFRCO-WUDYKRTCSA-N Mytomycin Chemical compound C1N2C(C(C(C)=C(N)C3=O)=O)=C3[C@@H](COC(N)=O)[C@@]2(OC)[C@@H]2[C@H]1N2 NWIBSHFKIJFRCO-WUDYKRTCSA-N 0.000 description 2
- LRHPLDYGYMQRHN-UHFFFAOYSA-N N-Butanol Chemical compound CCCCO LRHPLDYGYMQRHN-UHFFFAOYSA-N 0.000 description 2
- 206010028980 Neoplasm Diseases 0.000 description 2
- 101710141454 Nucleoprotein Proteins 0.000 description 2
- 241000276498 Pollachius virens Species 0.000 description 2
- 241000589516 Pseudomonas Species 0.000 description 2
- JUJWROOIHBZHMG-UHFFFAOYSA-N Pyridine Chemical compound C1=CC=NC=C1 JUJWROOIHBZHMG-UHFFFAOYSA-N 0.000 description 2
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 2
- 241000607142 Salmonella Species 0.000 description 2
- 241000293869 Salmonella enterica subsp. enterica serovar Typhimurium Species 0.000 description 2
- 108091081024 Start codon Proteins 0.000 description 2
- 108010075344 Tryptophan synthase Proteins 0.000 description 2
- ISAKRJDGNUQOIC-UHFFFAOYSA-N Uracil Chemical compound O=C1C=CNC(=O)N1 ISAKRJDGNUQOIC-UHFFFAOYSA-N 0.000 description 2
- 239000002253 acid Substances 0.000 description 2
- 150000007513 acids Chemical class 0.000 description 2
- 238000000246 agarose gel electrophoresis Methods 0.000 description 2
- 229940041514 candida albicans extract Drugs 0.000 description 2
- 229910052799 carbon Inorganic materials 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 230000008859 change Effects 0.000 description 2
- 238000003776 cleavage reaction Methods 0.000 description 2
- 230000000295 complement effect Effects 0.000 description 2
- 238000012258 culturing Methods 0.000 description 2
- OPTASPLRGRRNAP-UHFFFAOYSA-N cytosine Chemical compound NC=1C=CNC(=O)N=1 OPTASPLRGRRNAP-UHFFFAOYSA-N 0.000 description 2
- 230000007423 decrease Effects 0.000 description 2
- 230000002950 deficient Effects 0.000 description 2
- 230000009977 dual effect Effects 0.000 description 2
- 230000008030 elimination Effects 0.000 description 2
- 238000003379 elimination reaction Methods 0.000 description 2
- 230000002255 enzymatic effect Effects 0.000 description 2
- 230000001747 exhibiting effect Effects 0.000 description 2
- 230000004927 fusion Effects 0.000 description 2
- 239000008103 glucose Substances 0.000 description 2
- UYTPUPDQBNUYGX-UHFFFAOYSA-N guanine Chemical compound O=C1NC(N)=NC2=C1N=CN2 UYTPUPDQBNUYGX-UHFFFAOYSA-N 0.000 description 2
- 230000002779 inactivation Effects 0.000 description 2
- 230000005764 inhibitory process Effects 0.000 description 2
- 210000003292 kidney cell Anatomy 0.000 description 2
- 244000005700 microbiome Species 0.000 description 2
- 235000004252 protein component Nutrition 0.000 description 2
- 230000003362 replicative effect Effects 0.000 description 2
- 230000007017 scission Effects 0.000 description 2
- 238000000926 separation method Methods 0.000 description 2
- 238000012163 sequencing technique Methods 0.000 description 2
- 210000002966 serum Anatomy 0.000 description 2
- 238000006467 substitution reaction Methods 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- RWQNBRDOKXIBIV-UHFFFAOYSA-N thymine Chemical compound CC1=CNC(=O)NC1=O RWQNBRDOKXIBIV-UHFFFAOYSA-N 0.000 description 2
- 230000009466 transformation Effects 0.000 description 2
- 230000001131 transforming effect Effects 0.000 description 2
- 230000014621 translational initiation Effects 0.000 description 2
- 239000001226 triphosphate Substances 0.000 description 2
- 239000012138 yeast extract Substances 0.000 description 2
- 101150017816 40 gene Proteins 0.000 description 1
- 229930024421 Adenine Natural products 0.000 description 1
- GFFGJBXGBJISGV-UHFFFAOYSA-N Adenine Chemical compound NC1=NC=NC2=C1N=CN2 GFFGJBXGBJISGV-UHFFFAOYSA-N 0.000 description 1
- 108010037870 Anthranilate Synthase Proteins 0.000 description 1
