TWI482860B - 利用安定之輔酶使去氫酶安定之方法 - Google Patents
利用安定之輔酶使去氫酶安定之方法 Download PDFInfo
- Publication number
- TWI482860B TWI482860B TW098105120A TW98105120A TWI482860B TW I482860 B TWI482860 B TW I482860B TW 098105120 A TW098105120 A TW 098105120A TW 98105120 A TW98105120 A TW 98105120A TW I482860 B TWI482860 B TW I482860B
- Authority
- TW
- Taiwan
- Prior art keywords
- enzyme
- stabilized
- coenzyme
- stored
- dehydrogenase
- Prior art date
Links
- 239000005515 coenzyme Substances 0.000 title claims description 91
- 238000000034 method Methods 0.000 title claims description 42
- AAOVKJBEBIDNHE-UHFFFAOYSA-N diazepam Chemical compound N=1CC(=O)N(C)C2=CC=C(Cl)C=C2C=1C1=CC=CC=C1 AAOVKJBEBIDNHE-UHFFFAOYSA-N 0.000 title claims description 14
- 229960003529 diazepam Drugs 0.000 title claims description 14
- 101710088194 Dehydrogenase Proteins 0.000 title claims description 7
- 230000000087 stabilizing effect Effects 0.000 title claims description 5
- 102000004190 Enzymes Human genes 0.000 claims description 131
- 108090000790 Enzymes Proteins 0.000 claims description 131
- 229930027945 nicotinamide-adenine dinucleotide Natural products 0.000 claims description 95
- 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 claims description 85
- 108010050375 Glucose 1-Dehydrogenase Proteins 0.000 claims description 83
- 229950006238 nadide Drugs 0.000 claims description 81
- 238000012360 testing method Methods 0.000 claims description 34
- 150000001413 amino acids Chemical class 0.000 claims description 27
- 108010021809 Alcohol dehydrogenase Proteins 0.000 claims description 26
- 239000012491 analyte Substances 0.000 claims description 20
- 238000001514 detection method Methods 0.000 claims description 19
- -1 1.1.1.28) Proteins 0.000 claims description 18
- 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 claims description 18
- 150000001875 compounds Chemical class 0.000 claims description 14
- 239000003153 chemical reaction reagent Substances 0.000 claims description 13
- 229910052760 oxygen Inorganic materials 0.000 claims description 11
- 229910052717 sulfur Inorganic materials 0.000 claims description 11
- 125000004122 cyclic group Chemical group 0.000 claims description 10
- 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 claims description 10
- 102000007698 Alcohol dehydrogenase Human genes 0.000 claims description 9
- 229910052757 nitrogen Inorganic materials 0.000 claims description 9
- 125000004432 carbon atom Chemical group C* 0.000 claims description 8
- 230000003197 catalytic effect Effects 0.000 claims description 7
- 239000002274 desiccant Substances 0.000 claims description 7
- GFFGJBXGBJISGV-UHFFFAOYSA-N Adenine Chemical compound NC1=NC=NC2=C1N=CN2 GFFGJBXGBJISGV-UHFFFAOYSA-N 0.000 claims description 6
- 102000003855 L-lactate dehydrogenase Human genes 0.000 claims description 6
- 108700023483 L-lactate dehydrogenases Proteins 0.000 claims description 6
- 229910052739 hydrogen Inorganic materials 0.000 claims description 6
- 239000007791 liquid phase Substances 0.000 claims description 6
- IJGRMHOSHXDMSA-UHFFFAOYSA-N nitrogen Substances N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 claims description 6
- 229930024421 Adenine Natural products 0.000 claims description 5
- 229960000643 adenine Drugs 0.000 claims description 5
- 230000015556 catabolic process Effects 0.000 claims description 5
- 150000003839 salts Chemical class 0.000 claims description 5
- JUJWROOIHBZHMG-UHFFFAOYSA-N Pyridine Chemical group C1=CC=NC=C1 JUJWROOIHBZHMG-UHFFFAOYSA-N 0.000 claims description 4
- 229910052799 carbon Inorganic materials 0.000 claims description 4
- 238000006731 degradation reaction Methods 0.000 claims description 4
- 125000005842 heteroatom Chemical group 0.000 claims description 4
