ZA200107686B - Glucose dehydrogenase fusion proteins and their utilization in expression systems. - Google Patents
Glucose dehydrogenase fusion proteins and their utilization in expression systems. Download PDFInfo
- Publication number
- ZA200107686B ZA200107686B ZA200107686A ZA200107686A ZA200107686B ZA 200107686 B ZA200107686 B ZA 200107686B ZA 200107686 A ZA200107686 A ZA 200107686A ZA 200107686 A ZA200107686 A ZA 200107686A ZA 200107686 B ZA200107686 B ZA 200107686B
- Authority
- ZA
- South Africa
- Prior art keywords
- protein
- recombinant
- glcdh
- fusion protein
- polypeptide
- Prior art date
Links
- 108010050375 Glucose 1-Dehydrogenase Proteins 0.000 title claims description 129
- 108020001507 fusion proteins Proteins 0.000 title claims description 80
- 102000037865 fusion proteins Human genes 0.000 title claims description 79
- 230000014509 gene expression Effects 0.000 title claims description 59
- 108090000623 proteins and genes Proteins 0.000 claims description 138
- 102000004169 proteins and genes Human genes 0.000 claims description 112
- 238000001514 detection method Methods 0.000 claims description 47
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 claims description 36
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 claims description 36
- 238000000034 method Methods 0.000 claims description 35
- 230000000694 effects Effects 0.000 claims description 33
- 238000010186 staining Methods 0.000 claims description 29
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 27
- 229920001184 polypeptide Polymers 0.000 claims description 25
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 25
- 239000013598 vector Substances 0.000 claims description 25
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 claims description 13
- 230000004071 biological effect Effects 0.000 claims description 12
- 238000006243 chemical reaction Methods 0.000 claims description 11
- 239000013604 expression vector Substances 0.000 claims description 9
- 239000000470 constituent Substances 0.000 claims description 8
- FSVCQIDHPKZJSO-UHFFFAOYSA-L nitro blue tetrazolium dichloride Chemical compound [Cl-].[Cl-].COC1=CC(C=2C=C(OC)C(=CC=2)[N+]=2N(N=C(N=2)C=2C=CC=CC=2)C=2C=CC(=CC=2)[N+]([O-])=O)=CC=C1[N+]1=NC(C=2C=CC=CC=2)=NN1C1=CC=C([N+]([O-])=O)C=C1 FSVCQIDHPKZJSO-UHFFFAOYSA-L 0.000 claims description 8
- 238000002360 preparation method Methods 0.000 claims description 7
- 238000001502 gel electrophoresis Methods 0.000 claims description 6
- FICHIJLNRLOCNT-UHFFFAOYSA-O 1-(4-iodo-2-nitro-3-phenylphenyl)-5-phenyl-2H-tetrazol-1-ium Chemical class IC1=C(C(=C(C=C1)[N+]=1NN=NC=1C1=CC=CC=C1)[N+](=O)[O-])C1=CC=CC=C1 FICHIJLNRLOCNT-UHFFFAOYSA-O 0.000 claims description 3
- 125000003831 tetrazolyl group Chemical group 0.000 claims description 3
- 230000004850 protein–protein interaction Effects 0.000 claims description 2
- 125000003275 alpha amino acid group Chemical group 0.000 claims 1
- 235000018102 proteins Nutrition 0.000 description 90
- 210000004027 cell Anatomy 0.000 description 78
- 201000004283 Shwachman-Diamond syndrome Diseases 0.000 description 45
- 239000000499 gel Substances 0.000 description 45
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 37
- 241000588724 Escherichia coli Species 0.000 description 34
- 108010012726 tridegin Proteins 0.000 description 29
- 230000004927 fusion Effects 0.000 description 27
- 239000000284 extract Substances 0.000 description 25
- 239000003550 marker Substances 0.000 description 21
- 239000000243 solution Substances 0.000 description 21
- 239000012528 membrane Substances 0.000 description 17
- 239000000872 buffer Substances 0.000 description 16
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 14
- 239000013612 plasmid Substances 0.000 description 12
- 239000000047 product Substances 0.000 description 12
- 238000012360 testing method Methods 0.000 description 12
- 238000010367 cloning Methods 0.000 description 11
- 239000011535 reaction buffer Substances 0.000 description 11
- 230000035945 sensitivity Effects 0.000 description 11
- 239000011534 wash buffer Substances 0.000 description 11
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 10
- 239000000203 mixture Substances 0.000 description 10
- 238000001262 western blot Methods 0.000 description 10
- 102000004190 Enzymes Human genes 0.000 description 9
- 108090000790 Enzymes Proteins 0.000 description 9
- 239000007983 Tris buffer Substances 0.000 description 9
- 238000003776 cleavage reaction Methods 0.000 description 9
- 230000006870 function Effects 0.000 description 9
- 230000007017 scission Effects 0.000 description 9
- 230000009466 transformation Effects 0.000 description 9
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 9