- NVUIWHJLPSZZQC-CYDGBPFRSA-N Arg-Ile-Arg Chemical compound NC(N)=NCCC[C@H](N)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CCCN=C(N)N)C(O)=O NVUIWHJLPSZZQC-CYDGBPFRSA-N 0.000 description 1
- 101150076489 B gene Proteins 0.000 description 1
- 241000304886 Bacilli Species 0.000 description 1
- 241000193830 Bacillus <bacterium> Species 0.000 description 1
- 244000063299 Bacillus subtilis Species 0.000 description 1
- 235000014469 Bacillus subtilis Nutrition 0.000 description 1
- 108700027842 Bacteriophage lambda DNA replication complex Proteins 0.000 description 1
- 101100283604 Caenorhabditis elegans pigk-1 gene Proteins 0.000 description 1
- 101100148606 Caenorhabditis elegans pst-1 gene Proteins 0.000 description 1
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 1
- 229930186147 Cephalosporin Natural products 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- 108010073254 Colicins Proteins 0.000 description 1
- 108020004635 Complementary DNA Proteins 0.000 description 1
- IAZDPXIOMUYVGZ-UHFFFAOYSA-N DMSO Substances CS(C)=O IAZDPXIOMUYVGZ-UHFFFAOYSA-N 0.000 description 1
- 102000016928 DNA-directed DNA polymerase Human genes 0.000 description 1
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 description 1
- 108090000204 Dipeptidase 1 Proteins 0.000 description 1
- 101100145155 Escherichia phage lambda cIII gene Proteins 0.000 description 1
- 241000701959 Escherichia virus Lambda Species 0.000 description 1
- 241000701533 Escherichia virus T4 Species 0.000 description 1
- 108060002716 Exonuclease Proteins 0.000 description 1
- 241000193385 Geobacillus stearothermophilus Species 0.000 description 1
- 101000976075 Homo sapiens Insulin Proteins 0.000 description 1
- 101000599940 Homo sapiens Interferon gamma Proteins 0.000 description 1
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
- 241000193386 Lysinibacillus sphaericus Species 0.000 description 1
- 108020004485 Nonsense Codon Proteins 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 230000010800 Physiochemical Activity Effects 0.000 description 1
- 108010021757 Polynucleotide 5'-Hydroxyl-Kinase Proteins 0.000 description 1
- 102000008422 Polynucleotide 5'-hydroxyl-kinase Human genes 0.000 description 1
- 102000009661 Repressor Proteins Human genes 0.000 description 1
- 108010034634 Repressor Proteins Proteins 0.000 description 1
- 108020004682 Single-Stranded DNA Proteins 0.000 description 1
- 102000005157 Somatostatin Human genes 0.000 description 1
- 108010056088 Somatostatin Proteins 0.000 description 1
- 101100289792 Squirrel monkey polyomavirus large T gene Proteins 0.000 description 1
- 108020005038 Terminator Codon Proteins 0.000 description 1
- 108020004566 Transfer RNA Proteins 0.000 description 1
- 108050004197 Trp repressor Proteins 0.000 description 1
- 108020000999 Viral RNA Proteins 0.000 description 1
- 238000009825 accumulation Methods 0.000 description 1
- 229960000643 adenine Drugs 0.000 description 1
- OIRDTQYFTABQOQ-KQYNXXCUSA-N adenosine group Chemical group [C@@H]1([C@H](O)[C@H](O)[C@@H](CO)O1)N1C=NC=2C(N)=NC=NC12 OIRDTQYFTABQOQ-KQYNXXCUSA-N 0.000 description 1
- 125000003275 alpha amino acid group Chemical group 0.000 description 1
- 230000004075 alteration Effects 0.000 description 1
- 125000000539 amino acid group Chemical group 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 230000000840 anti-viral effect Effects 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 230000000890 antigenic effect Effects 0.000 description 1
- 239000004599 antimicrobial Substances 0.000 description 1
- 230000011681 asexual reproduction Effects 0.000 description 1
- 238000013465 asexual reproduction Methods 0.000 description 1
- 239000012911 assay medium Substances 0.000 description 1
- 238000000376 autoradiography Methods 0.000 description 1
- 230000010455 autoregulation Effects 0.000 description 1
