FI88309B - Ny biotest - Google Patents
Ny biotest Download PDFInfo
- Publication number
- FI88309B FI88309B FI891899A FI891899A FI88309B FI 88309 B FI88309 B FI 88309B FI 891899 A FI891899 A FI 891899A FI 891899 A FI891899 A FI 891899A FI 88309 B FI88309 B FI 88309B
- Authority
- FI
- Finland
- Prior art keywords
- cell
- plasmid
- recombinant dna
- protein
- dna
- Prior art date
Links
- 239000013612 plasmid Substances 0.000 claims description 187
- 108090000623 proteins and genes Proteins 0.000 claims description 131
- 210000004027 cell Anatomy 0.000 claims description 123
- 102000004169 proteins and genes Human genes 0.000 claims description 74
- 238000000034 method Methods 0.000 claims description 71
- 108020004511 Recombinant DNA Proteins 0.000 claims description 57
- 108020004414 DNA Proteins 0.000 claims description 55
- 241000894006 Bacteria Species 0.000 claims description 46
- 239000003242 anti bacterial agent Substances 0.000 claims description 36
- 230000000694 effects Effects 0.000 claims description 33
- 229940088710 antibiotic agent Drugs 0.000 claims description 30
- 230000001105 regulatory effect Effects 0.000 claims description 27
- 241000588724 Escherichia coli Species 0.000 claims description 25
- 230000014616 translation Effects 0.000 claims description 24
- 108060001084 Luciferase Proteins 0.000 claims description 21
- 230000010076 replication Effects 0.000 claims description 21
- 230000015572 biosynthetic process Effects 0.000 claims description 20
- 150000001875 compounds Chemical class 0.000 claims description 18
- 230000014509 gene expression Effects 0.000 claims description 17
- 210000003527 eukaryotic cell Anatomy 0.000 claims description 16
- 239000003550 marker Substances 0.000 claims description 15
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 14
- 102000004190 Enzymes Human genes 0.000 claims description 13
- 108090000790 Enzymes Proteins 0.000 claims description 13
- 229940088598 enzyme Drugs 0.000 claims description 13
- 238000005259 measurement Methods 0.000 claims description 13
- 239000005089 Luciferase Substances 0.000 claims description 12
- 210000005253 yeast cell Anatomy 0.000 claims description 12
- 238000003786 synthesis reaction Methods 0.000 claims description 11
- 210000000170 cell membrane Anatomy 0.000 claims description 10
- 238000006243 chemical reaction Methods 0.000 claims description 10
- 229960000210 nalidixic acid Drugs 0.000 claims description 10
- MHWLWQUZZRMNGJ-UHFFFAOYSA-N nalidixic acid Chemical compound C1=C(C)N=C2N(CC)C=C(C(O)=O)C(=O)C2=C1 MHWLWQUZZRMNGJ-UHFFFAOYSA-N 0.000 claims description 10
- 230000006820 DNA synthesis Effects 0.000 claims description 9
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 9
- 229910001385 heavy metal Inorganic materials 0.000 claims description 9
- 230000007246 mechanism Effects 0.000 claims description 9
- 230000004060 metabolic process Effects 0.000 claims description 9
- 238000001243 protein synthesis Methods 0.000 claims description 9
- 238000013518 transcription Methods 0.000 claims description 9
- 230000035897 transcription Effects 0.000 claims description 9
- 239000013611 chromosomal DNA Substances 0.000 claims description 8
- 230000000813 microbial effect Effects 0.000 claims description 8
- 108090000363 Bacterial Luciferases Proteins 0.000 claims description 7
- 241000700605 Viruses Species 0.000 claims description 7
- 230000006819 RNA synthesis Effects 0.000 claims description 6
- 230000000977 initiatory effect Effects 0.000 claims description 6
- 239000003471 mutagenic agent Substances 0.000 claims description 6
- 239000000523 sample Substances 0.000 claims description 6
- 238000013519 translation Methods 0.000 claims description 6
- 108010005774 beta-Galactosidase Proteins 0.000 claims description 5
- 230000001419 dependent effect Effects 0.000 claims description 5
- 239000003053 toxin Substances 0.000 claims description 5
- 231100000765 toxin Toxicity 0.000 claims description 5
- 108700012359 toxins Proteins 0.000 claims description 5
- 102000002260 Alkaline Phosphatase Human genes 0.000 claims description 4
- 108020004774 Alkaline Phosphatase Proteins 0.000 claims description 4
- 229930182555 Penicillin Natural products 0.000 claims description 4
- 210000001236 prokaryotic cell Anatomy 0.000 claims description 4
- JQXXHWHPUNPDRT-WLSIYKJHSA-N rifampicin Chemical compound O([C@](C1=O)(C)O/C=C/[C@@H]([C@H]([C@@H](OC(C)=O)[C@H](C)[C@H](O)[C@H](C)[C@@H](O)[C@@H](C)\C=C\C=C(C)/C(=O)NC=2C(O)=C3C([O-])=C4C)C)OC)C4=C1C3=C(O)C=2\C=N\N1CC[NH+](C)CC1 JQXXHWHPUNPDRT-WLSIYKJHSA-N 0.000 claims description 4
- 229960001225 rifampicin Drugs 0.000 claims description 4
- 235000014469 Bacillus subtilis Nutrition 0.000 claims description 3
- 229930186147 Cephalosporin Natural products 0.000 claims description 3
- 241000607598 Vibrio Species 0.000 claims description 3
- 229940126575 aminoglycoside Drugs 0.000 claims description 3
- 102000005936 beta-Galactosidase Human genes 0.000 claims description 3
- 229940124587 cephalosporin Drugs 0.000 claims description 3
- 239000013068 control sample Substances 0.000 claims description 3
- 239000007788 liquid Substances 0.000 claims description 3
- 235000013336 milk Nutrition 0.000 claims description 3
- 210000004080 milk Anatomy 0.000 claims description 3
- 239000008267 milk Substances 0.000 claims description 3
- 150000002960 penicillins Chemical class 0.000 claims description 3
- 102000037983 regulatory factors Human genes 0.000 claims description 3
- 108091008025 regulatory factors Proteins 0.000 claims description 3
- 102000003992 Peroxidases Human genes 0.000 claims description 2
- 230000004913 activation Effects 0.000 claims description 2
- 150000001780 cephalosporins Chemical class 0.000 claims description 2
- 230000001320 lysogenic effect Effects 0.000 claims description 2
- 230000002101 lytic effect Effects 0.000 claims description 2
- 230000002285 radioactive effect Effects 0.000 claims description 2
- 210000002966 serum Anatomy 0.000 claims description 2
- 244000063299 Bacillus subtilis Species 0.000 claims 2
- 230000005855 radiation Effects 0.000 claims 2
- 229930195730 Aflatoxin Natural products 0.000 claims 1
- 241000193830 Bacillus <bacterium> Species 0.000 claims 1
- 101000925646 Enterobacteria phage T4 Endolysin Proteins 0.000 claims 1
- 241000588921 Enterobacteriaceae Species 0.000 claims 1
- 230000002411 adverse Effects 0.000 claims 1
- 239000005409 aflatoxin Substances 0.000 claims 1
- 102000004139 alpha-Amylases Human genes 0.000 claims 1
- 108090000637 alpha-Amylases Proteins 0.000 claims 1
- 229940024171 alpha-amylase Drugs 0.000 claims 1
- 230000004075 alteration Effects 0.000 claims 1
- 230000004071 biological effect Effects 0.000 claims 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 claims 1
- 229960005542 ethidium bromide Drugs 0.000 claims 1
- 229940124307 fluoroquinolone Drugs 0.000 claims 1
- 125000002485 formyl group Chemical class [H]C(*)=O 0.000 claims 1
- 231100000707 mutagenic chemical Toxicity 0.000 claims 1
- 108040007629 peroxidase activity proteins Proteins 0.000 claims 1
- 239000007787 solid Substances 0.000 claims 1
- IEDVJHCEMCRBQM-UHFFFAOYSA-N trimethoprim Chemical compound COC1=C(OC)C(OC)=CC(CC=2C(=NC(N)=NC=2)N)=C1 IEDVJHCEMCRBQM-UHFFFAOYSA-N 0.000 claims 1
- 229960001082 trimethoprim Drugs 0.000 claims 1
