UA61066C2 - A METHOD FOR OBTAINING THE FOREIGN PROTEIN IN CELLS OF à.cÄLI, A PLASMID VECTOR AND TRANSFORMED STRAIN OF E. COLI FOR EXPRESSION OF THE FOREIGN PROTEIN - Google Patents
A METHOD FOR OBTAINING THE FOREIGN PROTEIN IN CELLS OF à.cÄLI, A PLASMID VECTOR AND TRANSFORMED STRAIN OF E. COLI FOR EXPRESSION OF THE FOREIGN PROTEIN Download PDFInfo
- Publication number
- UA61066C2 UA61066C2 UA98073658A UA98073658A UA61066C2 UA 61066 C2 UA61066 C2 UA 61066C2 UA 98073658 A UA98073658 A UA 98073658A UA 98073658 A UA98073658 A UA 98073658A UA 61066 C2 UA61066 C2 UA 61066C2
- Authority
- UA
- Ukraine
- Prior art keywords
- fact
- expression
- phase
- sequence
- vector
- Prior art date
Links
- 238000000034 method Methods 0.000 title claims abstract description 41
- 108090000623 proteins and genes Proteins 0.000 title claims description 40
- 102000004169 proteins and genes Human genes 0.000 title claims description 28
- 230000014509 gene expression Effects 0.000 title claims description 16
- 241000588724 Escherichia coli Species 0.000 title 1
- 239000013600 plasmid vector Substances 0.000 title 1
- 238000000855 fermentation Methods 0.000 claims abstract description 25
- 230000004151 fermentation Effects 0.000 claims abstract description 25
- 230000012010 growth Effects 0.000 claims abstract description 25
- 239000000758 substrate Substances 0.000 claims abstract description 14
- 230000002503 metabolic effect Effects 0.000 claims abstract description 6
- 230000009471 action Effects 0.000 claims abstract description 5
- 235000010469 Glycine max Nutrition 0.000 claims description 36
- 244000068988 Glycine max Species 0.000 claims description 28
- 239000013612 plasmid Substances 0.000 claims description 21
- 239000013598 vector Substances 0.000 claims description 17
- QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical compound CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 claims description 16
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 claims description 14
- 229910052799 carbon Inorganic materials 0.000 claims description 14
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 claims description 13
- 230000015572 biosynthetic process Effects 0.000 claims description 13
- 239000012634 fragment Substances 0.000 claims description 13
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 claims description 12
- 239000001301 oxygen Substances 0.000 claims description 12
- 229910052760 oxygen Inorganic materials 0.000 claims description 12
- 239000013604 expression vector Substances 0.000 claims description 11
- 108700007698 Genetic Terminator Regions Proteins 0.000 claims description 9
- 238000007792 addition Methods 0.000 claims description 9
- 102000008394 Immunoglobulin Fragments Human genes 0.000 claims description 8
- 108010021625 Immunoglobulin Fragments Proteins 0.000 claims description 8
- 229910019142 PO4 Inorganic materials 0.000 claims description 8
- 230000006698 induction Effects 0.000 claims description 8
- 239000010452 phosphate Substances 0.000 claims description 8
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 claims description 8
- 238000004458 analytical method Methods 0.000 claims description 7
- 238000004519 manufacturing process Methods 0.000 claims description 7
- 229910052757 nitrogen Inorganic materials 0.000 claims description 7
- 230000001105 regulatory effect Effects 0.000 claims description 7
- 230000000694 effects Effects 0.000 claims description 5
- 230000001939 inductive effect Effects 0.000 claims description 5
- 239000001963 growth medium Substances 0.000 claims description 4
- 108010076504 Protein Sorting Signals Proteins 0.000 claims description 3
- 230000010261 cell growth Effects 0.000 claims description 3
- 150000003839 salts Chemical class 0.000 claims description 3
- 238000003786 synthesis reaction Methods 0.000 claims description 3
- 239000011573 trace mineral Substances 0.000 claims description 3
- 235000013619 trace mineral Nutrition 0.000 claims description 3