- 102000006635 beta-lactamase Human genes 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 230000008827 biological function Effects 0.000 description 1
- 230000033228 biological regulation Effects 0.000 description 1
- 230000005540 biological transmission Effects 0.000 description 1
- 238000010804 cDNA synthesis Methods 0.000 description 1
- 239000001110 calcium chloride Substances 0.000 description 1
- 229910001628 calcium chloride Inorganic materials 0.000 description 1
- 235000011148 calcium chloride Nutrition 0.000 description 1
- 210000000234 capsid Anatomy 0.000 description 1
- 125000002843 carboxylic acid group Chemical group 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 230000019522 cellular metabolic process Effects 0.000 description 1
- 229940124587 cephalosporin Drugs 0.000 description 1
- 150000001780 cephalosporins Chemical class 0.000 description 1
- 238000002512 chemotherapy Methods 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 210000000349 chromosome Anatomy 0.000 description 1
- 230000005757 colony formation Effects 0.000 description 1
- 239000002299 complementary DNA Substances 0.000 description 1
- 229940104302 cytosine Drugs 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 239000005549 deoxyribonucleoside Substances 0.000 description 1
- 239000012636 effector Substances 0.000 description 1
- 230000007717 exclusion Effects 0.000 description 1
- 102000013165 exonuclease Human genes 0.000 description 1
- 108010092809 exonuclease Bal 31 Proteins 0.000 description 1
- 238000007710 freezing Methods 0.000 description 1
- 230000008014 freezing Effects 0.000 description 1
- 238000007429 general method Methods 0.000 description 1
- 229930182470 glycoside Natural products 0.000 description 1
- 150000002338 glycosides Chemical class 0.000 description 1
- 230000007412 host metabolism Effects 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 230000036039 immunity Effects 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 206010022000 influenza Diseases 0.000 description 1
- 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 description 1
- 238000002955 isolation Methods 0.000 description 1
- 238000005304 joining Methods 0.000 description 1
- 101150036274 kil gene Proteins 0.000 description 1
- 230000003902 lesion Effects 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 238000013507 mapping Methods 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 230000010534 mechanism of action Effects 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 238000013508 migration Methods 0.000 description 1
- 230000005012 migration Effects 0.000 description 1
- 229960004857 mitomycin Drugs 0.000 description 1
- 238000012544 monitoring process Methods 0.000 description 1
- 231100000252 nontoxic Toxicity 0.000 description 1
- 230000003000 nontoxic effect Effects 0.000 description 1
- 239000002777 nucleoside Substances 0.000 description 1
- 150000003833 nucleoside derivatives Chemical class 0.000 description 1
- 238000012261 overproduction Methods 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 210000004777 protein coat Anatomy 0.000 description 1
- UMJSCPRVCHMLSP-UHFFFAOYSA-N pyridine Natural products COC1=CC=CN=C1 UMJSCPRVCHMLSP-UHFFFAOYSA-N 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
- 210000003705 ribosome Anatomy 0.000 description 1
- 230000035945 sensitivity Effects 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
- 241000894007 species Species 0.000 description 1
- 108010068698 spleen exonuclease Proteins 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 230000001629 suppression Effects 0.000 description 1
- 230000004083 survival effect Effects 0.000 description 1
- 230000002459 sustained effect Effects 0.000 description 1
- 229940113082 thymine Drugs 0.000 description 1
- 230000000699 topical effect Effects 0.000 description 1
- 231100000419 toxicity Toxicity 0.000 description 1