- 238000012360 testing method Methods 0.000 description 63
- 238000004519 manufacturing process Methods 0.000 description 33
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 31
- 238000003556 assay Methods 0.000 description 29
- 230000001580 bacterial effect Effects 0.000 description 25
- 230000003115 biocidal effect Effects 0.000 description 22
- 239000013598 vector Substances 0.000 description 18
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 15
- 230000008859 change Effects 0.000 description 15
- 230000012010 growth Effects 0.000 description 15
- 239000000126 substance Substances 0.000 description 14
- 231100000219 mutagenic Toxicity 0.000 description 13
- 230000003505 mutagenic effect Effects 0.000 description 13
- 239000000243 solution Substances 0.000 description 13
- 108091008146 restriction endonucleases Proteins 0.000 description 12
- 230000009471 action Effects 0.000 description 11
- 241000701959 Escherichia virus Lambda Species 0.000 description 10
- 230000003321 amplification Effects 0.000 description 10
- 239000012634 fragment Substances 0.000 description 10
- 230000006870 function Effects 0.000 description 10
- 238000003199 nucleic acid amplification method Methods 0.000 description 10
- 239000000047 product Substances 0.000 description 10
- 230000006698 induction Effects 0.000 description 9
- 231100000331 toxic Toxicity 0.000 description 9
- 230000002588 toxic effect Effects 0.000 description 9
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 8
- 230000029918 bioluminescence Effects 0.000 description 7
- 238000005415 bioluminescence Methods 0.000 description 7
- 230000001738 genotoxic effect Effects 0.000 description 7
- 239000002609 medium Substances 0.000 description 7
- 239000000203 mixture Substances 0.000 description 7
- 239000003440 toxic substance Substances 0.000 description 7
- ULGZDMOVFRHVEP-RWJQBGPGSA-N Erythromycin Chemical compound O([C@@H]1[C@@H](C)C(=O)O[C@@H]([C@@]([C@H](O)[C@@H](C)C(=O)[C@H](C)C[C@@](C)(O)[C@H](O[C@H]2[C@@H]([C@H](C[C@@H](C)O2)N(C)C)O)[C@H]1C)(C)O)CC)[C@H]1C[C@@](C)(OC)[C@@H](O)[C@H](C)O1 ULGZDMOVFRHVEP-RWJQBGPGSA-N 0.000 description 6
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 6
- 102000009661 Repressor Proteins Human genes 0.000 description 6
- 230000006696 biosynthetic metabolic pathway Effects 0.000 description 6
- 230000032823 cell division Effects 0.000 description 6
- 210000002421 cell wall Anatomy 0.000 description 6
- 230000008878 coupling Effects 0.000 description 6
- 238000010168 coupling process Methods 0.000 description 6
- 238000005859 coupling reaction Methods 0.000 description 6
- KSMVZQYAVGTKIV-UHFFFAOYSA-N decanal Chemical compound CCCCCCCCCC=O KSMVZQYAVGTKIV-UHFFFAOYSA-N 0.000 description 6
- 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 6
- 230000035945 sensitivity Effects 0.000 description 6
- 238000012546 transfer Methods 0.000 description 6
- 241001515965 unidentified phage Species 0.000 description 6
- 238000010953 Ames test Methods 0.000 description 5
- 231100000039 Ames test Toxicity 0.000 description 5
- 102000053602 DNA Human genes 0.000 description 5
- 108010034634 Repressor Proteins Proteins 0.000 description 5
- 239000000427 antigen Substances 0.000 description 5
- 108091007433 antigens Proteins 0.000 description 5
- 102000036639 antigens Human genes 0.000 description 5
- 239000000499 gel Substances 0.000 description 5
- 231100000024 genotoxic Toxicity 0.000 description 5
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 5
- 108020004999 messenger RNA Proteins 0.000 description 5
- 231100000614 poison Toxicity 0.000 description 5
- -1 polycyclic hydrocarbons Chemical class 0.000 description 5
- 239000002244 precipitate 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
- 102000013563 Acid Phosphatase Human genes 0.000 description 4
- 108010051457 Acid Phosphatase Proteins 0.000 description 4
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 4
- 241000829100 Macaca mulatta polyomavirus 1 Species 0.000 description 4
- 102000004160 Phosphoric Monoester Hydrolases Human genes 0.000 description 4
- 108090000608 Phosphoric Monoester Hydrolases Proteins 0.000 description 4
- 241000607142 Salmonella Species 0.000 description 4
- 239000002253 acid Substances 0.000 description 4
- 238000004166 bioassay Methods 0.000 description 4
- 229910052799 carbon Inorganic materials 0.000 description 4
- 229960005091 chloramphenicol Drugs 0.000 description 4
- 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 4
- 239000001963 growth medium Substances 0.000 description 4
- 230000001965 increasing effect Effects 0.000 description 4
- 230000002401 inhibitory effect Effects 0.000 description 4
- 230000005764 inhibitory process Effects 0.000 description 4
- 231100000150 mutagenicity / genotoxicity testing Toxicity 0.000 description 4
- 230000035772 mutation Effects 0.000 description 4
- 102000039446 nucleic acids Human genes 0.000 description 4
- 108020004707 nucleic acids Proteins 0.000 description 4
- 150000007523 nucleic acids Chemical class 0.000 description 4
- 230000003389 potentiating effect Effects 0.000 description 4
- UCSJYZPVAKXKNQ-HZYVHMACSA-N streptomycin Chemical compound CN[C@H]1[C@H](O)[C@@H](O)[C@H](CO)O[C@H]1O[C@@H]1[C@](C=O)(O)[C@H](C)O[C@H]1O[C@@H]1[C@@H](NC(N)=N)[C@H](O)[C@@H](NC(N)=N)[C@H](O)[C@H]1O UCSJYZPVAKXKNQ-HZYVHMACSA-N 0.000 description 4
- 101100301559 Bacillus anthracis repS gene Proteins 0.000 description 3
- 206010007269 Carcinogenicity Diseases 0.000 description 3
- 101100247969 Clostridium saccharobutylicum regA gene Proteins 0.000 description 3
- 230000004543 DNA replication Effects 0.000 description 3
- 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 3
- 101100412434 Escherichia coli (strain K12) repB gene 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
- 102000014150 Interferons Human genes 0.000 description 3
- 108010050904 Interferons Proteins 0.000 description 3
- 108090000157 Metallothionein Proteins 0.000 description 3
- XDMCWZFLLGVIID-SXPRBRBTSA-N O-(3-O-D-galactosyl-N-acetyl-beta-D-galactosaminyl)-L-serine Chemical compound CC(=O)N[C@H]1[C@H](OC[C@H]([NH3+])C([O-])=O)O[C@H](CO)[C@H](O)[C@@H]1OC1[C@H](O)[C@@H](O)[C@@H](O)[C@@H](CO)O1 XDMCWZFLLGVIID-SXPRBRBTSA-N 0.000 description 3
- 241000607568 Photobacterium Species 0.000 description 3
- 241000607565 Photobacterium phosphoreum Species 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 101100114425 Streptococcus agalactiae copG gene Proteins 0.000 description 3
- YXFVVABEGXRONW-UHFFFAOYSA-N Toluene Chemical compound CC1=CC=CC=C1 YXFVVABEGXRONW-UHFFFAOYSA-N 0.000 description 3
- 238000002835 absorbance Methods 0.000 description 3
- 150000001413 amino acids Chemical class 0.000 description 3
- 231100000260 carcinogenicity Toxicity 0.000 description 3
- 230000007670 carcinogenicity Effects 0.000 description 3
- 230000001413 cellular effect Effects 0.000 description 3
- 230000006567 cellular energy metabolism Effects 0.000 description 3
- 230000019522 cellular metabolic process Effects 0.000 description 3
- 238000005119 centrifugation Methods 0.000 description 3
- 238000010367 cloning Methods 0.000 description 3
- 238000010276 construction Methods 0.000 description 3
- 229960003276 erythromycin Drugs 0.000 description 3
- 239000013604 expression vector Substances 0.000 description 3