- 230000009466 transformation Effects 0.000 claims description 3
- 101100350563 Streptomyces rimosus otrA gene Proteins 0.000 claims description 2
- 238000013461 design Methods 0.000 claims description 2
- 238000000605 extraction Methods 0.000 claims description 2
- 238000000746 purification Methods 0.000 claims description 2
- 230000035611 feeding Effects 0.000 claims 6
- 230000003115 biocidal effect Effects 0.000 claims 1
- 239000012526 feed medium Substances 0.000 claims 1
- 230000009469 supplementation Effects 0.000 claims 1
- 239000000047 product Substances 0.000 abstract description 11
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 abstract description 6
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 abstract description 6
- 239000006227 byproduct Substances 0.000 abstract description 5
- 230000004071 biological effect Effects 0.000 abstract description 3
- 238000002347 injection Methods 0.000 abstract description 3
- 239000007924 injection Substances 0.000 abstract description 3
- 210000004027 cell Anatomy 0.000 description 55
- 239000012071 phase Substances 0.000 description 23
- 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 20
- 239000008103 glucose Substances 0.000 description 20
- 239000002609 medium Substances 0.000 description 14
- 238000009825 accumulation Methods 0.000 description 9
- 239000000243 solution Substances 0.000 description 9
- 230000014616 translation Effects 0.000 description 7
- 238000010276 construction Methods 0.000 description 6
- 239000002028 Biomass Substances 0.000 description 5
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 5
- 230000027455 binding Effects 0.000 description 5
- 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 5
- 238000001243 protein synthesis Methods 0.000 description 5
- QGZKDVFQNNGYKY-UHFFFAOYSA-N Ammonia Chemical compound N QGZKDVFQNNGYKY-UHFFFAOYSA-N 0.000 description 4
- CURLTUGMZLYLDI-UHFFFAOYSA-N Carbon dioxide Chemical compound O=C=O CURLTUGMZLYLDI-UHFFFAOYSA-N 0.000 description 4
- XEEYBQQBJWHFJM-UHFFFAOYSA-N Iron Chemical compound [Fe] XEEYBQQBJWHFJM-UHFFFAOYSA-N 0.000 description 4
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 4
- 238000010790 dilution Methods 0.000 description 4
- 239000012895 dilution Substances 0.000 description 4
- 239000000499 gel Substances 0.000 description 4
- 108020004414 DNA Proteins 0.000 description 3
- 238000003776 cleavage reaction Methods 0.000 description 3
- 238000010367 cloning Methods 0.000 description 3
- 230000002349 favourable effect Effects 0.000 description 3
- 239000007789 gas Substances 0.000 description 3
- 239000003966 growth inhibitor Substances 0.000 description 3
- 239000000203 mixture Substances 0.000 description 3
- 235000015097 nutrients Nutrition 0.000 description 3
- 230000000737 periodic effect Effects 0.000 description 3
- 230000003234 polygenic effect Effects 0.000 description 3
- 230000008569 process Effects 0.000 description 3
- 230000007017 scission Effects 0.000 description 3
- 239000007790 solid phase Substances 0.000 description 3
- ZOXJGFHDIHLPTG-UHFFFAOYSA-N Boron Chemical compound [B] ZOXJGFHDIHLPTG-UHFFFAOYSA-N 0.000 description 2
- 235000008733 Citrus aurantifolia Nutrition 0.000 description 2
- 241001625930 Luria Species 0.000 description 2
- CSNNHWWHGAXBCP-UHFFFAOYSA-L Magnesium sulfate Chemical compound [Mg+2].[O-][S+2]([O-])([O-])[O-] CSNNHWWHGAXBCP-UHFFFAOYSA-L 0.000 description 2
- ZOKXTWBITQBERF-UHFFFAOYSA-N Molybdenum Chemical compound [Mo] ZOKXTWBITQBERF-UHFFFAOYSA-N 0.000 description 2
- 206010028980 Neoplasm Diseases 0.000 description 2
- 108091028043 Nucleic acid sequence Proteins 0.000 description 2
- 241000283973 Oryctolagus cuniculus Species 0.000 description 2
- 240000006909 Tilia x europaea Species 0.000 description 2
- 235000011941 Tilia x europaea Nutrition 0.000 description 2
- 229910021529 ammonia Inorganic materials 0.000 description 2
- XKMRRTOUMJRJIA-UHFFFAOYSA-N ammonia nh3 Chemical compound N.N XKMRRTOUMJRJIA-UHFFFAOYSA-N 0.000 description 2