- 125000002467 phosphate group Chemical group [H]OP(=O)(O[H])O[*] 0.000 claims description 4
- 108010026217 Malate Dehydrogenase Proteins 0.000 claims description 3
- 102000013460 Malate Dehydrogenase Human genes 0.000 claims description 3
- 230000003301 hydrolyzing effect Effects 0.000 claims description 3
- 125000006727 (C1-C6) alkenyl group Chemical group 0.000 claims description 2
- GVNVAWHJIKLAGL-UHFFFAOYSA-N 2-(cyclohexen-1-yl)cyclohexan-1-one Chemical compound O=C1CCCCC1C1=CCCCC1 GVNVAWHJIKLAGL-UHFFFAOYSA-N 0.000 claims description 2
- 125000001054 5 membered carbocyclic group Chemical group 0.000 claims description 2
- 101150065749 Churc1 gene Proteins 0.000 claims description 2
- 101000892220 Geobacillus thermodenitrificans (strain NG80-2) Long-chain-alcohol dehydrogenase 1 Proteins 0.000 claims description 2
- 108700040097 Glycerol dehydrogenases Proteins 0.000 claims description 2
- 108010009384 L-Iditol 2-Dehydrogenase Proteins 0.000 claims description 2
- 108030000198 L-amino-acid dehydrogenases Proteins 0.000 claims description 2
- 102100038239 Protein Churchill Human genes 0.000 claims description 2
- 102100026974 Sorbitol dehydrogenase Human genes 0.000 claims description 2
- 229910052770 Uranium Inorganic materials 0.000 claims description 2
- 125000006297 carbonyl amino group Chemical group [H]N([*:2])C([*:1])=O 0.000 claims description 2
- 229910052736 halogen Inorganic materials 0.000 claims description 2
- 125000000623 heterocyclic group Chemical group 0.000 claims description 2
- 125000000962 organic group Chemical group 0.000 claims description 2
- 229920006395 saturated elastomer Polymers 0.000 claims description 2
- 125000001424 substituent group Chemical group 0.000 claims description 2
- 108010050201 2-hydroxybutyrate dehydrogenase Proteins 0.000 claims 1
- 108020005199 Dehydrogenases Proteins 0.000 claims 1
- 150000002367 halogens Chemical class 0.000 claims 1
- 125000004433 nitrogen atom Chemical group N* 0.000 claims 1
- 125000004430 oxygen atom Chemical group O* 0.000 claims 1
- 125000004434 sulfur atom Chemical group 0.000 claims 1
- 229940088598 enzyme Drugs 0.000 description 102
- DGPLSUKWXXSBCU-UHFFFAOYSA-N [[5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl] [4-(3-carbamoylpyridin-1-ium-1-yl)-2,3-dihydroxycyclopentyl]methyl phosphate Chemical compound NC(=O)C1=CC=C[N+](C2C(C(O)C(COP([O-])(=O)OP(O)(=O)OCC3C(C(O)C(O3)N3C4=NC=NC(N)=C4N=C3)O)C2)O)=C1 DGPLSUKWXXSBCU-UHFFFAOYSA-N 0.000 description 56
- 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 33
- 239000008103 glucose Substances 0.000 description 33
- 230000000694 effects Effects 0.000 description 30
- 238000003860 storage Methods 0.000 description 29
- 235000001014 amino acid Nutrition 0.000 description 18
- 238000005259 measurement Methods 0.000 description 14
- 239000002609 medium Substances 0.000 description 13
- 230000003287 optical effect Effects 0.000 description 13
- 238000006243 chemical reaction Methods 0.000 description 9
- 230000035772 mutation Effects 0.000 description 9
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 7
- 238000004458 analytical method Methods 0.000 description 7
- 230000006870 function Effects 0.000 description 6
- 238000001502 gel electrophoresis Methods 0.000 description 6
- 238000005375 photometry Methods 0.000 description 6
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 5
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 5
- 210000004369 blood Anatomy 0.000 description 5
- 239000008280 blood Substances 0.000 description 5
- 230000007423 decrease Effects 0.000 description 5
- 235000013922 glutamic acid Nutrition 0.000 description 5
- 239000004220 glutamic acid Substances 0.000 description 5
- 239000007788 liquid Substances 0.000 description 5