- 230000001988 toxicity Effects 0.000 description 1
- 230000005030 transcription termination Effects 0.000 description 1
- 230000002463 transducing effect Effects 0.000 description 1
- 238000012546 transfer Methods 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
- 229940035893 uracil Drugs 0.000 description 1
- 108700026220 vif Genes Proteins 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-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
-
- 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
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/52—Cytokines; Lymphokines; Interferons
- C07K14/555—Interferons [IFN]
- C07K14/565—IFN-beta
-
- 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
- C12N15/52—Genes encoding for enzymes or proenzymes
-
- 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
- C12N15/73—Expression systems using phage (lambda) regulatory sequences
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- 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
- C07K2319/40—Fusion polypeptide containing a tag for immunodetection, or an epitope for immunisation
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/70—Fusion polypeptide containing domain for protein-protein interaction
- C07K2319/74—Fusion polypeptide containing domain for protein-protein interaction containing a fusion for binding to a cell surface receptor
- C07K2319/75—Fusion polypeptide containing domain for protein-protein interaction containing a fusion for binding to a cell surface receptor containing a fusion for activation of a cell surface receptor, e.g. thrombopoeitin, NPY and other peptide hormones
-
- 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
- C12N2710/00—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA dsDNA viruses
- C12N2710/00011—Details
- C12N2710/22011—Polyomaviridae, e.g. polyoma, SV40, JC
- C12N2710/22022—New viral proteins or individual genes, new structural or functional aspects of known viral proteins or genes
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Genetics & Genomics (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Organic Chemistry (AREA)
- Biomedical Technology (AREA)
- Zoology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biotechnology (AREA)
- Molecular Biology (AREA)
- Wood Science & Technology (AREA)
- General Engineering & Computer Science (AREA)
- Biophysics (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Plant Pathology (AREA)
- Physics & Mathematics (AREA)
- Microbiology (AREA)
- Gastroenterology & Hepatology (AREA)
- Medicinal Chemistry (AREA)
- Virology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Toxicology (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Saccharide Compounds (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
Applications Claiming Priority (3)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
GB8018701 | 1980-06-06 | ||
GB8026661 | 1980-08-15 | ||
GB8028983 | 1980-09-08 |
Publications (1)
Publication Number | Publication Date |
---|---|
NO811119L true NO811119L (no) | 1981-12-07 |
Family
ID=27260930
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
NO811119A NO811119L (no) | 1980-06-06 | 1981-04-01 | Forbedrede baerere, samt fremgangsmaate ved fremstilling av disse og for aa uttrykke klonede gener |
Country Status (17)
Country | Link |
---|---|
EP (1) | EP0041767B1 (ja) |
JP (6) | JPH0787785B2 (ja) |
KR (1) | KR860001557B1 (ja) |
BG (1) | BG60443B2 (ja) |
BR (1) | BR8101972A (ja) |
CA (1) | CA1207251A (ja) |
DD (1) | DD158918A5 (ja) |
DE (1) | DE3177298T2 (ja) |
DK (1) | DK171301B1 (ja) |
ES (1) | ES8302774A1 (ja) |
FI (1) | FI811009L (ja) |
GR (1) | GR74282B (ja) |
IE (1) | IE63126B1 (ja) |
IL (1) | IL62553A (ja) |
NO (1) | NO811119L (ja) |
PH (1) | PH22618A (ja) |
YU (1) | YU87581A (ja) |