- 229910052796 boron Inorganic materials 0.000 description 2
- 201000011510 cancer Diseases 0.000 description 2
- 229910002092 carbon dioxide Inorganic materials 0.000 description 2
- 239000001569 carbon dioxide Substances 0.000 description 2
- 229910002091 carbon monoxide Inorganic materials 0.000 description 2
- 239000010941 cobalt Substances 0.000 description 2
- 229910017052 cobalt Inorganic materials 0.000 description 2
- GUTLYIVDDKVIGB-UHFFFAOYSA-N cobalt atom Chemical compound [Co] GUTLYIVDDKVIGB-UHFFFAOYSA-N 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 229940088598 enzyme Drugs 0.000 description 2
- 230000004927 fusion Effects 0.000 description 2
- 235000011187 glycerol Nutrition 0.000 description 2
- 238000011081 inoculation Methods 0.000 description 2
- 229910052742 iron Inorganic materials 0.000 description 2
- 239000004571 lime Substances 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- WPBNNNQJVZRUHP-UHFFFAOYSA-L manganese(2+);methyl n-[[2-(methoxycarbonylcarbamothioylamino)phenyl]carbamothioyl]carbamate;n-[2-(sulfidocarbothioylamino)ethyl]carbamodithioate Chemical compound [Mn+2].[S-]C(=S)NCCNC([S-])=S.COC(=O)NC(=S)NC1=CC=CC=C1NC(=S)NC(=O)OC WPBNNNQJVZRUHP-UHFFFAOYSA-L 0.000 description 2
- 238000005259 measurement Methods 0.000 description 2
- 229910052750 molybdenum Inorganic materials 0.000 description 2
- 239000011733 molybdenum Substances 0.000 description 2
- 230000003287 optical effect Effects 0.000 description 2
- 238000003752 polymerase chain reaction Methods 0.000 description 2
- 238000000926 separation method Methods 0.000 description 2
- 210000002966 serum Anatomy 0.000 description 2
- 238000010561 standard procedure Methods 0.000 description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
- BPHPUYQFMNQIOC-MBOVONDJSA-N (2r,3r,4s,5r)-2-(hydroxymethyl)-6-propan-2-ylsulfanyloxane-3,4,5-triol Chemical compound CC(C)SC1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-MBOVONDJSA-N 0.000 description 1
- 108010000700 Acetolactate synthase Proteins 0.000 description 1
- 229920001817 Agar Polymers 0.000 description 1
- NLXLAEXVIDQMFP-UHFFFAOYSA-N Ammonium chloride Substances [NH4+].[Cl-] NLXLAEXVIDQMFP-UHFFFAOYSA-N 0.000 description 1
- VHUUQVKOLVNVRT-UHFFFAOYSA-N Ammonium hydroxide Chemical compound [NH4+].[OH-] VHUUQVKOLVNVRT-UHFFFAOYSA-N 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- 206010010144 Completed suicide Diseases 0.000 description 1
- RYGMFSIKBFXOCR-UHFFFAOYSA-N Copper Chemical compound [Cu] RYGMFSIKBFXOCR-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
- 108060006698 EGF receptor Proteins 0.000 description 1
- 102000001301 EGF receptor Human genes 0.000 description 1
- 238000002965 ELISA Methods 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 102000009024 Epidermal Growth Factor Human genes 0.000 description 1
- 101800003838 Epidermal growth factor Proteins 0.000 description 1
- 108010050375 Glucose 1-Dehydrogenase Proteins 0.000 description 1
- 102000003886 Glycoproteins Human genes 0.000 description 1
- 108090000288 Glycoproteins Proteins 0.000 description 1
- 108010006464 Hemolysin Proteins Proteins 0.000 description 1
- 102000007625 Hirudins Human genes 0.000 description 1
- 108010007267 Hirudins Proteins 0.000 description 1
- 101000851181 Homo sapiens Epidermal growth factor receptor Proteins 0.000 description 1
- 108060003951 Immunoglobulin Proteins 0.000 description 1
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 1
- 206010027145 Melanocytic naevus Diseases 0.000 description 1
- 241001529936 Murinae Species 0.000 description 1
- 208000007256 Nevus Diseases 0.000 description 1
- 102000003992 Peroxidases Human genes 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 1
- 108010023197 Streptokinase Proteins 0.000 description 1
- 108090000190 Thrombin Proteins 0.000 description 1
- ATJFFYVFTNAWJD-UHFFFAOYSA-N Tin Chemical compound [Sn] ATJFFYVFTNAWJD-UHFFFAOYSA-N 0.000 description 1
- 230000003213 activating effect Effects 0.000 description 1