- 230000008901 benefit Effects 0.000 description 8
- 239000002609 medium Substances 0.000 description 8
- 239000000725 suspension Substances 0.000 description 8
- 108020004414 DNA Proteins 0.000 description 7
- 108010000196 Factor XIIIa Proteins 0.000 description 7
- BAWFJGJZGIEFAR-NNYOXOHSSA-N NAD zwitterion Chemical compound NC(=O)C1=CC=C[N+]([C@H]2[C@@H]([C@H](O)[C@@H](COP([O-])(=O)OP(O)(=O)OC[C@@H]3[C@H]([C@@H](O)[C@@H](O3)N3C4=NC=NC(N)=C4N=C3)O)O2)O)=C1 BAWFJGJZGIEFAR-NNYOXOHSSA-N 0.000 description 7
- 210000003000 inclusion body Anatomy 0.000 description 7
- 229950006238 nadide Drugs 0.000 description 7
- 102000013415 peroxidase activity proteins Human genes 0.000 description 7
- 108040007629 peroxidase activity proteins Proteins 0.000 description 7
- 230000017854 proteolysis Effects 0.000 description 7
- 238000000746 purification Methods 0.000 description 7
- 239000000758 substrate Substances 0.000 description 7
- 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 6
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 6
- 239000006285 cell suspension Substances 0.000 description 6
- 238000010276 construction Methods 0.000 description 6
- 238000010790 dilution Methods 0.000 description 6
- 239000012895 dilution Substances 0.000 description 6
- 230000001900 immune effect Effects 0.000 description 6
- 238000012546 transfer Methods 0.000 description 6
- 238000005406 washing Methods 0.000 description 6
- QLAJNZSPVITUCQ-UHFFFAOYSA-N 1,3,2-dioxathietane 2,2-dioxide Chemical compound O=S1(=O)OCO1 QLAJNZSPVITUCQ-UHFFFAOYSA-N 0.000 description 5
- 108010043121 Green Fluorescent Proteins Proteins 0.000 description 5
- 102000004144 Green Fluorescent Proteins Human genes 0.000 description 5
- 102000004160 Phosphoric Monoester Hydrolases Human genes 0.000 description 5
- 108090000608 Phosphoric Monoester Hydrolases Proteins 0.000 description 5
- 230000001580 bacterial effect Effects 0.000 description 5
- 230000001086 cytosolic effect Effects 0.000 description 5
- 239000000975 dye Substances 0.000 description 5
- 239000005090 green fluorescent protein Substances 0.000 description 5
- 230000006698 induction Effects 0.000 description 5
- 229920002981 polyvinylidene fluoride Polymers 0.000 description 5
- 239000000843 powder Substances 0.000 description 5
- 235000020183 skimmed milk Nutrition 0.000 description 5
- 239000011780 sodium chloride Substances 0.000 description 5
- 229930101283 tetracycline Natural products 0.000 description 5
- 241000194107 Bacillus megaterium Species 0.000 description 4
- 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 4
- 239000002033 PVDF binder Substances 0.000 description 4
- 150000001413 amino acids Chemical group 0.000 description 4
- 238000004458 analytical method Methods 0.000 description 4
- 230000002255 enzymatic effect Effects 0.000 description 4
- 239000012634 fragment Substances 0.000 description 4
- 238000011533 pre-incubation Methods 0.000 description 4
- 238000001742 protein purification Methods 0.000 description 4
- 238000012163 sequencing technique Methods 0.000 description 4
- OFVLGDICTFRJMM-WESIUVDSSA-N tetracycline Chemical compound C1=CC=C2[C@](O)(C)[C@H]3C[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 OFVLGDICTFRJMM-WESIUVDSSA-N 0.000 description 4
- ZYECOAILUNWEAL-NUDFZHEQSA-N (4z)-4-[[2-methoxy-5-(phenylcarbamoyl)phenyl]hydrazinylidene]-n-(3-nitrophenyl)-3-oxonaphthalene-2-carboxamide Chemical compound COC1=CC=C(C(=O)NC=2C=CC=CC=2)C=C1N\N=C(C1=CC=CC=C1C=1)/C(=O)C=1C(=O)NC1=CC=CC([N+]([O-])=O)=C1 ZYECOAILUNWEAL-NUDFZHEQSA-N 0.000 description 3
- 229920001817 Agar Polymers 0.000 description 3
- 241000388002 Agonus cataphractus Species 0.000 description 3
- 238000011537 Coomassie blue staining Methods 0.000 description 3
- 241000545744 Hirudinea Species 0.000 description 3
- 238000001042 affinity chromatography Methods 0.000 description 3
- 150000001412 amines Chemical class 0.000 description 3
- -1 aminohexyl-AMP Chemical class 0.000 description 3
- 229960000723 ampicillin Drugs 0.000 description 3
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 3
- 230000008827 biological function Effects 0.000 description 3
- 230000010261 cell growth Effects 0.000 description 3
- 238000005119 centrifugation Methods 0.000 description 3
- 238000001943 fluorescence-activated cell sorting Methods 0.000 description 3
- 229960001031 glucose Drugs 0.000 description 3
- 238000011534 incubation Methods 0.000 description 3
- 239000003112 inhibitor Substances 0.000 description 3
- 230000005764 inhibitory process Effects 0.000 description 3
- 230000017730 intein-mediated protein splicing Effects 0.000 description 3
- 230000003993 interaction Effects 0.000 description 3
- 101150023497 mcrA gene Proteins 0.000 description 3