Families Citing this family (40)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US5510472A (en) * | 1979-11-21 | 1996-04-23 | Yeda Research And Development Co. Ltd. | Production of recombinant human interferon-beta2 |
IL58765A (en) * | 1979-11-21 | 1986-09-30 | Yeda Res & Dev | Process for the production of essentially pure messenger rna of human fibroblast interferon and process for the production of interferon beta |
US5554513A (en) * | 1979-11-21 | 1996-09-10 | Yeda Research & Development Co. Ltd. | Production of recombinant human interferon-beta2 |
DE3177213D1 (de) | 1980-04-03 | 1990-10-18 | Biogen Inc | Dns-sequenzen, rekombinante dns-molekuele und verfahren zur herstellung von dem menschlichen fibroblast-interferon. |
IL65475A0 (en) * | 1981-04-17 | 1982-07-30 | Meloy Lab | Production of immune interferon and its mrna |
GB2103622B (en) * | 1981-06-16 | 1986-01-15 | Genentech Inc | Production of foot and mouth disease vaccine from microbially expressed antigens |
JPS5835198A (ja) * | 1981-08-28 | 1983-03-01 | Mitsubishi Petrochem Co Ltd | 新規ベクター |
ZA831854B (en) * | 1982-03-26 | 1984-01-25 | Biogen Nv | Small peptides with the specificity of foot and mouth disease viral antigens |
WO1983003413A1 (en) * | 1982-03-31 | 1983-10-13 | Genetics Inst | Creation of dna sequences encoding modified proinsulin precursors |
FR2526661B1 (fr) * | 1982-05-13 | 1986-02-21 | Transgene Sa | Nouveaux vecteurs d'expression de la proteine antigenique de la rage et leur application a la preparation de vaccins |
US4582800A (en) * | 1982-07-12 | 1986-04-15 | Hoffmann-La Roche Inc. | Novel vectors and method for controlling interferon expression |
CA1209501A (en) * | 1982-09-16 | 1986-08-12 | Nikos Panayotatos | Expression vector |
CA1341012C (en) * | 1982-09-27 | 2000-06-06 | Biogen, Inc. | Dna sequences, recombinant dna molecules and processes for producing swine growth hormone-like polypeptides |
AU575301B2 (en) * | 1982-10-08 | 1988-07-28 | Juridical Foundation, Japanese Foundation For Cancer Research | Novel vector |
FR2539758B1 (fr) * | 1983-01-21 | 1985-11-15 | Transgene Sa | Nouveaux vecteurs d'expression et leur application a la preparation d'une proteine ayant l'activite de l'antitrypsine-a1 humaine |
DE3482840D1 (de) * | 1983-01-21 | 1990-09-06 | Transgene Sa | Expressionsvektoren und deren verwendung zur herstellung eines proteins mit menschlicher alpha-antitrypsin-aktivitaet. |
GB8308235D0 (en) * | 1983-03-25 | 1983-05-05 | Celltech Ltd | Polypeptides |
US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
DE3319242A1 (de) * | 1983-05-27 | 1984-11-29 | Battelle-Institut E.V., 6000 Frankfurt | Verfahren und plasmid zur steuerung der expression von klonierten genen |
BG49718A3 (en) * | 1983-07-15 | 1992-01-15 | Bio- Technology General Corp | Method for preparing of polypeptid with superoxiddismutasne activitty |
US5670371A (en) * | 1983-07-15 | 1997-09-23 | Bio-Technology General Corp. | Bacterial expression of superoxide dismutase |
US5162216A (en) * | 1983-09-23 | 1992-11-10 | Enzon Labs Inc. | Hybrid gene regulatory region operable in E. coli |
FR2556365B1 (fr) * | 1983-12-09 | 1987-07-31 | Transgene Sa | Vecteurs de clonage et d'expression de l'interferon-g, bacteries transformees et procede de preparation de l'interferon-g |
DE3587730T2 (de) * | 1984-02-08 | 1994-05-05 | Cetus Oncology Corp | Kontrollsysteme für rekombinant-manipulationen. |
US4711845A (en) * | 1984-08-31 | 1987-12-08 | Cetus Corporation | Portable temperature-sensitive control cassette |
US5081020A (en) * | 1984-08-27 | 1992-01-14 | Bio-Technology General Corp. | Expression vectors containing λPL promoter, T1 T2 rRNA termination sequence and origin of replication derived from a constitutive high copy number plasmid hosts and related methods |