- 235000013305 food Nutrition 0.000 description 3
- 238000001502 gel electrophoresis Methods 0.000 description 3
- 239000008103 glucose Substances 0.000 description 3
- 238000010438 heat treatment Methods 0.000 description 3
- 239000003112 inhibitor Substances 0.000 description 3
- 229940079322 interferon Drugs 0.000 description 3
- 108010079892 phosphoglycerol kinase Proteins 0.000 description 3
- 230000002829 reductive effect Effects 0.000 description 3
- 101150044854 repA gene Proteins 0.000 description 3
- 239000000758 substrate Substances 0.000 description 3
- 231100000167 toxic agent Toxicity 0.000 description 3
- 230000009466 transformation Effects 0.000 description 3
- 238000011282 treatment Methods 0.000 description 3
- GZCWLCBFPRFLKL-UHFFFAOYSA-N 1-prop-2-ynoxypropan-2-ol Chemical compound CC(O)COCC#C GZCWLCBFPRFLKL-UHFFFAOYSA-N 0.000 description 2
- KUWPCJHYPSUOFW-YBXAARCKSA-N 2-nitrophenyl beta-D-galactoside Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1OC1=CC=CC=C1[N+]([O-])=O KUWPCJHYPSUOFW-YBXAARCKSA-N 0.000 description 2
- IKHGUXGNUITLKF-UHFFFAOYSA-N Acetaldehyde Chemical compound CC=O IKHGUXGNUITLKF-UHFFFAOYSA-N 0.000 description 2
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
- 108020000946 Bacterial DNA Proteins 0.000 description 2
- 241000761389 Copa Species 0.000 description 2
- 230000004568 DNA-binding Effects 0.000 description 2
- 102000016928 DNA-directed DNA polymerase Human genes 0.000 description 2
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 description 2
- 101100125027 Dictyostelium discoideum mhsp70 gene Proteins 0.000 description 2
- 108090000204 Dipeptidase 1 Proteins 0.000 description 2
- 101150031823 HSP70 gene Proteins 0.000 description 2
- 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 2
- 102000003960 Ligases Human genes 0.000 description 2
- 108090000364 Ligases Proteins 0.000 description 2
- 102000003792 Metallothionein Human genes 0.000 description 2
- 229930193140 Neomycin Natural products 0.000 description 2
- 108091005461 Nucleic proteins Proteins 0.000 description 2
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 2
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 2
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 2
- 101100083263 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) PHO80 gene Proteins 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- 239000004098 Tetracycline Substances 0.000 description 2
- 230000003213 activating effect Effects 0.000 description 2
- 238000000246 agarose gel electrophoresis Methods 0.000 description 2
- 229960000723 ampicillin Drugs 0.000 description 2
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 2
- 238000004458 analytical method Methods 0.000 description 2
- 239000004599 antimicrobial Substances 0.000 description 2
- 210000004507 artificial chromosome Anatomy 0.000 description 2
- 230000008901 benefit Effects 0.000 description 2
- 230000027455 binding Effects 0.000 description 2
- 230000001851 biosynthetic effect Effects 0.000 description 2
- 229910052793 cadmium Inorganic materials 0.000 description 2
- BDOSMKKIYDKNTQ-UHFFFAOYSA-N cadmium atom Chemical compound [Cd] BDOSMKKIYDKNTQ-UHFFFAOYSA-N 0.000 description 2
- AIYUHDOJVYHVIT-UHFFFAOYSA-M caesium chloride Chemical compound [Cl-].[Cs+] AIYUHDOJVYHVIT-UHFFFAOYSA-M 0.000 description 2
- 230000000711 cancerogenic effect Effects 0.000 description 2
- 231100000315 carcinogenic Toxicity 0.000 description 2
- 108091092356 cellular DNA Proteins 0.000 description 2
- 235000013351 cheese Nutrition 0.000 description 2
- 238000012412 chemical coupling Methods 0.000 description 2
- 210000000349 chromosome Anatomy 0.000 description 2
- 230000001276 controlling effect Effects 0.000 description 2
- 101150023807 copB gene Proteins 0.000 description 2
- 230000009089 cytolysis Effects 0.000 description 2
- 230000003247 decreasing effect Effects 0.000 description 2
- 230000002950 deficient Effects 0.000 description 2
- 238000001514 detection method Methods 0.000 description 2
- 238000009826 distribution Methods 0.000 description 2
- 101150052825 dnaK gene Proteins 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 238000000684 flow cytometry Methods 0.000 description 2
- 230000002068 genetic effect Effects 0.000 description 2
- 231100000025 genetic toxicology Toxicity 0.000 description 2
- 238000011534 incubation Methods 0.000 description 2
- 230000001939 inductive effect Effects 0.000 description 2
- 229910052816 inorganic phosphate Inorganic materials 0.000 description 2
- 238000002955 isolation Methods 0.000 description 2
- 229960000318 kanamycin Drugs 0.000 description 2
- 229930027917 kanamycin Natural products 0.000 description 2
- 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 2
- 229930182823 kanamycin A Natural products 0.000 description 2
- 239000008101 lactose Substances 0.000 description 2
- 238000002844 melting Methods 0.000 description 2
- 230000002503 metabolic effect Effects 0.000 description 2
- 239000002207 metabolite Substances 0.000 description 2
- 230000002906 microbiologic effect Effects 0.000 description 2
- 230000011278 mitosis Effects 0.000 description 2
- 229960004927 neomycin Drugs 0.000 description 2
- 235000015097 nutrients Nutrition 0.000 description 2
- 239000008188 pellet Substances 0.000 description 2
- SCVFZCLFOSHCOH-UHFFFAOYSA-M potassium acetate Chemical compound [K+].CC([O-])=O SCVFZCLFOSHCOH-UHFFFAOYSA-M 0.000 description 2
- 238000001556 precipitation Methods 0.000 description 2
- 101150055347 repA2 gene Proteins 0.000 description 2
- 230000003362 replicative effect Effects 0.000 description 2
- 150000003839 salts Chemical class 0.000 description 2
- 229960005322 streptomycin Drugs 0.000 description 2
- 239000006228 supernatant Substances 0.000 description 2
- 235000019364 tetracycline Nutrition 0.000 description 2
- 239000001226 triphosphate Substances 0.000 description 2
- 235000011178 triphosphate Nutrition 0.000 description 2
- 230000003612 virological effect Effects 0.000 description 2
- 239000003643 water by type Substances 0.000 description 2
- DIGQNXIGRZPYDK-WKSCXVIASA-N (2R)-6-amino-2-[[2-[[(2S)-2-[[2-[[(2R)-2-[[(2S)-2-[[(2R,3S)-2-[[2-[[(2S)-2-[[2-[[(2S)-2-[[(2S)-2-[[(2R)-2-[[(2S,3S)-2-[[(2R)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-[[(2R)-2-[[2-[[2-[[2-[(2-amino-1-hydroxyethylidene)amino]-3-carboxy-1-hydroxypropylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1-hydroxyethylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1,3-dihydroxypropylidene]amino]-1-hydroxyethylidene]amino]-1-hydroxypropylidene]amino]-1,3-dihydroxypropylidene]amino]-1,3-dihydroxypropylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1,3-dihydroxybutylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1-hydroxypropylidene]amino]-1,3-dihydroxypropylidene]amino]-1-hydroxyethylidene]amino]-1,5-dihydroxy-5-iminopentylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1,3-dihydroxybutylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1,3-dihydroxypropylidene]amino]-1-hydroxyethylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1-hydroxyethylidene]amino]hexanoic acid Chemical compound C[C@@H]([C@@H](C(=N[C@@H](CS)C(=N[C@@H](C)C(=N[C@@H](CO)C(=NCC(=N[C@@H](CCC(=N)O)C(=NC(CS)C(=N[C@H]([C@H](C)O)C(=N[C@H](CS)C(=N[C@H](CO)C(=NCC(=N[C@H](CS)C(=NCC(=N[C@H](CCCCN)C(=O)O)O)O)O)O)O)O)O)O)O)O)O)O)O)N=C([C@H](CS)N=C([C@H](CO)N=C([C@H](CO)N=C([C@H](C)N=C(CN=C([C@H](CO)N=C([C@H](CS)N=C(CN=C(C(CS)N=C(C(CC(=O)O)N=C(CN)O)O)O)O)O)O)O)O)O)O)O)O DIGQNXIGRZPYDK-WKSCXVIASA-N 0.000 description 1