- 230000006978 adaptation Effects 0.000 description 1
- 230000002411 adverse Effects 0.000 description 1
- 239000008272 agar Substances 0.000 description 1
- 150000001413 amino acids Chemical group 0.000 description 1
- LFVGISIMTYGQHF-UHFFFAOYSA-N ammonium dihydrogen phosphate Chemical compound [NH4+].OP(O)([O-])=O LFVGISIMTYGQHF-UHFFFAOYSA-N 0.000 description 1
- 229910000387 ammonium dihydrogen phosphate Inorganic materials 0.000 description 1
- 235000011114 ammonium hydroxide Nutrition 0.000 description 1
- 150000003863 ammonium salts Chemical class 0.000 description 1
- 230000003321 amplification Effects 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- PYMYPHUHKUWMLA-WDCZJNDASA-N arabinose Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)C=O PYMYPHUHKUWMLA-WDCZJNDASA-N 0.000 description 1
- PYMYPHUHKUWMLA-UHFFFAOYSA-N arabinose Natural products OCC(O)C(O)C(O)C=O PYMYPHUHKUWMLA-UHFFFAOYSA-N 0.000 description 1
- 101150082462 arpA gene Proteins 0.000 description 1
- 238000012365 batch cultivation Methods 0.000 description 1
- SRBFZHDQGSBBOR-UHFFFAOYSA-N beta-D-Pyranose-Lyxose Natural products OC1COC(O)C(O)C1O SRBFZHDQGSBBOR-UHFFFAOYSA-N 0.000 description 1
- 230000033228 biological regulation Effects 0.000 description 1
- 230000023555 blood coagulation Effects 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 238000004883 computer application Methods 0.000 description 1
- 238000011437 continuous method Methods 0.000 description 1
- 230000001276 controlling effect Effects 0.000 description 1
- 229910052802 copper Inorganic materials 0.000 description 1
- 239000010949 copper Substances 0.000 description 1
- 230000037029 cross reaction Effects 0.000 description 1
- 239000000287 crude extract Substances 0.000 description 1
- 230000001086 cytosolic effect Effects 0.000 description 1
- 231100000433 cytotoxic Toxicity 0.000 description 1
- 230000001472 cytotoxic effect Effects 0.000 description 1
- 230000007423 decrease Effects 0.000 description 1
- 230000007812 deficiency Effects 0.000 description 1
- 239000013530 defoamer Substances 0.000 description 1
- 230000006866 deterioration Effects 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 229910000388 diammonium phosphate Inorganic materials 0.000 description 1
- 229910003460 diamond Inorganic materials 0.000 description 1
- 239000010432 diamond Substances 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 229940116977 epidermal growth factor Drugs 0.000 description 1
- -1 ethylenediaminetetraacetic acid dihydrate Chemical class 0.000 description 1
- 238000013401 experimental design Methods 0.000 description 1
- 239000000284 extract Substances 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 238000005206 flow analysis Methods 0.000 description 1
- 238000004401 flow injection analysis Methods 0.000 description 1
- 102000037865 fusion proteins Human genes 0.000 description 1
- 108020001507 fusion proteins Proteins 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 150000002301 glucosamine derivatives Chemical class 0.000 description 1
- 125000002791 glucosyl group Chemical group C1([C@H](O)[C@@H](O)[C@H](O)[C@H](O1)CO)* 0.000 description 1
- 108010005808 hementin Proteins 0.000 description 1
- 239000003228 hemolysin Substances 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- WQPDUTSPKFMPDP-OUMQNGNKSA-N hirudin Chemical compound C([C@@H](C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC=1C=CC(OS(O)(=O)=O)=CC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(O)=O)NC(=O)[C@H](CC(O)=O)NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CCCCN)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](NC(=O)CNC(=O)[C@H](CCC(O)=O)NC(=O)CNC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H]1NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCC(O)=O)NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CO)NC(=O)CNC(=O)[C@H](CC(C)C)NC(=O)[C@H]([C@@H](C)CC)NC(=O)[C@@H]2CSSC[C@@H](C(=O)N[C@@H](CCC(O)=O)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@H](C(=O)N[C@H](C(NCC(=O)N[C@@H](CCC(N)=O)C(=O)NCC(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCCCN)C(=O)N2)=O)CSSC1)C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H]1NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)CNC(=O)[C@H](CO)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CC=2C=CC(O)=CC=2)NC(=O)[C@@H](NC(=O)[C@@H](N)C(C)C)C(C)C)[C@@H](C)O)CSSC1)C(C)C)[C@@H](C)O)[C@@H](C)O)C1=CC=CC=C1 WQPDUTSPKFMPDP-OUMQNGNKSA-N 0.000 description 1