- 229910052751 metal Inorganic materials 0.000 description 3
- 239000002184 metal Substances 0.000 description 3
- 229920002704 polyhistidine Polymers 0.000 description 3
- 238000005215 recombination Methods 0.000 description 3
- 230000006798 recombination Effects 0.000 description 3
- 239000000523 sample Substances 0.000 description 3
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 2
- OSNSWKAZFASRNG-WNFIKIDCSA-N (2s,3r,4s,5s,6r)-6-(hydroxymethyl)oxane-2,3,4,5-tetrol;hydrate Chemical compound O.OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@@H]1O OSNSWKAZFASRNG-WNFIKIDCSA-N 0.000 description 2
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 2
- ZMAUOSVZWQAOML-UHFFFAOYSA-N 1-(3-iodo-2-phenylphenyl)-5-nitro-2H-tetrazol-1-ium chloride Chemical compound [Cl-].IC=1C(=C(C=CC=1)[N+]=1NN=NC=1[N+](=O)[O-])C1=CC=CC=C1 ZMAUOSVZWQAOML-UHFFFAOYSA-N 0.000 description 2
- WBVSERCLMQZOBK-UHFFFAOYSA-N 1-methylphenazine Chemical compound C1=CC=C2N=C3C(C)=CC=CC3=NC2=C1 WBVSERCLMQZOBK-UHFFFAOYSA-N 0.000 description 2
- DLZKEQQWXODGGZ-KCJUWKMLSA-N 2-[[(2r)-2-[[(2s)-2-amino-3-(4-hydroxyphenyl)propanoyl]amino]propanoyl]amino]acetic acid Chemical compound OC(=O)CNC(=O)[C@@H](C)NC(=O)[C@@H](N)CC1=CC=C(O)C=C1 DLZKEQQWXODGGZ-KCJUWKMLSA-N 0.000 description 2
- XZKIHKMTEMTJQX-UHFFFAOYSA-N 4-Nitrophenyl Phosphate Chemical compound OP(O)(=O)OC1=CC=C([N+]([O-])=O)C=C1 XZKIHKMTEMTJQX-UHFFFAOYSA-N 0.000 description 2
- BTJIUGUIPKRLHP-UHFFFAOYSA-M 4-nitrophenolate Chemical compound [O-]C1=CC=C([N+]([O-])=O)C=C1 BTJIUGUIPKRLHP-UHFFFAOYSA-M 0.000 description 2
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 2
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 2
- 229920002101 Chitin Polymers 0.000 description 2
- 108020005199 Dehydrogenases Proteins 0.000 description 2
- 241001302584 Escherichia coli str. K-12 substr. W3110 Species 0.000 description 2
- 102000005720 Glutathione transferase Human genes 0.000 description 2
- 108010070675 Glutathione transferase Proteins 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- 241000237654 Haementeria ghilianii Species 0.000 description 2
- 241000238631 Hexapoda Species 0.000 description 2
- 101710175625 Maltose/maltodextrin-binding periplasmic protein Proteins 0.000 description 2
- KWYHDKDOAIKMQN-UHFFFAOYSA-N N,N,N',N'-tetramethylethylenediamine Chemical compound CN(C)CCN(C)C KWYHDKDOAIKMQN-UHFFFAOYSA-N 0.000 description 2
- 108010038807 Oligopeptides Proteins 0.000 description 2
- 102000015636 Oligopeptides Human genes 0.000 description 2
- 102000035195 Peptidases Human genes 0.000 description 2
- 108091005804 Peptidases Proteins 0.000 description 2
- 239000004365 Protease Substances 0.000 description 2
- 229940124158 Protease/peptidase inhibitor Drugs 0.000 description 2
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 2
- 108010090804 Streptavidin Proteins 0.000 description 2
- 229920004890 Triton X-100 Polymers 0.000 description 2
- 239000013504 Triton X-100 Substances 0.000 description 2
- ISAKRJDGNUQOIC-UHFFFAOYSA-N Uracil Chemical compound O=C1C=CNC(=O)N1 ISAKRJDGNUQOIC-UHFFFAOYSA-N 0.000 description 2
- 238000010521 absorption reaction Methods 0.000 description 2
- OIRDTQYFTABQOQ-KQYNXXCUSA-N adenosine Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@@H]1O[C@H](CO)[C@@H](O)[C@H]1O OIRDTQYFTABQOQ-KQYNXXCUSA-N 0.000 description 2
- 239000008272 agar Substances 0.000 description 2
- 230000002776 aggregation Effects 0.000 description 2
- 238000004220 aggregation Methods 0.000 description 2
- 229910001870 ammonium persulfate Inorganic materials 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- 230000000903 blocking effect Effects 0.000 description 2
- 108010051489 calin Proteins 0.000 description 2
- 239000005018 casein Substances 0.000 description 2
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 2
- 235000021240 caseins Nutrition 0.000 description 2
- 238000012512 characterization method Methods 0.000 description 2
- 239000005515 coenzyme Substances 0.000 description 2
- 239000007857 degradation product Substances 0.000 description 2
- 238000011161 development Methods 0.000 description 2
- 230000018109 developmental process Effects 0.000 description 2
- 238000006911 enzymatic reaction Methods 0.000 description 2
- ZMMJGEGLRURXTF-UHFFFAOYSA-N ethidium bromide Chemical compound [Br-].C12=CC(N)=CC=C2C2=CC=C(N)C=C2[N+](CC)=C1C1=CC=CC=C1 ZMMJGEGLRURXTF-UHFFFAOYSA-N 0.000 description 2
- 210000003527 eukaryotic cell Anatomy 0.000 description 2
- 238000005755 formation reaction Methods 0.000 description 2
- 101150045500 galK gene Proteins 0.000 description 2
- 101150041954 galU gene Proteins 0.000 description 2
- 210000004907 gland Anatomy 0.000 description 2