US5059529A (en) * | 1984-08-27 | 1991-10-22 | Bio-Technology General Corp. | Stabilized expression vectors containing λPL promoter and the gene for the cI434 repressor, plasmids containing the vectors, hosts containing the plasmids and related methods |
US5162217A (en) * | 1984-08-27 | 1992-11-10 | Bio-Technology General Corp. | Plasmids for expression of human superoxide dismutase (SOD) analogs containing lambda PL promoter with engineered restriction site for substituting ribosomal binding sites and methods of use thereof |
US5143836A (en) * | 1984-08-27 | 1992-09-01 | Bio-Technology General Corp. | Plasmids for expression of human superoxide dismutase (SOD) analogs containing lambda pl promoter with engineered restriction site for substituting ribosomal binding sites and methods of use thereof |
CA1340597C (en) * | 1984-08-27 | 1999-06-22 | Haim Aviv | Expression vectors containing pl promoter, and engineered restriction site for convenient replacement of ribosomal binding site, plasmids containing the vectors, hosts containing the plasmids and related methods |
US5112744A (en) * | 1984-08-27 | 1992-05-12 | Bio-Technology General Corp. | Plasmids for the production of human Cu-Zn superoxide dismutase, bacterial hosts containing the plasmids and methods for production and recovery of such superoxide dismutase |
US5126252A (en) * | 1984-08-27 | 1992-06-30 | Bio-Technology General Corp. | Expressions vectors containing Lambda PL promoter and T1 T2 RNA termination sequence, plasmids containing the vectors, hosts containing the plasmids and relatedmethods |
US5759816A (en) * | 1984-08-27 | 1998-06-02 | Bio-Technology General Corp. | Expression vectors containing λPL promoter and T1 T2 rRNA termination sequence plasmids containing the vectors hosts containing the plasmids and related methods |
US4766066A (en) * | 1984-09-27 | 1988-08-23 | Eli Lilly And Company | Method of using bacteriophage lambda p1 promoter to produce a functional polypeptide in streptomyces |
US5510238A (en) * | 1984-10-26 | 1996-04-23 | The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services | Production of human T-cell leukemia (lymphotropic) retrovirus (HTLV-I) envelope protein fragments in bacteria and use in seroepidemiological studies |
EP0216786B1 (en) | 1984-12-21 | 1992-03-18 | Biogen, Inc. | Purification, production and use of tumor necrosis factors |
US5182196A (en) * | 1985-10-09 | 1993-01-26 | Biogen, Inc. | Expression systems for overproduction of desired proteins |
ATE123526T1 (de) * | 1987-08-17 | 1995-06-15 | Hoffmann La Roche | Hochreprimierbare expressionskontrollsequenzen. |
JP2003204783A (ja) * | 1999-07-19 | 2003-07-22 | Ajinomoto Co Inc | 発酵法による目的物質の製造法 |
US7579005B2 (en) | 2005-11-28 | 2009-08-25 | E. I. Du Pont De Nemours And Company | Process for recombinant expression and purification of antimicrobial peptides using periplasmic targeting signals as precipitable hydrophobic tags |
Family Cites Families (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
DE3177213D1 (de) * | 1980-04-03 | 1990-10-18 | Biogen Inc | Dns-sequenzen, rekombinante dns-molekuele und verfahren zur herstellung von dem menschlichen fibroblast-interferon. |
PL231111A1 (en) * | 1980-05-12 | 1983-07-18 | Biogen Nv | Dna sequences,molecules of dna recombinants and methodsof preparing of polypeptides of specifity of antigens of virus foot-and-mouth disease |
-
1981
- 1981-04-01 IE IE75781A patent/IE63126B1/en not_active IP Right Cessation
- 1981-04-01 PH PH25458A patent/PH22618A/en unknown
- 1981-04-01 KR KR1019810001102A patent/KR860001557B1/ko active
- 1981-04-01 DK DK148681A patent/DK171301B1/da not_active IP Right Cessation
- 1981-04-01 CA CA000374394A patent/CA1207251A/en not_active Expired
- 1981-04-01 EP EP81301413A patent/EP0041767B1/en not_active Revoked
- 1981-04-01 ES ES500967A patent/ES8302774A1/es not_active Expired
- 1981-04-01 JP JP56047362A patent/JPH0787785B2/ja not_active Expired - Lifetime