- MSTNYGQPCMXVAQ-RYUDHWBXSA-N (6S)-5,6,7,8-tetrahydrofolic acid Chemical compound C([C@H]1CNC=2N=C(NC(=O)C=2N1)N)NC1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 MSTNYGQPCMXVAQ-RYUDHWBXSA-N 0.000 description 1
- QRBLKGHRWFGINE-UGWAGOLRSA-N 2-[2-[2-[[2-[[4-[[2-[[6-amino-2-[3-amino-1-[(2,3-diamino-3-oxopropyl)amino]-3-oxopropyl]-5-methylpyrimidine-4-carbonyl]amino]-3-[(2r,3s,4s,5s,6s)-3-[(2s,3r,4r,5s)-4-carbamoyl-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-4,5-dihydroxy-6-(hydroxymethyl)- Chemical compound N=1C(C=2SC=C(N=2)C(N)=O)CSC=1CCNC(=O)C(C(C)=O)NC(=O)C(C)C(O)C(C)NC(=O)C(C(O[C@H]1[C@@]([C@@H](O)[C@H](O)[C@H](CO)O1)(C)O[C@H]1[C@@H]([C@](O)([C@@H](O)C(CO)O1)C(N)=O)O)C=1NC=NC=1)NC(=O)C1=NC(C(CC(N)=O)NCC(N)C(N)=O)=NC(N)=C1C QRBLKGHRWFGINE-UGWAGOLRSA-N 0.000 description 1
- QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical compound CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 description 1
- 229920001817 Agar Polymers 0.000 description 1
- 102000013142 Amylases Human genes 0.000 description 1
- 108010065511 Amylases Proteins 0.000 description 1
- 108020005544 Antisense RNA Proteins 0.000 description 1
- 108010001478 Bacitracin Proteins 0.000 description 1
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 1
- 108010035563 Chloramphenicol O-acetyltransferase Proteins 0.000 description 1
- 108020004638 Circular DNA Proteins 0.000 description 1
- 108091026890 Coding region Proteins 0.000 description 1
- 108010073254 Colicins Proteins 0.000 description 1
- 230000004544 DNA amplification Effects 0.000 description 1
- 230000007067 DNA methylation Effects 0.000 description 1
- 230000008265 DNA repair mechanism Effects 0.000 description 1
- 230000007018 DNA scission Effects 0.000 description 1
- 102000004163 DNA-directed RNA polymerases Human genes 0.000 description 1
- 108090000626 DNA-directed RNA polymerases Proteins 0.000 description 1
- 108010092160 Dactinomycin Proteins 0.000 description 1
- 241000255601 Drosophila melanogaster Species 0.000 description 1
- 241001288713 Escherichia coli MC1061 Species 0.000 description 1
- 108091092566 Extrachromosomal DNA Proteins 0.000 description 1
- 102000002464 Galactosidases Human genes 0.000 description 1
- 108010093031 Galactosidases Proteins 0.000 description 1
- 108700039691 Genetic Promoter Regions Proteins 0.000 description 1
- 239000012981 Hank's balanced salt solution Substances 0.000 description 1
- 102000002812 Heat-Shock Proteins Human genes 0.000 description 1
- 108010004889 Heat-Shock Proteins 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
- 206010020751 Hypersensitivity Diseases 0.000 description 1
- 108091029795 Intergenic region Proteins 0.000 description 1
- 108010044467 Isoenzymes Proteins 0.000 description 1
- 238000002768 Kirby-Bauer method Methods 0.000 description 1
- 108010054278 Lac Repressors Proteins 0.000 description 1
- OJMMVQQUTAEWLP-UHFFFAOYSA-N Lincomycin Natural products CN1CC(CCC)CC1C(=O)NC(C(C)O)C1C(O)C(O)C(O)C(SC)O1 OJMMVQQUTAEWLP-UHFFFAOYSA-N 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 102000016943 Muramidase Human genes 0.000 description 1
- 108010014251 Muramidase Proteins 0.000 description 1
- 240000008790 Musa x paradisiaca Species 0.000 description 1
- 235000018290 Musa x paradisiaca Nutrition 0.000 description 1
- 231100000678 Mycotoxin Toxicity 0.000 description 1
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
- 206010028980 Neoplasm Diseases 0.000 description 1
- 108090000854 Oxidoreductases Proteins 0.000 description 1
- 102000004316 Oxidoreductases Human genes 0.000 description 1
- 239000004100 Oxytetracycline Substances 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- JGSARLDLIJGVTE-MBNYWOFBSA-N Penicillin G Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)CC1=CC=CC=C1 JGSARLDLIJGVTE-MBNYWOFBSA-N 0.000 description 1
- LTQCLFMNABRKSH-UHFFFAOYSA-N Phleomycin Natural products N=1C(C=2SC=C(N=2)C(N)=O)CSC=1CCNC(=O)C(C(O)C)NC(=O)C(C)C(O)C(C)NC(=O)C(C(OC1C(C(O)C(O)C(CO)O1)OC1C(C(OC(N)=O)C(O)C(CO)O1)O)C=1NC=NC=1)NC(=O)C1=NC(C(CC(N)=O)NCC(N)C(N)=O)=NC(N)=C1C LTQCLFMNABRKSH-UHFFFAOYSA-N 0.000 description 1
- 108010035235 Phleomycins Proteins 0.000 description 1
- 108010040201 Polymyxins Proteins 0.000 description 1
- 241000220010 Rhode Species 0.000 description 1
- 108091028664 Ribonucleotide Proteins 0.000 description 1
- 229930189077 Rifamycin Natural products 0.000 description 1
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 1
- NSFFHOGKXHRQEW-UHFFFAOYSA-N Thiostrepton B Natural products N1C(=O)C(C)NC(=O)C(=C)NC(=O)C(C)NC(=O)C(C(C)CC)NC(C(C2=N3)O)C=CC2=C(C(C)O)C=C3C(=O)OC(C)C(C=2SC=C(N=2)C2N=3)NC(=O)C(N=4)=CSC=4C(C(C)(O)C(C)O)NC(=O)C(N=4)CSC=4C(=CC)NC(=O)C(C(C)O)NC(=O)C(N=4)=CSC=4C21CCC=3C1=NC(C(=O)NC(=C)C(=O)NC(=C)C(N)=O)=CS1 NSFFHOGKXHRQEW-UHFFFAOYSA-N 0.000 description 1
- 108010067973 Valinomycin Proteins 0.000 description 1
- 108010059993 Vancomycin Proteins 0.000 description 1
- 101710123661 Venom allergen 5 Proteins 0.000 description 1
- OZKXLOZHHUHGNV-UHFFFAOYSA-N Viomycin Natural products NCCCC(N)CC(=O)NC1CNC(=O)C(=CNC(=O)N)NC(=O)C(CO)NC(=O)C(CO)NC(=O)C(NC1=O)C2CC(O)NC(=N)N2 OZKXLOZHHUHGNV-UHFFFAOYSA-N 0.000 description 1
- 108010015940 Viomycin Proteins 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 108020002494 acetyltransferase Proteins 0.000 description 1
- 102000005421 acetyltransferase Human genes 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 229930183665 actinomycin Natural products 0.000 description 1
- 239000008272 agar Substances 0.000 description 1
- 208000026935 allergic disease Diseases 0.000 description 1
- 230000007815 allergy Effects 0.000 description 1
- 235000019418 amylase Nutrition 0.000 description 1
- 229940025131 amylases Drugs 0.000 description 1
- 239000012491 analyte Substances 0.000 description 1
- 210000004102 animal cell Anatomy 0.000 description 1
- 238000010171 animal model Methods 0.000 description 1
- 230000000845 anti-microbial effect Effects 0.000 description 1
- 239000002246 antineoplastic agent Substances 0.000 description 1
- 229940041181 antineoplastic drug Drugs 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 150000004982 aromatic amines Chemical class 0.000 description 1
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 1
- 101150026213 atpB gene Proteins 0.000 description 1
- 229960003071 bacitracin Drugs 0.000 description 1
- 229930184125 bacitracin Natural products 0.000 description 1
- CLKOFPXJLQSYAH-ABRJDSQDSA-N bacitracin A Chemical compound C1SC([C@@H](N)[C@@H](C)CC)=N[C@@H]1C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](CCC(O)=O)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H]1C(=O)N[C@H](CCCN)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@H](CC=2C=CC=CC=2)C(=O)N[C@@H](CC=2N=CNC=2)C(=O)N[C@H](CC(O)=O)C(=O)N[C@@H](CC(N)=O)C(=O)NCCCC1 CLKOFPXJLQSYAH-ABRJDSQDSA-N 0.000 description 1
- 210000004666 bacterial spore Anatomy 0.000 description 1
- 230000004888 barrier function Effects 0.000 description 1
- 102000006635 beta-lactamase Human genes 0.000 description 1
- 125000003460 beta-lactamyl group Chemical group 0.000 description 1