- 239000008103 glucose Substances 0.000 description 2
- 230000012010 growth Effects 0.000 description 2
- 101150096208 gtaB gene Proteins 0.000 description 2
- UYTPUPDQBNUYGX-UHFFFAOYSA-N guanine Chemical compound O=C1NC(N)=NC2=C1N=CN2 UYTPUPDQBNUYGX-UHFFFAOYSA-N 0.000 description 2
- 125000000487 histidyl group Chemical group [H]N([H])C(C(=O)O*)C([H])([H])C1=C([H])N([H])C([H])=N1 0.000 description 2
- 238000010348 incorporation Methods 0.000 description 2
- 238000002955 isolation Methods 0.000 description 2
- 101150109249 lacI gene Proteins 0.000 description 2
- 239000012160 loading buffer Substances 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 244000005700 microbiome Species 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 239000013642 negative control Substances 0.000 description 2
- 239000002773 nucleotide Substances 0.000 description 2
- 125000003729 nucleotide group Chemical group 0.000 description 2
- 101150012154 nupG gene Proteins 0.000 description 2
- 238000005457 optimization Methods 0.000 description 2
- 239000000137 peptide hydrolase inhibitor Substances 0.000 description 2
- 210000001322 periplasm Anatomy 0.000 description 2
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 2
- 230000001124 posttranscriptional effect Effects 0.000 description 2
- 230000037452 priming Effects 0.000 description 2
- 230000005855 radiation Effects 0.000 description 2
- 230000010076 replication Effects 0.000 description 2
- 101150098466 rpsL gene Proteins 0.000 description 2
- 239000012723 sample buffer Substances 0.000 description 2
- 230000035939 shock Effects 0.000 description 2
- 238000010561 standard procedure Methods 0.000 description 2
- 239000006228 supernatant Substances 0.000 description 2
- RWQNBRDOKXIBIV-UHFFFAOYSA-N thymine Chemical compound CC1=CNC(=O)NC1=O RWQNBRDOKXIBIV-UHFFFAOYSA-N 0.000 description 2
- 239000001226 triphosphate Substances 0.000 description 2
- OWEGMIWEEQEYGQ-UHFFFAOYSA-N 100676-05-9 Natural products OC1C(O)C(O)C(CO)OC1OCC1C(O)C(O)C(O)C(OC2C(OC(O)C(O)C2O)CO)O1 OWEGMIWEEQEYGQ-UHFFFAOYSA-N 0.000 description 1
- MLONYBFKXHEPCD-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol Chemical compound OCC(N)(CO)CO.OCC(N)(CO)CO MLONYBFKXHEPCD-UHFFFAOYSA-N 0.000 description 1
- QFVHZQCOUORWEI-UHFFFAOYSA-N 4-[(4-anilino-5-sulfonaphthalen-1-yl)diazenyl]-5-hydroxynaphthalene-2,7-disulfonic acid Chemical compound C=12C(O)=CC(S(O)(=O)=O)=CC2=CC(S(O)(=O)=O)=CC=1N=NC(C1=CC=CC(=C11)S(O)(=O)=O)=CC=C1NC1=CC=CC=C1 QFVHZQCOUORWEI-UHFFFAOYSA-N 0.000 description 1
- BTJIUGUIPKRLHP-UHFFFAOYSA-N 4-nitrophenol Chemical compound OC1=CC=C([N+]([O-])=O)C=C1 BTJIUGUIPKRLHP-UHFFFAOYSA-N 0.000 description 1
- CCSGGWGTGOLEHK-OBJOEFQTSA-N 5-[(3as,4s,6ar)-2-oxo-1,3,3a,4,6,6a-hexahydrothieno[3,4-d]imidazol-4-yl]-n-(5-aminopentyl)pentanamide Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)NCCCCCN)SC[C@@H]21 CCSGGWGTGOLEHK-OBJOEFQTSA-N 0.000 description 1
- 229930024421 Adenine Natural products 0.000 description 1
- GFFGJBXGBJISGV-UHFFFAOYSA-N Adenine Chemical compound NC1=NC=NC2=C1N=CN2 GFFGJBXGBJISGV-UHFFFAOYSA-N 0.000 description 1
- 241000242764 Aequorea victoria Species 0.000 description 1
- 229920000936 Agarose Polymers 0.000 description 1
- 108010011170 Ala-Trp-Arg-His-Pro-Gln-Phe-Gly-Gly Proteins 0.000 description 1
- 229920000856 Amylose Polymers 0.000 description 1
- 208000002109 Argyria Diseases 0.000 description 1
- 239000002028 Biomass Substances 0.000 description 1
- 108010039209 Blood Coagulation Factors Proteins 0.000 description 1
- 102000015081 Blood Coagulation Factors Human genes 0.000 description 1
- 210000003771 C cell Anatomy 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- 241000701022 Cytomegalovirus Species 0.000 description 1
- PHOQVHQSTUBQQK-SQOUGZDYSA-N D-glucono-1,5-lactone Chemical compound OC[C@H]1OC(=O)[C@H](O)[C@@H](O)[C@@H]1O PHOQVHQSTUBQQK-SQOUGZDYSA-N 0.000 description 1
- 102000053602 DNA Human genes 0.000 description 1
- 238000012270 DNA recombination Methods 0.000 description 1
- 101710088194 Dehydrogenase Proteins 0.000 description 1
- 238000002965 ELISA Methods 0.000 description 1
- 241001522878 Escherichia coli B Species 0.000 description 1
- 241001646716 Escherichia coli K-12 Species 0.000 description 1
- 108010093031 Galactosidases Proteins 0.000 description 1
- 241000206672 Gelidium Species 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 1
- 241000701024 Human betaherpesvirus 5 Species 0.000 description 1
- UFHFLCQGNIYNRP-UHFFFAOYSA-N Hydrogen Chemical compound [H][H] UFHFLCQGNIYNRP-UHFFFAOYSA-N 0.000 description 1
- 241001484259 Lacuna Species 0.000 description 1
- 102000006830 Luminescent Proteins Human genes 0.000 description 1
- 108010047357 Luminescent Proteins Proteins 0.000 description 1