- 229940006607 hirudin Drugs 0.000 description 1
- 230000014726 immortalization of host cell Effects 0.000 description 1
- 102000018358 immunoglobulin Human genes 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- NPFOYSMITVOQOS-UHFFFAOYSA-K iron(III) citrate Chemical compound [Fe+3].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NPFOYSMITVOQOS-UHFFFAOYSA-K 0.000 description 1
- 239000003446 ligand Substances 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 229910052943 magnesium sulfate Inorganic materials 0.000 description 1
- 235000019341 magnesium sulphate Nutrition 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 230000004060 metabolic process Effects 0.000 description 1
- 239000002207 metabolite Substances 0.000 description 1
- 230000002906 microbiologic effect Effects 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 235000019837 monoammonium phosphate Nutrition 0.000 description 1
- 210000003205 muscle Anatomy 0.000 description 1
- 238000003199 nucleic acid amplification method Methods 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 230000001717 pathogenic effect Effects 0.000 description 1
- 210000001322 periplasm Anatomy 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 238000003259 recombinant expression Methods 0.000 description 1
- 238000005215 recombination Methods 0.000 description 1
- 239000000523 sample Substances 0.000 description 1
- 238000005070 sampling Methods 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 238000004062 sedimentation Methods 0.000 description 1
- 230000001953 sensory effect Effects 0.000 description 1
- 230000009870 specific binding Effects 0.000 description 1
- 229960005202 streptokinase Drugs 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000013589 supplement Substances 0.000 description 1
- 230000000153 supplemental effect Effects 0.000 description 1
- 108010049694 theromin Proteins 0.000 description 1
- 229960004072 thrombin Drugs 0.000 description 1
- 229910052718 tin Inorganic materials 0.000 description 1
- 239000011135 tin Substances 0.000 description 1
- 238000004448 titration Methods 0.000 description 1
- 231100000331 toxic Toxicity 0.000 description 1
- 230000002588 toxic effect Effects 0.000 description 1
- 230000002103 transcriptional effect Effects 0.000 description 1
- 230000001131 transforming effect Effects 0.000 description 1
- 210000004881 tumor cell Anatomy 0.000 description 1
- VBEQCZHXXJYVRD-GACYYNSASA-N uroanthelone Chemical compound C([C@@H](C(=O)N[C@H](C(=O)N[C@@H](CS)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CS)C(=O)N[C@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)NCC(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O)C(C)C)[C@@H](C)O)NC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CCSC)NC(=O)[C@H](CS)NC(=O)[C@@H](NC(=O)CNC(=O)CNC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CS)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CS)NC(=O)CNC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC(N)=O)C(C)C)[C@@H](C)CC)C1=CC=C(O)C=C1 VBEQCZHXXJYVRD-GACYYNSASA-N 0.000 description 1
- 150000003751 zinc Chemical class 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
- C07K16/2863—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against receptors for growth factors, growth regulators
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
-
- 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
- C12N15/72—Expression systems using regulatory sequences derived from the lac-operon