- 239000011230 binding agent Substances 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
- 238000004113 cell culture Methods 0.000 description 1
- 239000006143 cell culture medium Substances 0.000 description 1
- 230000010261 cell growth Effects 0.000 description 1
- 210000002230 centromere Anatomy 0.000 description 1
- 239000007795 chemical reaction product Substances 0.000 description 1
- 150000008280 chlorinated hydrocarbons Chemical class 0.000 description 1
- 230000024321 chromosome segregation Effects 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 230000015271 coagulation Effects 0.000 description 1
- 238000005345 coagulation Methods 0.000 description 1
- 239000003184 complementary RNA Substances 0.000 description 1
- FCFNRCROJUBPLU-UHFFFAOYSA-N compound M126 Natural products CC(C)C1NC(=O)C(C)OC(=O)C(C(C)C)NC(=O)C(C(C)C)OC(=O)C(C(C)C)NC(=O)C(C)OC(=O)C(C(C)C)NC(=O)C(C(C)C)OC(=O)C(C(C)C)NC(=O)C(C)OC(=O)C(C(C)C)NC(=O)C(C(C)C)OC1=O FCFNRCROJUBPLU-UHFFFAOYSA-N 0.000 description 1
- 235000020247 cow milk Nutrition 0.000 description 1
- 238000005520 cutting process Methods 0.000 description 1
- 230000001086 cytosolic 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
- CFCUWKMKBJTWLW-UHFFFAOYSA-N deoliosyl-3C-alpha-L-digitoxosyl-MTM Natural products CC=1C(O)=C2C(O)=C3C(=O)C(OC4OC(C)C(O)C(OC5OC(C)C(O)C(OC6OC(C)C(O)C(C)(O)C6)C5)C4)C(C(OC)C(=O)C(O)C(C)O)CC3=CC2=CC=1OC(OC(C)C1O)CC1OC1CC(O)C(O)C(C)O1 CFCUWKMKBJTWLW-UHFFFAOYSA-N 0.000 description 1
- 230000001627 detrimental effect Effects 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 238000010586 diagram Methods 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 238000004090 dissolution Methods 0.000 description 1
- 239000010840 domestic wastewater Substances 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 238000001035 drying Methods 0.000 description 1
- 101150012763 endA gene Proteins 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 238000001704 evaporation Methods 0.000 description 1
- 230000008020 evaporation Effects 0.000 description 1
- 235000013373 food additive Nutrition 0.000 description 1
- 239000002778 food additive Substances 0.000 description 1
- 231100000221 frame shift mutation induction Toxicity 0.000 description 1
- 230000037433 frameshift Effects 0.000 description 1
- 108091006104 gene-regulatory proteins Proteins 0.000 description 1
- 102000034356 gene-regulatory proteins Human genes 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 239000003862 glucocorticoid Substances 0.000 description 1
- 239000003673 groundwater Substances 0.000 description 1
- 239000003102 growth factor Substances 0.000 description 1
- 210000004349 growth plate Anatomy 0.000 description 1
- 239000005556 hormone Substances 0.000 description 1
- 229940088597 hormone Drugs 0.000 description 1
- 229930195733 hydrocarbon Natural products 0.000 description 1
- 238000010324 immunological assay Methods 0.000 description 1
- 230000001771 impaired effect Effects 0.000 description 1
- 239000000411 inducer Substances 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 238000011835 investigation Methods 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- 101150109249 lacI gene Proteins 0.000 description 1
- OJMMVQQUTAEWLP-KIDUDLJLSA-N lincomycin Chemical compound CN1C[C@H](CCC)C[C@H]1C(=O)N[C@H]([C@@H](C)O)[C@@H]1[C@H](O)[C@H](O)[C@@H](O)[C@@H](SC)O1 OJMMVQQUTAEWLP-KIDUDLJLSA-N 0.000 description 1
- 229960005287 lincomycin Drugs 0.000 description 1
- 229960000274 lysozyme Drugs 0.000 description 1
- 239000004325 lysozyme Substances 0.000 description 1
- 235000010335 lysozyme Nutrition 0.000 description 1
- 239000003120 macrolide antibiotic agent Substances 0.000 description 1
- 229940041033 macrolides Drugs 0.000 description 1
- 238000000691 measurement method Methods 0.000 description 1
- 235000013372 meat Nutrition 0.000 description 1
- 230000010534 mechanism of action Effects 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 230000021121 meiosis Effects 0.000 description 1
- 230000008018 melting Effects 0.000 description 1
- 230000037353 metabolic pathway Effects 0.000 description 1
- 229910052751 metal Inorganic materials 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- 238000009629 microbiological culture Methods 0.000 description 1
- 238000013048 microbiological method Methods 0.000 description 1
- 238000012009 microbiological test Methods 0.000 description 1
- 230000005012 migration Effects 0.000 description 1
- 238000013508 migration Methods 0.000 description 1
- CFCUWKMKBJTWLW-BKHRDMLASA-N mithramycin Chemical compound O([C@@H]1C[C@@H](O[C@H](C)[C@H]1O)OC=1C=C2C=C3C[C@H]([C@@H](C(=O)C3=C(O)C2=C(O)C=1C)O[C@@H]1O[C@H](C)[C@@H](O)[C@H](O[C@@H]2O[C@H](C)[C@H](O)[C@H](O[C@@H]3O[C@H](C)[C@@H](O)[C@@](C)(O)C3)C2)C1)[C@H](OC)C(=O)[C@@H](O)[C@@H](C)O)[C@H]1C[C@@H](O)[C@H](O)[C@@H](C)O1 CFCUWKMKBJTWLW-BKHRDMLASA-N 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 238000012544 monitoring process Methods 0.000 description 1
- 231100000299 mutagenicity Toxicity 0.000 description 1
- 230000007886 mutagenicity Effects 0.000 description 1
- 239000002636 mycotoxin Substances 0.000 description 1
- VMGAPWLDMVPYIA-HIDZBRGKSA-N n'-amino-n-iminomethanimidamide Chemical compound N\N=C\N=N VMGAPWLDMVPYIA-HIDZBRGKSA-N 0.000 description 1
- 230000007524 negative regulation of DNA replication Effects 0.000 description 1
- 229930027945 nicotinamide-adenine dinucleotide Natural products 0.000 description 1
- BOPGDPNILDQYTO-NNYOXOHSSA-N nicotinamide-adenine dinucleotide Chemical compound C1=CCC(C(=O)N)=CN1[C@H]1[C@H](O)[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OC[C@@H]2[C@H]([C@@H](O)[C@@H](O2)N2C3=NC=NC(N)=C3N=C2)O)O1 BOPGDPNILDQYTO-NNYOXOHSSA-N 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 238000001668 nucleic acid synthesis Methods 0.000 description 1
- 239000002773 nucleotide Substances 0.000 description 1
- 125000003729 nucleotide group Chemical group 0.000 description 1
- 238000012261 overproduction Methods 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 229910052760 oxygen Inorganic materials 0.000 description 1
- 239000001301 oxygen Substances 0.000 description 1
- 229960000625 oxytetracycline Drugs 0.000 description 1
- IWVCMVBTMGNXQD-PXOLEDIWSA-N oxytetracycline Chemical compound C1=CC=C2[C@](O)(C)[C@H]3[C@H](O)[C@H]4[C@H](N(C)C)C(O)=C(C(N)=O)C(=O)[C@@]4(O)C(O)=C3C(=O)C2=C1O IWVCMVBTMGNXQD-PXOLEDIWSA-N 0.000 description 1
- 235000019366 oxytetracycline Nutrition 0.000 description 1
- 229940049954 penicillin Drugs 0.000 description 1
- 108010083127 phage repressor proteins Proteins 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
- 125000002467 phosphate group Chemical group [H]OP(=O)(O[H])O[*] 0.000 description 1
- 238000005424 photoluminescence Methods 0.000 description 1
- 229960003171 plicamycin Drugs 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 229940041153 polymyxins Drugs 0.000 description 1
- 235000011056 potassium acetate Nutrition 0.000 description 1
- 230000003334 potential effect Effects 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 108090000765 processed proteins & peptides Proteins 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- RXWNCPJZOCPEPQ-NVWDDTSBSA-N puromycin Natural products C1=CC(OC)=CC=C1C[C@H](N)C(=O)N[C@H]1[C@@H](O)[C@H](N2C3=NC=NC(=C3N=C2)N(C)C)O[C@@H]1CO RXWNCPJZOCPEPQ-NVWDDTSBSA-N 0.000 description 1