- 229920002774 Maltodextrin Polymers 0.000 description 1
- GUBGYTABKSRVRQ-PICCSMPSSA-N Maltose Natural products O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@@H](CO)OC(O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-PICCSMPSSA-N 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 101100174763 Mus musculus Galk1 gene Proteins 0.000 description 1
- 239000000020 Nitrocellulose Substances 0.000 description 1
- 108091028043 Nucleic acid sequence Proteins 0.000 description 1
- 108010079246 OMPA outer membrane proteins Proteins 0.000 description 1
- 238000010222 PCR analysis Methods 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 108010090127 Periplasmic Proteins Proteins 0.000 description 1
- 101710118538 Protease Proteins 0.000 description 1
- 108010076504 Protein Sorting Signals Proteins 0.000 description 1
- JQYMGXZJTCOARG-UHFFFAOYSA-N Reactive blue 2 Chemical compound C1=2C(=O)C3=CC=CC=C3C(=O)C=2C(N)=C(S(O)(=O)=O)C=C1NC(C=C1S(O)(=O)=O)=CC=C1NC(N=1)=NC(Cl)=NC=1NC1=CC=CC(S(O)(=O)=O)=C1 JQYMGXZJTCOARG-UHFFFAOYSA-N 0.000 description 1
- 102000006382 Ribonucleases Human genes 0.000 description 1
- 108010083644 Ribonucleases Proteins 0.000 description 1
- 241000242583 Scyphozoa Species 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- 108020004682 Single-Stranded DNA Proteins 0.000 description 1
- 101710136739 Teichoic acid poly(glycerol phosphate) polymerase Proteins 0.000 description 1
- 239000004098 Tetracycline Substances 0.000 description 1
- 108020004566 Transfer RNA Proteins 0.000 description 1
- XJLXINKUBYWONI-DQQFMEOOSA-N [[(2r,3r,4r,5r)-5-(6-aminopurin-9-yl)-3-hydroxy-4-phosphonooxyoxolan-2-yl]methoxy-hydroxyphosphoryl] [(2s,3r,4s,5s)-5-(3-carbamoylpyridin-1-ium-1-yl)-3,4-dihydroxyoxolan-2-yl]methyl phosphate Chemical compound NC(=O)C1=CC=C[N+]([C@@H]2[C@H]([C@@H](O)[C@H](COP([O-])(=O)OP(O)(=O)OC[C@@H]3[C@H]([C@@H](OP(O)(O)=O)[C@@H](O3)N3C4=NC=NC(N)=C4N=C3)O)O2)O)=C1 XJLXINKUBYWONI-DQQFMEOOSA-N 0.000 description 1
- QPMSXSBEVQLBIL-CZRHPSIPSA-N ac1mix0p Chemical compound C1=CC=C2N(C[C@H](C)CN(C)C)C3=CC(OC)=CC=C3SC2=C1.O([C@H]1[C@]2(OC)C=CC34C[C@@H]2[C@](C)(O)CCC)C2=C5[C@]41CCN(C)[C@@H]3CC5=CC=C2O QPMSXSBEVQLBIL-CZRHPSIPSA-N 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 229960000643 adenine Drugs 0.000 description 1
- 235000010419 agar Nutrition 0.000 description 1
- 239000000427 antigen Substances 0.000 description 1
- 102000036639 antigens Human genes 0.000 description 1
- 108091007433 antigens Proteins 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 210000004666 bacterial spore Anatomy 0.000 description 1
- 230000000975 bioactive effect Effects 0.000 description 1
- 229960002685 biotin Drugs 0.000 description 1
- 235000020958 biotin Nutrition 0.000 description 1
- 239000011616 biotin Substances 0.000 description 1
- 239000003114 blood coagulation factor Substances 0.000 description 1
- 229940019700 blood coagulation factors Drugs 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 244000309466 calf Species 0.000 description 1
- 229940041514 candida albicans extract Drugs 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 239000013592 cell lysate Substances 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 239000013522 chelant Substances 0.000 description 1
- 150000004697 chelate complex Chemical class 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 239000011248 coating agent Substances 0.000 description 1
- 238000000576 coating method Methods 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 230000008878 coupling Effects 0.000 description 1
- 238000010168 coupling process Methods 0.000 description 1
- 238000005859 coupling reaction Methods 0.000 description 1
- 210000000805 cytoplasm Anatomy 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 239000008367 deionised water Substances 0.000 description 1
- 229910021641 deionized water Inorganic materials 0.000 description 1
- 101150106284 deoR gene Proteins 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- UXGNZZKBCMGWAZ-UHFFFAOYSA-N dimethylformamide dmf Chemical compound CN(C)C=O.CN(C)C=O UXGNZZKBCMGWAZ-UHFFFAOYSA-N 0.000 description 1
- BNIILDVGGAEEIG-UHFFFAOYSA-L disodium hydrogen phosphate Chemical compound [Na+].[Na+].OP([O-])([O-])=O BNIILDVGGAEEIG-UHFFFAOYSA-L 0.000 description 1
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 1
- CETRZFQIITUQQL-UHFFFAOYSA-N dmso dimethylsulfoxide Chemical compound CS(C)=O.CS(C)=O CETRZFQIITUQQL-UHFFFAOYSA-N 0.000 description 1
- 239000012154 double-distilled water Substances 0.000 description 1
- 238000012137 double-staining Methods 0.000 description 1
- 239000012992 electron transfer agent Substances 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 230000008030 elimination Effects 0.000 description 1