- 1981-04-01 NO NO811119A patent/NO811119L/no unknown
- 1981-04-01 FI FI811009A patent/FI811009L/fi not_active Application Discontinuation
- 1981-04-01 DE DE8181301413T patent/DE3177298T2/de not_active Expired - Lifetime
- 1981-04-01 GR GR64560A patent/GR74282B/el unknown
- 1981-04-01 IL IL62553A patent/IL62553A/xx active IP Right Review Request
- 1981-04-01 BR BR8101972A patent/BR8101972A/pt unknown
- 1981-04-02 DD DD81228898A patent/DD158918A5/de unknown
- 1981-04-02 YU YU00875/81A patent/YU87581A/xx unknown
-
1994
- 1994-02-11 BG BG098457A patent/BG60443B2/bg unknown
-
1995
- 1995-04-10 JP JP10784895A patent/JP3158953B2/ja not_active Expired - Lifetime
- 1995-04-10 JP JP10784795A patent/JP3158952B2/ja not_active Expired - Lifetime
- 1995-04-10 JP JP10784695A patent/JP3158951B2/ja not_active Expired - Lifetime
-
1998
- 1998-03-11 JP JP10060225A patent/JPH10304876A/ja active Pending
-
2000
- 2000-10-13 JP JP2000314383A patent/JP2001136966A/ja active Pending
Also Published As
Publication number | Publication date |
---|---|
JP3158951B2 (ja) | 2001-04-23 |
DE3177298T2 (de) | 1993-07-01 |
BR8101972A (pt) | 1982-08-17 |
BG60443B2 (bg) | 1995-03-31 |
JPH0838177A (ja) | 1996-02-13 |
IE63126B1 (en) | 1995-03-22 |
DK148681A (da) | 1981-12-07 |
JPH0838179A (ja) | 1996-02-13 |
JP3158953B2 (ja) | 2001-04-23 |
JP2001136966A (ja) | 2001-05-22 |
CA1207251A (en) | 1986-07-08 |
JPH0787785B2 (ja) | 1995-09-27 |
EP0041767A3 (en) | 1982-09-29 |
ES500967A0 (es) | 1983-01-16 |
IE810757L (en) | 1981-12-06 |
KR830005353A (ko) | 1983-08-13 |
IL62553A (en) | 1984-12-31 |
JPS5714599A (en) | 1982-01-25 |
ES8302774A1 (es) | 1983-01-16 |
JPH0838176A (ja) | 1996-02-13 |
DK171301B1 (da) | 1996-08-26 |
GR74282B (ja) | 1984-06-21 |
PH22618A (en) | 1988-10-28 |
IL62553A0 (en) | 1981-06-29 |
EP0041767B1 (en) | 1993-03-03 |
DD158918A5 (de) | 1983-02-09 |
DE3177298D1 (de) | 1993-04-08 |
JP3158952B2 (ja) | 2001-04-23 |
YU87581A (en) | 1984-04-30 |
JPH10304876A (ja) | 1998-11-17 |
EP0041767A2 (en) | 1981-12-16 |
KR860001557B1 (ko) | 1986-10-04 |
FI811009L (fi) | 1981-12-07 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
NO811119L (no) | Forbedrede baerere, samt fremgangsmaate ved fremstilling av disse og for aa uttrykke klonede gener | |
US4758512A (en) | Hosts and methods for producing recombinant products in high yields | |
EP0013828B1 (en) | Recombinant DNA, hosts transformed with it and processes for the preparation of polypeptides | |
US5401642A (en) | Vectors and methods for making such vectors and for expressing cloned genes | |
EP0041313A2 (en) | DNA sequences, recombinant DNA molecules and processes for producing human fibroblast interferon | |
JPH07170978A (ja) | レンニンの製造方法 | |
DK159976B (da) | Plasmidvektorer, fremgangsmaade til fremstilling deraf, bakterieceller transformeret med plasmidvektorer samt udtrykkelse af protein i transformerede bakterieceller | |
NO810986L (no) | Bakteriell polypeptid-ekspresjon under anvendelse av tryptofon-promoter-operator | |
US4716112A (en) | Vectors for increased expression of cloned genes | |
NO811609L (no) | Dna-sekvenser, rekombinante dna-molekyler, samt fremstilling av aktive polypeptider | |
EP0182442B1 (en) | Recombinant dna molecules and their method of production | |
JP2579619B2 (ja) | 組換えリシン毒素フラグメント | |
JP2905921B2 (ja) | 細菌中に含まれるプラスミドの安定化方法 | |
US5182196A (en) | Expression systems for overproduction of desired proteins | |
JP2515488B2 (ja) | ポリペプチドの製造方法 | |
EP0179786B1 (en) | High copy number expression vectors | |
JP2595205B2 (ja) | 発現カセット | |
US4845031A (en) | Recombinant DNA process for producing useful polypeptides | |
NO164664B (no) | Rekombinante dna-molekyler som omfatter en dna-sekvens som koder for et polypeptid av interferon alpha (ifn-alfa) type. | |
HU196236B (en) | Process for producing polypeptides showing hepatitis b virus antigenicity |