- 229950010131 puromycin Drugs 0.000 description 1
- 238000003908 quality control method Methods 0.000 description 1
- 239000002994 raw material Substances 0.000 description 1
- 239000011541 reaction mixture Substances 0.000 description 1
- 239000001044 red dye Substances 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 230000009711 regulatory function Effects 0.000 description 1
- BOLDJAUMGUJJKM-LSDHHAIUSA-N renifolin D Natural products CC(=C)[C@@H]1Cc2c(O)c(O)ccc2[C@H]1CC(=O)c3ccc(O)cc3O BOLDJAUMGUJJKM-LSDHHAIUSA-N 0.000 description 1
- 230000001718 repressive effect Effects 0.000 description 1
- 239000002336 ribonucleotide Substances 0.000 description 1
- 210000004708 ribosome subunit Anatomy 0.000 description 1
- BTVYFIMKUHNOBZ-QXMMDKDBSA-N rifamycin s Chemical class O=C1C(C(O)=C2C)=C3C(=O)C=C1NC(=O)\C(C)=C/C=C\C(C)C(O)C(C)C(O)C(C)C(OC(C)=O)C(C)C(OC)\C=C/OC1(C)OC2=C3C1=O BTVYFIMKUHNOBZ-QXMMDKDBSA-N 0.000 description 1
- 229940081192 rifamycins Drugs 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 230000035939 shock Effects 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 239000002689 soil Substances 0.000 description 1
- 229960000268 spectinomycin Drugs 0.000 description 1
- UNFWWIHTNXNPBV-WXKVUWSESA-N spectinomycin Chemical compound O([C@@H]1[C@@H](NC)[C@@H](O)[C@H]([C@@H]([C@H]1O1)O)NC)[C@]2(O)[C@H]1O[C@H](C)CC2=O UNFWWIHTNXNPBV-WXKVUWSESA-N 0.000 description 1
- 210000004215 spore Anatomy 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 229940124530 sulfonamide Drugs 0.000 description 1
- 150000003456 sulfonamides Chemical class 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 208000024891 symptom Diseases 0.000 description 1
- IWVCMVBTMGNXQD-UHFFFAOYSA-N terramycin dehydrate Natural products C1=CC=C2C(O)(C)C3C(O)C4C(N(C)C)C(O)=C(C(N)=O)C(=O)C4(O)C(O)=C3C(=O)C2=C1O IWVCMVBTMGNXQD-UHFFFAOYSA-N 0.000 description 1
- 229960002180 tetracycline Drugs 0.000 description 1
- 229930101283 tetracycline Natural products 0.000 description 1
- 150000003522 tetracyclines Chemical class 0.000 description 1
- 229940040944 tetracyclines Drugs 0.000 description 1
- 239000005460 tetrahydrofolate Substances 0.000 description 1
- 125000003831 tetrazolyl group Chemical group 0.000 description 1
- 230000001225 therapeutic effect Effects 0.000 description 1
- 229940063214 thiostrepton Drugs 0.000 description 1
- 229930188070 thiostrepton Natural products 0.000 description 1
- NSFFHOGKXHRQEW-AIHSUZKVSA-N thiostrepton Chemical compound C([C@]12C=3SC=C(N=3)C(=O)N[C@H](C(=O)NC(/C=3SC[C@@H](N=3)C(=O)N[C@H](C=3SC=C(N=3)C(=O)N[C@H](C=3SC=C(N=3)[C@H]1N=1)[C@@H](C)OC(=O)C3=CC(=C4C=C[C@H]([C@@H](C4=N3)O)N[C@H](C(N[C@@H](C)C(=O)NC(=C)C(=O)N[C@@H](C)C(=O)N2)=O)[C@@H](C)CC)[C@H](C)O)[C@](C)(O)[C@@H](C)O)=C\C)[C@@H](C)O)CC=1C1=NC(C(=O)NC(=C)C(=O)NC(=C)C(N)=O)=CS1 NSFFHOGKXHRQEW-AIHSUZKVSA-N 0.000 description 1
- NSFFHOGKXHRQEW-OFMUQYBVSA-N thiostrepton A Natural products CC[C@H](C)[C@@H]1N[C@@H]2C=Cc3c(cc(nc3[C@H]2O)C(=O)O[C@H](C)[C@@H]4NC(=O)c5csc(n5)[C@@H](NC(=O)[C@H]6CSC(=N6)C(=CC)NC(=O)[C@@H](NC(=O)c7csc(n7)[C@]8(CCC(=N[C@@H]8c9csc4n9)c%10nc(cs%10)C(=O)NC(=C)C(=O)NC(=C)C(=O)N)NC(=O)[C@H](C)NC(=O)C(=C)NC(=O)[C@H](C)NC1=O)[C@@H](C)O)[C@](C)(O)[C@@H](C)O)[C@H](C)O NSFFHOGKXHRQEW-OFMUQYBVSA-N 0.000 description 1
- 231100000820 toxicity test Toxicity 0.000 description 1
- 238000012549 training Methods 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
- 239000012137 tryptone Substances 0.000 description 1
- 229960003165 vancomycin Drugs 0.000 description 1
- MYPYJXKWCTUITO-LYRMYLQWSA-N vancomycin Chemical compound O([C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@H]1OC1=C2C=C3C=C1OC1=CC=C(C=C1Cl)[C@@H](O)[C@H](C(N[C@@H](CC(N)=O)C(=O)N[C@H]3C(=O)N[C@H]1C(=O)N[C@H](C(N[C@@H](C3=CC(O)=CC(O)=C3C=3C(O)=CC=C1C=3)C(O)=O)=O)[C@H](O)C1=CC=C(C(=C1)Cl)O2)=O)NC(=O)[C@@H](CC(C)C)NC)[C@H]1C[C@](C)(N)[C@H](O)[C@H](C)O1 MYPYJXKWCTUITO-LYRMYLQWSA-N 0.000 description 1
- MYPYJXKWCTUITO-UHFFFAOYSA-N vancomycin Natural products O1C(C(=C2)Cl)=CC=C2C(O)C(C(NC(C2=CC(O)=CC(O)=C2C=2C(O)=CC=C3C=2)C(O)=O)=O)NC(=O)C3NC(=O)C2NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(CC(C)C)NC)C(O)C(C=C3Cl)=CC=C3OC3=CC2=CC1=C3OC1OC(CO)C(O)C(O)C1OC1CC(C)(N)C(O)C(C)O1 MYPYJXKWCTUITO-UHFFFAOYSA-N 0.000 description 1
- 229950001272 viomycin Drugs 0.000 description 1
- GXFAIFRPOKBQRV-GHXCTMGLSA-N viomycin Chemical compound N1C(=O)\C(=C\NC(N)=O)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)C[C@@H](N)CCCN)CNC(=O)[C@@H]1[C@@H]1NC(=N)N[C@@H](O)C1 GXFAIFRPOKBQRV-GHXCTMGLSA-N 0.000 description 1
- 230000000007 visual effect Effects 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/02—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving viable microorganisms
- C12Q1/025—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving viable microorganisms for testing or evaluating the effect of chemical or biological compounds, e.g. drugs, cosmetics
-
- 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
- C12N15/67—General methods for enhancing the expression
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/68—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving nucleic acids
- C12Q1/6897—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving nucleic acids involving reporter genes operably linked to promoters
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Genetics & Genomics (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Engineering & Computer Science (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biotechnology (AREA)
- Biochemistry (AREA)
- Physics & Mathematics (AREA)
- Molecular Biology (AREA)
- Microbiology (AREA)
- Biophysics (AREA)
- General Health & Medical Sciences (AREA)
- Biomedical Technology (AREA)
- Analytical Chemistry (AREA)
- Immunology (AREA)
- Toxicology (AREA)
- Medicinal Chemistry (AREA)
- Plant Pathology (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Claims (21)
1. Förfarande för bestämning av en faktor, som inverkar pä en encellig organism, säsom tili exempel en mikrob- eller jästcell, vilken faktor inverkar direkt eller indirekt pä 5 cellens DNA, RNA och/eller proteiner eller deras syntesme-kanismer, kännetecknat av att a) intill cellen införs en rekombinant-DNA-plasmid, vars initiationsställe eller -ställen av dupliceringsmekanism 10 ansvarig för replikationen är avhängiga av en regulerbar promotor, som kan kontrolleras antingen med en positiv eller en negativ feedback; b) cellen innehällande rekombinant-DNA-plasmiden bringas i 15 kontakt med en effektiv faktor, tili exempel genom att inku- bera dem tillsammans; c) den effektiva faktorn tkr inverka pä cellen innehdllande rekombinant-DNA-plasmiden för en lämplig tid, varefter pro- 20 motorn, som reglerar initiationsstället av dupliceringsme- kanismen ansvarig för rekombinant-DNA-plasmidens replikation aktiveras, varvid plasmidens kopital börjar öka i cellen, om den effektiva faktorn inte har inverkat pä ett hindrande sätt pä plasmidens replikation; 25 d) ändring av rekombinant-DNA-plasmidens kopital i cellen bestäms direkt eller indirekt; e) kopitalet jämförs med ett kontrollprov, väri ingen effek-30 tiv faktor var närvarande och/eller den fanns i en känd mängd i reaktionen, varvid närvaron och/eller mängden av den effektiva faktorn kan bestämmas.