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/02—Preparation of peptides or proteins having a known sequence of two or more amino acids, e.g. glutathione
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Genetics & Genomics (AREA)
- Engineering & Computer Science (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Biotechnology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Health & Medical Sciences (AREA)
- General Engineering & Computer Science (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Microbiology (AREA)
- Biomedical Technology (AREA)
- Biophysics (AREA)
- Immunology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Physics & Mathematics (AREA)
- Plant Pathology (AREA)
- Medicinal Chemistry (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP95119478 | 1995-12-11 | ||
| PCT/EP1996/005260 WO1997021829A1 (de) | 1995-12-11 | 1996-11-28 | Verfahren zur herstellung von rekombinanten proteinen in e. coli mittels hochzelldichte-fermentation |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| UA61066C2 true UA61066C2 (en) | 2003-11-17 |
Family
ID=8219878
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| UA98073658A UA61066C2 (en) | 1995-12-11 | 1996-11-28 | A METHOD FOR OBTAINING THE FOREIGN PROTEIN IN CELLS OF à.cÄLI, A PLASMID VECTOR AND TRANSFORMED STRAIN OF E. COLI FOR EXPRESSION OF THE FOREIGN PROTEIN |
Country Status (24)
| Country | Link |
|---|---|
| US (1) | US6410270B1 (da) |
| EP (1) | EP0866876B1 (da) |
| JP (2) | JP4101879B2 (da) |
| KR (1) | KR100444735B1 (da) |
| CN (1) | CN1117160C (da) |
| AR (1) | AR005035A1 (da) |
| AT (1) | ATE213271T1 (da) |
| AU (1) | AU716612B2 (da) |
| BR (1) | BR9611937A (da) |
| CA (1) | CA2240097C (da) |
| CZ (1) | CZ291415B6 (da) |
| DE (1) | DE59608743D1 (da) |
| DK (1) | DK0866876T3 (da) |
| ES (1) | ES2171752T3 (da) |
| HU (1) | HU227945B1 (da) |
| NO (1) | NO319090B1 (da) |
| PL (1) | PL185665B1 (da) |
| PT (1) | PT866876E (da) |
| RU (1) | RU2201455C2 (da) |
| SI (1) | SI0866876T1 (da) |
| SK (1) | SK283169B6 (da) |
| UA (1) | UA61066C2 (da) |
| WO (1) | WO1997021829A1 (da) |
| ZA (1) | ZA9610384B (da) |
Families Citing this family (43)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB9715895D0 (en) | 1997-07-29 | 1997-10-01 | Zeneca Ltd | Heterocyclic compounds |
| WO2000024769A2 (en) | 1998-10-28 | 2000-05-04 | Genentech, Inc. | Process for recovering heterologous polypeptide from bacterial refractile particles |
| ATE426674T1 (de) | 2000-11-03 | 2009-04-15 | Genentech Inc | Stoffwechselanderungen in garungen zur produktion rekombinanter proteine |
| PT1407052E (pt) * | 2001-07-06 | 2009-03-05 | Merck Patent Gmbh | Método para a expressão melhorada de proteínas em bactérias por monitorização e modulação da dobragem das proteínas |
| US20050181395A1 (en) * | 2003-12-12 | 2005-08-18 | Conjugon, Inc. | Systems for tightly regulated gene expression |
| DE60332667D1 (de) * | 2003-12-23 | 2010-07-01 | Council Scient Ind Res | Verfahren zur herstellung von streptokinase durch kultivierung von genetisch veränderten escherichia coli |
| NZ588430A (en) * | 2004-12-22 | 2012-10-26 | Genentech Inc | Methods for producing soluble multi-membrane-spanning proteins |
| SG174013A1 (en) * | 2006-07-27 | 2011-09-29 | Wyeth Corp | High-cell density fed-batch fermentation process for producing recombinant protein |
| TW201516149A (zh) | 2006-09-13 | 2015-05-01 | Abbvie Inc | 細胞培養改良 |
| US8911964B2 (en) | 2006-09-13 | 2014-12-16 | Abbvie Inc. | Fed-batch method of making human anti-TNF-alpha antibody |
| CN102216459A (zh) | 2008-09-15 | 2011-10-12 | 弗·哈夫曼-拉罗切有限公司 | 调节细胞摩尔渗透压浓度的组合物和方法 |
| WO2011013721A1 (ja) * | 2009-07-28 | 2011-02-03 | 三井化学株式会社 | 乳酸製造方法 |
| CA2788607C (en) * | 2010-02-01 | 2018-03-20 | Digna Biotech,S.L. | Process for the production of interferon alpha 5 |
| BR112013004396A2 (pt) * | 2010-08-30 | 2016-05-17 | Hoffmann La Roche | alimentação alcalina |
| KR101252150B1 (ko) * | 2010-11-18 | 2013-04-08 | 한국과학기술원 | 재조합 ＤＮＡ 분자 클로닝을 위한 알데히드 환원효소 ＹｑｈＤ 유전자를 포함하는 자살 벡터 |