- 238000003379 elimination reaction Methods 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- OCLXJTCGWSSVOE-UHFFFAOYSA-N ethanol etoh Chemical compound CCO.CCO OCLXJTCGWSSVOE-UHFFFAOYSA-N 0.000 description 1
- 229960005542 ethidium bromide Drugs 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 230000002349 favourable effect Effects 0.000 description 1
- 230000005714 functional activity Effects 0.000 description 1
- 238000011990 functional testing Methods 0.000 description 1
- 101150048790 gdhB gene Proteins 0.000 description 1
- 229960003681 gluconolactone Drugs 0.000 description 1
- 230000013595 glycosylation Effects 0.000 description 1
- 238000006206 glycosylation reaction Methods 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 229910052739 hydrogen Inorganic materials 0.000 description 1
- 239000001257 hydrogen Substances 0.000 description 1
- 229940027941 immunoglobulin g Drugs 0.000 description 1
- 230000016784 immunoglobulin production Effects 0.000 description 1
- 239000003547 immunosorbent Substances 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 238000011081 inoculation Methods 0.000 description 1
- 230000002452 interceptive effect Effects 0.000 description 1
- 230000000968 intestinal effect Effects 0.000 description 1
- JORABGDXCIBAFL-UHFFFAOYSA-M iodonitrotetrazolium chloride Chemical compound [Cl-].C1=CC([N+](=O)[O-])=CC=C1N1[N+](C=2C=CC(I)=CC=2)=NC(C=2C=CC=CC=2)=N1 JORABGDXCIBAFL-UHFFFAOYSA-M 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- 229930027917 kanamycin Natural products 0.000 description 1
- 229960000318 kanamycin Drugs 0.000 description 1
- 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 1
- 229930182823 kanamycin A Natural products 0.000 description 1
- 101150066555 lacZ gene Proteins 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 239000006166 lysate Substances 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 238000002844 melting Methods 0.000 description 1
- 230000008018 melting Effects 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- 238000013508 migration Methods 0.000 description 1
- 230000005012 migration Effects 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 229910000402 monopotassium phosphate Inorganic materials 0.000 description 1
- 235000019796 monopotassium phosphate Nutrition 0.000 description 1
- 238000002703 mutagenesis Methods 0.000 description 1
- 231100000350 mutagenesis Toxicity 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
- 239000006225 natural substrate Substances 0.000 description 1
- 229930027945 nicotinamide-adenine dinucleotide Natural products 0.000 description 1
- 229920001220 nitrocellulos Polymers 0.000 description 1
- 108020004707 nucleic acids Proteins 0.000 description 1
- 102000039446 nucleic acids Human genes 0.000 description 1
- 150000007523 nucleic acids Chemical class 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 230000002018 overexpression Effects 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 239000000123 paper Substances 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- 239000012071 phase Substances 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- PJNZPQUBCPKICU-UHFFFAOYSA-N phosphoric acid;potassium Chemical compound [K].OP(O)(O)=O PJNZPQUBCPKICU-UHFFFAOYSA-N 0.000 description 1
- 230000026731 phosphorylation Effects 0.000 description 1
- 238000006366 phosphorylation reaction Methods 0.000 description 1
- 238000005375 photometry Methods 0.000 description 1
- 239000002985 plastic film Substances 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 238000003752 polymerase chain reaction Methods 0.000 description 1
- 239000013641 positive control Substances 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 210000001236 prokaryotic cell Anatomy 0.000 description 1
- 238000002331 protein detection Methods 0.000 description 1
- 239000012460 protein solution Substances 0.000 description 1
- 238000001243 protein synthesis Methods 0.000 description 1
- 238000010188 recombinant method Methods 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
- 230000000717 retained effect Effects 0.000 description 1
- 108020004418 ribosomal RNA Proteins 0.000 description 1
- 229920002477 rna polymer Polymers 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 239000013606 secretion vector Substances 0.000 description 1
- 238000011896 sensitive detection Methods 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 238000013207 serial dilution Methods 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 239000007790 solid phase Substances 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 238000011895 specific detection Methods 0.000 description 1