2. Förfarande enligt patentkravet l, kännetecknat av att <’> rekombinant-DNA-plasmiden innehäller en DNA-sekvens, som ko- dar en eller flera selektiva proteiner eller en för biolo-gisk aktivitet väsentlig del därav av en virus, prokariot-cell eller eukariotcell och plasmiden kan innehälla en eller 4i 8 8 309 flera DNA-sekvenser, som gör cellen resistent mot anti-biotika, tungmetaller och/eller toxiner.
3. Förfarande enligt patentkravet 2, k&nnetecknat av att 5 DNA-sekvensen som kodar proteinet är avhängig av en reguler- bar promotor, som kontrolleras antingen med en positiv eller en negativ feedback och är regulerbar i använda mikrobcellen samt aktiveras samtidigt eller pä önskad tidpunkt efter ak-tiveringen av promotorn som reglerar initiationsstället av 10 replikationen.
4. Förfarande enligt patentkravet 3, k&nnetecknat av att faktoren som skall bestämmas är en faktor som inverkar pä rekombinant-DNA-plasmidens DNA biosyntes eller replikation,
5. Förfarande enligt patentkravet 4, k&nnetecknat av att cellen är Escherichia coli och dupliceringsmekanismen ansva- 25 rig för rekombinant-DNA-plasmidens replikation i bakterie kan strängt regleras med en kraftig promotor, säsom lambda λ. PL- och lac-promotorer.
6. Förfarande för bestämning av en faktor som inverkar pä 30 en cell, vilken faktor inverkar direkt eller indirekt pä cellens DNA, RNA och/eller proteiner eller deras syntesme-kanismer,'k&nnetecknat av att a) intill cellen införs en rekombinant-DNA-plasmid, som 35 finns i cellen pä flera kopior och plasmiden innehäller som markerprotein en DNA-sekvens, som kodar ett protein eller en för biologisk aktivitet väsentlig del därav av en virus, prokariotcell eller eukariotcell, vilken DNA-sekvens är av- 42 8 8 3 ϋ 9 hängiga av en regulerbar promotor och är kontrollerad antin- gen med en positiv eller en negativ feedback; b) cellen innehällande rekombinant-DNA-plasmiden bringas i 5 kontakt med en effektiv faktor, tili exempel genom att inku-bera dem tillsammans; c) den effektiva faktorn fär inverka pä cellen innehällande rekombinant-DNA-plasmiden för en lämplig tid, varefter den 10 regulerbara promotorn, som kontrollerar expression av rekom-binant-DNA-plasmidens markerprotein aktiveras, varvid mar-kerproteinets mängd börjar oka i cellen, om den effektiva faktorn inte har inverkat direkt eller indirekt pä protein-syntesen; 15 d) ändring av markerproteinet i rekombinant-DNA-plasmiden mäts; e) markerproteinets mängd jämförs med ett kontrollprov, väri 20 ingen effektiv faktor var närvarande och/eller den fanns i en känd mängd i reaktionen, varvid närvaron och/eller mäng-den av den effektiva faktorn kan bestämmas.
7. Förfarande enligt patentkrav l eller 6, kannetecknat av 25 att cellen är en gramnegativ eller grampositiv bakterie som hör tili gruppen Enterobacteriaceae, företrädesvis Escherichia coli eller tili gruppen Bacillus, företrädesvis Bacillus subtilis. 30
8. Förfarande enligt patentkraven 1-3, 6 eller 7, kanne tecknat av att promotorns reguleringsfaktorer produceras utav värdcellens kromosomala DNA, utav en andra tili en annan inkombatibilitetsklass hörande plasmid i cellen, utav densamma plasmiden, utav en lytisk eller lysogenisk fag el-35 ler virus eller reguleringsfaktorer tillsätts utifrän celler säsom tili exempel genom tillsättning av kemiska föreningar, förändring av temperaturen eller genom strälning. 43 8 8 3 C 9
9. Förfarande enligt patentkravet 8, kannetecknat av att rekombinant-DNA-plasmiden kan innehälla en eller flera DNA-sekvenser, som gör cellen resistent mot antibiotika, tungme-taller och/eller toxiner. 5
10. Förfarande enligt patentkravet 1 eller 6, kannetecknat av att provet som skall undersökas är i en flytande eller fast form eller provet innehäller radioaktiv strälning eller ultravioletsträlning. 10
11. Förfarande enligt patentkravet 1 eller 6, k&nnetecknat av att cellerna är lyofiliserade och de rehydreras före bes-tämningen med en lämplig buffert eller odlingslösning. 15
12. Förfarande enligt patentkravet 6, kännetecknat av att den effektiva faktorn är en faktor som inverkar pä rekom-binant-DNA-plasmidens DNA-biosyntes, RNA-biosyntes, transkription, translation, cellmembraner eller metabolism, säsom mutagener, antibiotika, tungmetaller eller toxiner. 20
13. Förfarande enligt patentkravet 12, k&nnetecknat av att cellen är Bacillus subtilis.
14. Förfarande enligt patentkravet 13, k&nnetecknat av att 25 markerproteinet i rekombinant-DNA-plasmiden är avhängig av en regulerbar stark promotor, säsom ol05, och markerproteinet är en alfa-amylas, alkalisk fosfatas eller luciferas.
15. Förfarande enligt patentkravet 12, k&nnetecknat av att 30 cellen är Escherichia coli.
15 RNA-biosyntes, transkription, translation, cellmembraner, metabolism eller enzyxnaktivitet, säsom tili exempel aflato-xiner, tungmetaller, etidiumbromid, nalidixinsyra, trimeto-prim, fluorokinoloner, aminoglykosider, penicilliner, kefa-losporiner, rifampicin, kloramfenikol, tetracykliner, sul-20 fonamider och den använda cellen är sensitiv mot de bestämda antibiotika.
16. Förfarande enligt patentkravet 5 eller 15, k&nnetecknat av att rekombinant-DNA-plasmiden innehäller en DNA-sek-vens, som kodar ett protein eller en för biologisk aktivi- '35 tet väsentlig del därav av en virus, prokariotcell eller eukariotcell, och proteinets expression kan kontrolleras med en regulerbar promotor, säsom tili exempel lac eller lambda 44 8 8 3 G 9
17. Förfarande enligt patentkravet 16, kännetecknat av att proteinet är luciferas, beta-galaktosidas, alkalisk fosfa-tas, peroksidas eller T4-lysozym. 5
18. Förfarande enligt patentkravet 17, kännetecknat av att rekombinant-DNA-plasmiden kodar luciferas av Vibrio harvey eller en annan bakterieluciferas.