| RU2507736C2 (ru) * | 2011-01-11 | 2014-02-27 | Федеральное государственное бюджетное учреждение науки Институт биологии гена Российской академии наук (ИБГ РАН) | Способ создания трансгенных растений с высоким уровнем экспрессии трансгенного белка |
| EP2702077A2 (en) | 2011-04-27 | 2014-03-05 | AbbVie Inc. | Methods for controlling the galactosylation profile of recombinantly-expressed proteins |
| RU2496877C2 (ru) * | 2011-12-15 | 2013-10-27 | Общество с ограниченной ответственностью "Лаборатория медицинской биотехнологии" (ООО "ЛМБТ") | ПЛАЗМИДНЫЙ ВЕКТОР pHYP С ПОВЫШЕННОЙ СЕГРЕГАЦИОННОЙ СТАБИЛЬНОСТЬЮ ДЛЯ ЭКСПРЕССИИ РЕКОМБИНАНТНОГО БЕЛКА, БАКТЕРИЯ - ПРОДУЦЕНТ ПРЕДШЕСТВЕННИКА РЕКОМБИНАНТНОГО БЕЛКА И СПОСОБ ПОЛУЧЕНИЯ РЕКОМБИНАНТНОГО БЕЛКА |
| EP2825633B1 (en) | 2012-03-12 | 2019-03-06 | Hanmi Science Co., Ltd. | Method of culturing e. coli cells for high density |
| CN102604904B (zh) * | 2012-03-14 | 2013-09-18 | 苏州汉酶生物技术有限公司 | 一种葡萄糖脱氢酶的生产方法 |
| WO2013158279A1 (en) | 2012-04-20 | 2013-10-24 | Abbvie Inc. | Protein purification methods to reduce acidic species |
| US9067990B2 (en) | 2013-03-14 | 2015-06-30 | Abbvie, Inc. | Protein purification using displacement chromatography |
| US9181572B2 (en) | 2012-04-20 | 2015-11-10 | Abbvie, Inc. | Methods to modulate lysine variant distribution |
| WO2013176754A1 (en) | 2012-05-24 | 2013-11-28 | Abbvie Inc. | Novel purification of antibodies using hydrophobic interaction chromatography |
| US9512214B2 (en) | 2012-09-02 | 2016-12-06 | Abbvie, Inc. | Methods to control protein heterogeneity |
| AU2013309506A1 (en) | 2012-09-02 | 2015-03-12 | Abbvie Inc. | Methods to control protein heterogeneity |
| WO2014137903A2 (en) | 2013-03-08 | 2014-09-12 | Genzyme Corporation | Integrated continuous manufacturing of therapeutic protein drug substances |
| AU2013381687A1 (en) | 2013-03-12 | 2015-09-24 | Abbvie Inc. | Human antibodies that bind human TNF-alpha and methods of preparing the same |
| US8921526B2 (en) | 2013-03-14 | 2014-12-30 | Abbvie, Inc. | Mutated anti-TNFα antibodies and methods of their use |
| WO2014151878A2 (en) | 2013-03-14 | 2014-09-25 | Abbvie Inc. | Methods for modulating protein glycosylation profiles of recombinant protein therapeutics using monosaccharides and oligosacharides |
| US9017687B1 (en) | 2013-10-18 | 2015-04-28 | Abbvie, Inc. | Low acidic species compositions and methods for producing and using the same using displacement chromatography |
| EP3052640A2 (en) | 2013-10-04 | 2016-08-10 | AbbVie Inc. | Use of metal ions for modulation of protein glycosylation profiles of recombinant proteins |
| US8946395B1 (en) | 2013-10-18 | 2015-02-03 | Abbvie Inc. | Purification of proteins using hydrophobic interaction chromatography |
| US9181337B2 (en) | 2013-10-18 | 2015-11-10 | Abbvie, Inc. | Modulated lysine variant species compositions and methods for producing and using the same |
| US9085618B2 (en) | 2013-10-18 | 2015-07-21 | Abbvie, Inc. | Low acidic species compositions and methods for producing and using the same |
| WO2015073884A2 (en) | 2013-11-15 | 2015-05-21 | Abbvie, Inc. | Glycoengineered binding protein compositions |
| TWI709570B (zh) | 2014-01-17 | 2020-11-11 | 美商健臻公司 | 無菌層析法及製法 |
| TWI709569B (zh) | 2014-01-17 | 2020-11-11 | 美商健臻公司 | 無菌層析樹脂及其用於製造方法的用途 |
| US9714273B2 (en) * | 2014-10-08 | 2017-07-25 | Utah State University | Expression systems and associated methods |
| MA45489A (fr) | 2015-10-22 | 2018-08-29 | Juno Therapeutics Gmbh | Procédés de culture de cellules, kits et appareil associés |
| MA49288A (fr) | 2017-04-27 | 2020-03-04 | Juno Therapeutics Gmbh | Reactifs particulaires oligomères et leurs méthodes d'utilisation |
| KR20210049155A (ko) | 2018-08-31 | 2021-05-04 | 젠자임 코포레이션 | 멸균 크로마토그래피 수지 및 제조 공정에서 이의 용도 |
| CN110684101A (zh) * | 2019-11-15 | 2020-01-14 | 上海松皓生物科技有限公司 | 一种重组水蛭素的制备方法 |
Family Cites Families (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| SK281142B6 (sk) * | 1991-03-06 | 2000-12-11 | Merck Patent Gesellschaft Mit Beschr�Nkter Haftung | Humanizovaná monoklonálna protilátka, expresné vektory a farmaceutický prostriedok |