- 230000028070 sporulation Effects 0.000 description 1
- 238000007447 staining method Methods 0.000 description 1
- 239000008223 sterile water Substances 0.000 description 1
- 239000012536 storage buffer Substances 0.000 description 1
- 229960002180 tetracycline Drugs 0.000 description 1
- 235000019364 tetracycline Nutrition 0.000 description 1
- 150000003522 tetracyclines Chemical class 0.000 description 1
- 229940113082 thymine Drugs 0.000 description 1
- 238000001890 transfection Methods 0.000 description 1
- 230000014616 translation Effects 0.000 description 1
- YNJBWRMUSHSURL-UHFFFAOYSA-N trichloroacetic acid Chemical compound OC(=O)C(Cl)(Cl)Cl YNJBWRMUSHSURL-UHFFFAOYSA-N 0.000 description 1
- GPRLSGONYQIRFK-MNYXATJNSA-N triton Chemical compound [3H+] GPRLSGONYQIRFK-MNYXATJNSA-N 0.000 description 1
- 239000012137 tryptone Substances 0.000 description 1
- 238000011144 upstream manufacturing Methods 0.000 description 1
- 229940035893 uracil Drugs 0.000 description 1
- 239000012138 yeast extract Substances 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K19/00—Hybrid peptides, i.e. peptides covalently bound to nucleic acids, or non-covalently bound protein-protein complexes
-
- 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
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/0004—Oxidoreductases (1.)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/81—Protease inhibitors
- C07K14/815—Protease inhibitors from leeches, e.g. hirudin, eglin
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
-
- 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
- C12N2799/00—Uses of viruses
- C12N2799/02—Uses of viruses as vector
- C12N2799/021—Uses of viruses as vector for the expression of a heterologous nucleic acid
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Genetics & Genomics (AREA)
- Biochemistry (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- General Health & Medical Sciences (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biophysics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Tropical Medicine & Parasitology (AREA)
- Biotechnology (AREA)
- Microbiology (AREA)
- Biomedical Technology (AREA)
- Gastroenterology & Hepatology (AREA)
- General Engineering & Computer Science (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Enzymes And Modification Thereof (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
- Investigating Or Analysing Biological Materials (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DE19906920 | 1999-02-19 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| ZA200107686B true ZA200107686B (en) | 2002-12-18 |
Family
ID=7897979
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| ZA200107686A ZA200107686B (en) | 1999-02-19 | 2001-09-18 | Glucose dehydrogenase fusion proteins and their utilization in expression systems. |
Country Status (16)
| Country | Link |
|---|---|
| US (1) | US20050112744A1 (pt) |
| EP (1) | EP1155130A2 (pt) |
| JP (1) | JP2002538782A (pt) |
| KR (1) | KR20010103017A (pt) |
| CN (1) | CN1340104A (pt) |
| AR (1) | AR022630A1 (pt) |
| AU (1) | AU771320B2 (pt) |
| BR (1) | BR0008370A (pt) |
| CA (1) | CA2368461A1 (pt) |
| CZ (1) | CZ20012739A3 (pt) |
| HU (1) | HUP0200285A2 (pt) |
| NO (1) | NO20014011L (pt) |
| PL (1) | PL350574A1 (pt) |
| SK (1) | SK11742001A3 (pt) |
| WO (1) | WO2000049039A2 (pt) |
| ZA (1) | ZA200107686B (pt) |
Families Citing this family (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| ATE390481T1 (de) * | 2001-12-21 | 2008-04-15 | Curacyte Ag | Modifizierte tridegine, ihre herstellung und verwendung als transglutaminase-inhibitoren |
| MXPA06001719A (es) | 2003-08-11 | 2006-05-19 | Codexis Inc | Polipeptidos de glucosa deshidrogenasa mejorados, y polinucleotidos relacionados. |
| HUE032804T2 (en) * | 2006-04-13 | 2017-11-28 | Hoffmann La Roche | Enhanced mutants of pyrroloquinoline-quinone-dependent soluble glucose dehydrogenase |
| CN110894504A (zh) * | 2019-12-20 | 2020-03-20 | 武汉茵慕生物科技有限公司 | 强化表达葡萄糖6-磷酸脱氢酶的地衣芽胞杆菌在异源蛋白生产中的应用 |
Family Cites Families (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS60141299A (ja) * | 1983-12-28 | 1985-07-26 | Wako Pure Chem Ind Ltd | 脱水素酵素の活性度測定法 |
| JPS63230098A (ja) * | 1987-03-18 | 1988-09-26 | Fujitsu Ltd | 酵素の分析方法 |
| DE3711881A1 (de) * | 1987-04-08 | 1988-10-27 | Merck Patent Gmbh | Verfahren zur herstellung von glucosedehydrogenase aus bacillus megaterium |
| AU4032997A (en) * | 1997-02-07 | 1998-08-26 | Kaneka Corporation | Novel carbonyl reductase, gene that encodes the same, and method of utilizing these |
| US6399859B1 (en) * | 1997-12-10 | 2002-06-04 | Pioneer Hi-Bred International, Inc. | Plant uridine diphosphate-glucose dehydrogenase genes, proteins, and uses thereof |
-
2000