19. Förfarande enligt patentkravet 18, kännetecknat av att 10 rekombinant-DNA-plasmiden är plasmiden pCSS112.
20. Förfarande enligt nägot av patentkraven 17-19, känne-tecknad av att aldehyd tillsätts tili reaktionen när mängden av det uttryckta luciferasenzymet i bakterien mäts. 15
21. Förfarande enligt patentkravet 4 eller 12, kännetecknat av att bestämningen görs utav mjölk, serum eller vatten.
Priority Applications (6)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
FI891899A FI88309C (sv) | 1989-04-20 | 1989-04-20 | Ny biotest |
PCT/FI1990/000112 WO1990012887A1 (en) | 1989-04-20 | 1990-04-20 | Determination of factors affecting gene regulation and/or gene replication |
DE69023642T DE69023642T2 (de) | 1989-04-20 | 1990-04-20 | Bestimmung der die genregelung und/oder genreplikation betreffenden faktoren. |
US07/768,741 US6475719B1 (en) | 1989-04-20 | 1990-04-20 | Determination of factors affecting gene regulation and/or gene replication |
EP90906232A EP0469021B1 (en) | 1989-04-20 | 1990-04-20 | Determination of factors affecting gene regulation and/or gene replication |
ES90906232T ES2081981T3 (es) | 1989-04-20 | 1990-04-20 | Determinacion de los factores que afectan la regulacion y/o replicacion de genes. |
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
FI891899A FI88309C (sv) | 1989-04-20 | 1989-04-20 | Ny biotest |
FI891899 | 1989-04-20 |
Publications (4)
Publication Number | Publication Date |
---|---|
FI891899A0 FI891899A0 (fi) | 1989-04-20 |
FI891899A FI891899A (fi) | 1990-10-21 |
FI88309B true FI88309B (fi) | 1993-01-15 |
FI88309C FI88309C (sv) | 1993-04-26 |
Family
ID=8528282
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
FI891899A FI88309C (sv) | 1989-04-20 | 1989-04-20 | Ny biotest |
Country Status (6)
Country | Link |
---|---|
US (1) | US6475719B1 (sv) |
EP (1) | EP0469021B1 (sv) |
DE (1) | DE69023642T2 (sv) |
ES (1) | ES2081981T3 (sv) |
FI (1) | FI88309C (sv) |
WO (1) | WO1990012887A1 (sv) |
Families Citing this family (12)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
ATE280219T1 (de) * | 1992-03-16 | 2004-11-15 | Jacob Nathaniel Wohlstadter | Mutagenese und selektionsmethoden in den selben wirtszellen |
FI95484C (sv) * | 1994-01-17 | 1996-02-12 | Marko Virta | Förvarande för bestämning av metall i provet |
WO1996001899A1 (en) * | 1994-07-08 | 1996-01-25 | Schering Corporation | METHOD FOR IDENTIFYING NUCLEIC ACIDS ENCODING c-fos PROMOTER ACTIVATING PROTEINS |
US5504093A (en) * | 1994-08-01 | 1996-04-02 | Otsuka Pharmaceutical Co., Ltd. | Method for inhibiting nucleoside and nucleobase transport in mammalian cells, and method for inhibition of DNA virus replication |
US5736331A (en) * | 1995-07-08 | 1998-04-07 | Schering Corporation | Method for identifying nucleic acids encoding c-fos promoter activating proteins |
US7132247B1 (en) | 1998-09-17 | 2006-11-07 | Regents Of The University Of Minnesota | Composite devices incorporating biological material and methods |
WO2000037676A1 (en) * | 1998-12-22 | 2000-06-29 | Isis Innovation Limited | Method of sequence identification |
GB9910499D0 (en) * | 1999-05-06 | 1999-07-07 | Azur Env Ltd | Assay reagent |
DE602004029868D1 (de) * | 2003-03-05 | 2010-12-16 | Chemo Sero Therapeut Res Inst | Verfahren zur herstellung eines heterologen proteins in e. coli |
EP2363025A1 (en) | 2003-03-27 | 2011-09-07 | PTC Therapeutics, Inc. | Targeting enzymes of the TRNA splicing pathway for identification of anti-fungal and/or anti-proliferative molecules |
JP4634371B2 (ja) | 2003-03-27 | 2011-02-16 | ピーティーシー セラピューティクス,インコーポレーテッド | tRNAスプライシングエンドヌクレアーゼに標的化する化合物の同定方法、および該化合物の抗増殖剤としての使用 |
WO2005014805A1 (en) | 2003-08-08 | 2005-02-17 | Regents Of The University Of Minnesota | A structured material for the production of hydrogen |
Family Cites Families (4)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
SE424090B (sv) | 1981-08-18 | 1982-06-28 | Technion Res & Dev Foundation | Forfarande for bestemning av en antibiotikakoncentration |
US4806471A (en) * | 1982-09-16 | 1989-02-21 | A/S Alfred Benzon | Plasmids with conditional uncontrolled replication behavior |
GB8308236D0 (en) | 1983-03-25 | 1983-05-05 | Celltech Ltd | Dna vectors |
DE3882394T2 (de) * | 1987-03-03 | 1993-12-16 | Light Oil Utilization Res Ass | Plasmide. |
-
1989
- 1989-04-20 FI FI891899A patent/FI88309C/sv active IP Right Grant
-
1990
- 1990-04-20 EP EP90906232A patent/EP0469021B1/en not_active Expired - Lifetime
- 1990-04-20 US US07/768,741 patent/US6475719B1/en not_active Expired - Fee Related
- 1990-04-20 DE DE69023642T patent/DE69023642T2/de not_active Expired - Fee Related
- 1990-04-20 WO PCT/FI1990/000112 patent/WO1990012887A1/en active IP Right Grant
- 1990-04-20 ES ES90906232T patent/ES2081981T3/es not_active Expired - Lifetime
Also Published As
Publication number | Publication date |
---|---|
DE69023642D1 (de) | 1995-12-21 |
EP0469021A1 (en) | 1992-02-05 |
US6475719B1 (en) | 2002-11-05 |
FI891899A0 (fi) | 1989-04-20 |
DE69023642T2 (de) | 1996-10-17 |
WO1990012887A1 (en) | 1990-11-01 |
FI891899A (fi) | 1990-10-21 |
ES2081981T3 (es) | 1996-03-16 |
FI88309C (sv) | 1993-04-26 |
EP0469021B1 (en) | 1995-11-15 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
US5683868A (en) | Highly sensitive method for detecting environmental insults | |
Engebrecht et al. | Bacterial bioluminescence: isolation and genetic analysis of functions from Vibrio fischeri | |
Davidov et al. | Improved bacterial SOS promoter∷ lux fusions for genotoxicity detection | |
Price et al. | Characterization of the Cpx regulon in Escherichia coli strain MC4100 | |
Ferrières et al. | The RcsC sensor kinase is required for normal biofilm formation in Escherichia coli K‐12 and controls the expression of a regulon in response to growth on a solid surface | |
FI88309B (fi) | Ny biotest | |
Wei et al. | Global control of GacA in secondary metabolism, primary metabolism, secretion systems, and motility in the rhizobacterium Pseudomonas aeruginosa M18 | |
EP0793729B1 (en) | Lyophilized bioluminescent bacterial reagent for the detection of toxicants | |
EP0922106B1 (en) | Light emitting biosensor | |
Nosho et al. | cAMP-CRP acts as a key regulator for the viable but non-culturable state in Escherichia coli | |
Alavi et al. | [3] Surface sensing, swarmer cell differentiation, and biofilm development | |
Rosen et al. | Microbial sensors of ultraviolet radiation based on recA’:: lux fusions | |
US5776681A (en) | Method for determining a metal present in a sample | |
JP3329395B2 (ja) | テトラサイクリンのスクリーニング法 | |
CA2267999A1 (en) | A small volume, highly sensitive method for detecting environmental insults | |
Kotova et al. | Inducible specific lux-biosensors for the detection of antibiotics: Construction and main parameters | |
CA2279576A1 (en) | A method for identifying the site of action of xenobiotic chemicals | |
Cao et al. | Regulatory mutants of the Vibrio harveyi lux system | |
US20030119094A1 (en) | Solubility reporter gene constructs | |
Peterson et al. | Characterization of conserved bases in 4.5 S RNA of Escherichia coli by construction of new F′ factors | |
Kago et al. | (p) ppGpp is required for virulence of Shigella flexneri | |
Troupp | Optimization of bioluminescent bioreporters for macrolides | |
EP1364055A2 (en) | Solubility reporter gene constructs | |
Hinde et al. | The potential of site-specific recombinases as novel reporters in whole-cell biosensors of pollution | |
江口陽子 et al. | Molecular mechanisms of multi-drug resistance induced by EvgA/EvgS, a two-component signal transduction system in Escherichia coli |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
BB | Publication of examined application | ||
PC | Transfer of assignment of patent |
Owner name: LABSYSTEMS OY |
|
FG | Patent granted |
Owner name: LABSYSTEMS OY |