-
1996
- 1996-11-12 AR ARP960105609A patent/AR005035A1/es unknown
- 1996-11-28 SK SK740-98A patent/SK283169B6/sk not_active IP Right Cessation
- 1996-11-28 CN CN96198949A patent/CN1117160C/zh not_active Expired - Fee Related
- 1996-11-28 KR KR10-1998-0704331A patent/KR100444735B1/ko not_active IP Right Cessation
- 1996-11-28 PL PL96327188A patent/PL185665B1/pl not_active IP Right Cessation
- 1996-11-28 AU AU10325/97A patent/AU716612B2/en not_active Ceased
- 1996-11-28 UA UA98073658A patent/UA61066C2/uk unknown
- 1996-11-28 CZ CZ19981652A patent/CZ291415B6/cs not_active IP Right Cessation
- 1996-11-28 HU HU0000317A patent/HU227945B1/hu not_active IP Right Cessation
- 1996-11-28 EP EP96941047A patent/EP0866876B1/de not_active Expired - Lifetime
- 1996-11-28 DE DE59608743T patent/DE59608743D1/de not_active Expired - Lifetime
- 1996-11-28 US US09/077,549 patent/US6410270B1/en not_active Expired - Lifetime
- 1996-11-28 PT PT96941047T patent/PT866876E/pt unknown
- 1996-11-28 JP JP52166297A patent/JP4101879B2/ja not_active Expired - Fee Related
- 1996-11-28 SI SI9630466T patent/SI0866876T1/xx unknown
- 1996-11-28 ES ES96941047T patent/ES2171752T3/es not_active Expired - Lifetime
- 1996-11-28 RU RU98113062/13A patent/RU2201455C2/ru not_active IP Right Cessation
- 1996-11-28 DK DK96941047T patent/DK0866876T3/da active
- 1996-11-28 CA CA002240097A patent/CA2240097C/en not_active Expired - Fee Related
- 1996-11-28 BR BR9611937A patent/BR9611937A/pt not_active Application Discontinuation
- 1996-11-28 WO PCT/EP1996/005260 patent/WO1997021829A1/de active IP Right Grant
- 1996-11-28 AT AT96941047T patent/ATE213271T1/de active
- 1996-12-10 ZA ZA9610384A patent/ZA9610384B/xx unknown
-
1998
- 1998-06-10 NO NO19982672A patent/NO319090B1/no not_active IP Right Cessation
-
2007
- 2007-04-18 JP JP2007109443A patent/JP4102422B2/ja not_active Expired - Fee Related
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| UA61066C2 (en) | A METHOD FOR OBTAINING THE FOREIGN PROTEIN IN CELLS OF à.cÄLI, A PLASMID VECTOR AND TRANSFORMED STRAIN OF E. COLI FOR EXPRESSION OF THE FOREIGN PROTEIN | |
| US8148494B2 (en) | Signal peptide for the production of recombinant proteins | |
| CN103975069B (zh) | 通过使用AlkB烷烃1-单加氧酶氧化烷烃的方法 | |
| JP4751374B2 (ja) | 異種タンパク質の製造方法並びにタンパク質の分泌方法 | |
| CN106047913B (zh) | 一种生产α-酮戊二酸的双酶共表达菌株的构建方法 | |
| CN105821066B (zh) | 一种生产α-酮戊二酸的双酶共表达菌株 | |
| CN102911958B (zh) | 编码重组人TNFR-Fc融合蛋白的基因及其应用 | |
| CN102392047B (zh) | 一种适用于哺乳动物细胞的双顺反子表达载体及其应用 | |
| Tran et al. | High yield fermentation of L-serine in recombinant Escherichia coli via co-localization of SerB and EamA through protein scaffold | |
| JP5768341B2 (ja) | Ｆｃ結合性タンパク質の製造方法 | |
| CN109207446A (zh) | 葡萄糖氧化酶突变体 | |
| Schroeckh et al. | Formation of recombinant proteins in Escherichia coli under control of a nitrogen regulated promoter at low and high cell densities | |
| CN110205336A (zh) | 一种Brevinin-2GUb多肽的重组表达方法及应用 | |
| CN114480409B (zh) | 一种信号肽及促进胶原蛋白在谷氨酸棒杆菌中分泌表达的方法 | |
| CN101492662A (zh) | 生产人组织纤溶酶原激活剂的方法 | |
| MXPA98004566A (en) | Procedure for preparing recombinant proteins in e. coli through fermentation with great concentration of celu | |
| CN108265061B (zh) | 一种大规模制备重组人成纤维细胞生长因子21(fgf21)的生产方法 | |
| CN106834333B (zh) | 一种能高效表达中性蛋白酶的质粒、其构建方法及其应用 | |
| CN109055464A (zh) | 一种生产重组人脑利钠肽的培养基及发酵工艺 | |
| SG181805A1 (en) | Method for optimizing a biopharmaceutical production process | |
| CN114806987A (zh) | 一种改造的大肠杆菌工程菌及其生产柠苹酸的方法 | |
| Vardanyan et al. | Development of Biotechnological Methods for Intensification of Proline Supersynthesis by Brevibacterium flavum AP-112 Producing Stain | |
| Luli | The influence of glucose metabolism on high cell density fermentation | |
| Kiss | Metabolic activity control of the L-lysine fermentation by restrained growth fed-batch strategies | |
| Wong | Bioreactor cultivation of Bacillus methanolicus expressing green fluorescent protein |