- 2000-02-08 EP EP00903672A patent/EP1155130A2/de not_active Withdrawn
- 2000-02-08 JP JP2000599776A patent/JP2002538782A/ja active Pending
- 2000-02-08 PL PL00350574A patent/PL350574A1/xx unknown
- 2000-02-08 CZ CZ20012739A patent/CZ20012739A3/cs unknown
- 2000-02-08 HU HU0200285A patent/HUP0200285A2/hu unknown
- 2000-02-08 CN CN00803879A patent/CN1340104A/zh active Pending
- 2000-02-08 KR KR1020017010567A patent/KR20010103017A/ko not_active Application Discontinuation
- 2000-02-08 BR BR0008370-4A patent/BR0008370A/pt not_active Application Discontinuation
- 2000-02-08 CA CA002368461A patent/CA2368461A1/en not_active Abandoned
- 2000-02-08 SK SK1174-2001A patent/SK11742001A3/sk unknown
- 2000-02-08 WO PCT/EP2000/000978 patent/WO2000049039A2/de not_active Application Discontinuation
- 2000-02-08 AU AU25468/00A patent/AU771320B2/en not_active Ceased
- 2000-02-18 AR ARP000100695A patent/AR022630A1/es unknown
-
2001
- 2001-08-17 NO NO20014011A patent/NO20014011L/no not_active Application Discontinuation
- 2001-09-18 ZA ZA200107686A patent/ZA200107686B/en unknown
-
2003
- 2003-10-09 US US10/681,207 patent/US20050112744A1/en not_active Abandoned
Also Published As
| Publication number | Publication date |
|---|---|
| AU2546800A (en) | 2000-09-04 |
| AU771320B2 (en) | 2004-03-18 |
| JP2002538782A (ja) | 2002-11-19 |
| NO20014011D0 (no) | 2001-08-17 |
| CA2368461A1 (en) | 2000-08-24 |
| CN1340104A (zh) | 2002-03-13 |
| EP1155130A2 (de) | 2001-11-21 |
| US20050112744A1 (en) | 2005-05-26 |
| NO20014011L (no) | 2001-10-02 |
| KR20010103017A (ko) | 2001-11-17 |
| HUP0200285A2 (hu) | 2002-05-29 |
| BR0008370A (pt) | 2001-11-06 |
| WO2000049039A3 (de) | 2000-12-14 |
| WO2000049039A2 (de) | 2000-08-24 |
| CZ20012739A3 (cs) | 2001-11-14 |
| SK11742001A3 (sk) | 2002-03-05 |
| PL350574A1 (en) | 2002-12-30 |
| AR022630A1 (es) | 2002-09-04 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US5338678A (en) | Expression of DNA sequences encoding a thermally stable cytosine deaminase from saccharomyces | |
| US4375514A (en) | Preparation and use of recombinant plasmids containing genes for alkaline phosphatases | |
| FI95046C (fi) | Menetelmä lämpöstabiilin sytosiinideaminaasin tuottamiseksi | |
| KR960002869B1 (ko) | 이황화 결합을 갖는 분비된 단백질의 수율을 증가시키는 방법 | |
| JP2008119000A (ja) | タンパク質の産生方法 | |
| AU730811B2 (en) | AFC1 and RCE1:isoprenylated CAAX processing enzymes | |
| Wang et al. | Expression, purification, and characterization of the functional dimeric cytoplasmic domain of human erythrocyte band 3 in Escherichia coli | |
| Kotler et al. | Activity of avian retroviral protease expressed in Escherichia coli | |
| ZA200107686B (en) | Glucose dehydrogenase fusion proteins and their utilization in expression systems. | |
| Zijderveld et al. | Differences between inner membrane and peptidoglycan-associated PBP1B dimers of Escherichia coli | |
| Anisimova et al. | Renaturation, activation, and practical use of recombinant duplex-specific nuclease from Kamchatka crab | |
| JP2971290B2 (ja) | プラスミド及びそれで形質転換されたエシェリチア・コリ | |
| JPH0638771A (ja) | ヒトプロテインジスルフィドイソメラーゼ遺伝子の発現方法および該遺伝子との共発現によるポリペプチドの製造方法 | |
| RU2760578C2 (ru) | Слитый белок, содержащий модифицированный безметиониновый белок GroEL и димер полипептида полифемузина I | |
| Ibrahim et al. | Determination of the optimal conditions of cloning Aerolysin gene from the common carp pathogen Aeromonas hydrophila in Escherichia coli BL21 | |
| RU2355769C1 (ru) | СПОСОБ ПОЛУЧЕНИЯ ФУНКЦИОНАЛЬНО АКТИВНОГО РЕКОМБИНАНТНОГО БЕЛКА ЛЕТАЛЬНОГО ФАКТОРА СИБИРСКОЙ ЯЗВЫ (LF), РЕКОМБИНАНТНАЯ ПЛАЗМИДНАЯ ДНК pETGST-LFmin, КОДИРУЮЩАЯ АКТИВНЫЙ БЕЛОК LF, И ШТАММ Escherichia coli BL-GSTLFmin, ПРОДУЦИРУЮЩИЙ АКТИВНЫЙ БЕЛОК ЛЕТАЛЬНОГО ФАКТОРА СИБИРСКОЙ ЯЗВЫ | |
| Ubeidat et al. | Expression and one-step purification of a developmentally regulated protein from Dictyostelium discoideum | |
| Keßler et al. | Ser644 is important for catalytic activity but is not involved in cAMP-dependent phosphorylation of yeast 6-phosphofructo-2-kinase | |
| RU2058391C1 (ru) | ПОЛИПЕПТИД, ФРАГМЕНТ ДНК НС270, ШТАММ БАКТЕРИЙ ESCHERICHIA COLI - ПРОДУЦЕНТ ПОЛИПЕПТИДА НС86, СЛИТОГО С β ГАЛАКТОЗИДАЗОЙ ESCHERICHIA COLI | |
| RU2361921C1 (ru) | СПОСОБ ПОЛУЧЕНИЯ ФУНКЦИОНАЛЬНО АКТИВНОГО РЕКОМБИНАНТНОГО БЕЛКА ЛЕТАЛЬНОГО ФАКТОРА ЯЗВЫ (LF), РЕКОМБИНАНТНАЯ ПЛАЗМИДНАЯ ДНК pETHIS-LF, КОДИРУЮЩАЯ АКТИВНЫЙ БЕЛОК LF И ШТАММ ESCHERICHIA COLI BL-HISLF, ПРОДУЦИРУЮЩИЙ АКТИВНЫЙ БЕЛОК ЛЕТАЛЬНОГО ФАКТОРА СИБИРСКОЙ ЯЗВЫ | |
| JP3484954B2 (ja) | Ｄｎａジャイレース阻害蛋白質 | |
| MXPA01008380A (en) | Glucose dehydrogenase fusion proteins and their utilization in expression systems | |
| JPS6167490A (ja) | Ｐ▲ｌ▼プロモ−タ−を有する環状二重鎖ｄｎａ | |
| JP2001033448A (ja) | 組み換え型ウイルス抗原の調製法 | |
| KR20010009554A (ko) | 세포 사멸 관련 유전자의 검색 키트 |