- 239000000126 substance Substances 0.000 description 5
- BXGYYDRIMBPOMN-UHFFFAOYSA-N 2-(hydroxymethoxy)ethoxymethanol Chemical compound OCOCCOCO BXGYYDRIMBPOMN-UHFFFAOYSA-N 0.000 description 4
- 244000063299 Bacillus subtilis Species 0.000 description 4
- 235000014469 Bacillus subtilis Nutrition 0.000 description 4
- 102000004316 Oxidoreductases Human genes 0.000 description 4
- 108090000854 Oxidoreductases Proteins 0.000 description 4
- 239000002253 acid Substances 0.000 description 4
- 238000011325 biochemical measurement Methods 0.000 description 4
- 230000001419 dependent effect Effects 0.000 description 4
- 238000002848 electrochemical method Methods 0.000 description 4
- 230000002255 enzymatic effect Effects 0.000 description 4
- 125000003147 glycosyl group Chemical group 0.000 description 4
- 230000007774 longterm Effects 0.000 description 4
- 125000000548 ribosyl group Chemical group C1([C@H](O)[C@H](O)[C@H](O1)CO)* 0.000 description 4
- 230000006641 stabilisation Effects 0.000 description 4
- 238000011105 stabilization Methods 0.000 description 4
- VEPOHXYIFQMVHW-XOZOLZJESA-N 2,3-dihydroxybutanedioic acid (2S,3S)-3,4-dimethyl-2-phenylmorpholine Chemical compound OC(C(O)C(O)=O)C(O)=O.C[C@H]1[C@@H](OCCN1C)c1ccccc1 VEPOHXYIFQMVHW-XOZOLZJESA-N 0.000 description 3
- 241000894006 Bacteria Species 0.000 description 3
- 102000004420 Creatine Kinase Human genes 0.000 description 3
- 108010042126 Creatine kinase Proteins 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- 239000004471 Glycine Substances 0.000 description 3
- DFPAKSUCGFBDDF-UHFFFAOYSA-N Nicotinamide Chemical group NC(=O)C1=CC=CN=C1 DFPAKSUCGFBDDF-UHFFFAOYSA-N 0.000 description 3
- PCNDJXKNXGMECE-UHFFFAOYSA-N Phenazine Natural products C1=CC=CC2=NC3=CC=CC=C3N=C21 PCNDJXKNXGMECE-UHFFFAOYSA-N 0.000 description 3
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 3
- 239000000872 buffer Substances 0.000 description 3
- 238000006555 catalytic reaction Methods 0.000 description 3
- 239000000499 gel Substances 0.000 description 3
- MMXZSJMASHPLLR-UHFFFAOYSA-N pyrroloquinoline quinone Chemical compound C12=C(C(O)=O)C=C(C(O)=O)N=C2C(=O)C(=O)C2=C1NC(C(=O)O)=C2 MMXZSJMASHPLLR-UHFFFAOYSA-N 0.000 description 3
- 238000006722 reduction reaction Methods 0.000 description 3
- 238000006467 substitution reaction Methods 0.000 description 3
- AZQWKYJCGOJGHM-UHFFFAOYSA-N 1,4-benzoquinone Chemical compound O=C1C=CC(=O)C=C1 AZQWKYJCGOJGHM-UHFFFAOYSA-N 0.000 description 2
- 102000004008 5'-Nucleotidase Human genes 0.000 description 2
- CIWBSHSKHKDKBQ-JLAZNSOCSA-N Ascorbic acid Chemical compound OC[C@H](O)[C@H]1OC(=O)C(O)=C1O CIWBSHSKHKDKBQ-JLAZNSOCSA-N 0.000 description 2
- CURLTUGMZLYLDI-UHFFFAOYSA-N Carbon dioxide Chemical compound O=C=O CURLTUGMZLYLDI-UHFFFAOYSA-N 0.000 description 2
- 108010089254 Cholesterol oxidase Proteins 0.000 description 2
- HMFHBZSHGGEWLO-SOOFDHNKSA-N D-ribofuranose Chemical compound OC[C@H]1OC(O)[C@H](O)[C@@H]1O HMFHBZSHGGEWLO-SOOFDHNKSA-N 0.000 description 2
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 2
- 108010015776 Glucose oxidase Proteins 0.000 description 2
- 108010020056 Hydrogenase Proteins 0.000 description 2
- 239000004472 Lysine Substances 0.000 description 2
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 2
- LCTONWCANYUPML-UHFFFAOYSA-N Pyruvic acid Chemical compound CC(=O)C(O)=O LCTONWCANYUPML-UHFFFAOYSA-N 0.000 description 2
- PYMYPHUHKUWMLA-LMVFSUKVSA-N Ribose Natural products OC[C@@H](O)[C@@H](O)[C@@H](O)C=O PYMYPHUHKUWMLA-LMVFSUKVSA-N 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 2
- DGEZNRSVGBDHLK-UHFFFAOYSA-N [1,10]phenanthroline Chemical compound C1=CN=C2C3=NC=CC=C3C=CC2=C1 DGEZNRSVGBDHLK-UHFFFAOYSA-N 0.000 description 2
- 239000002250 absorbent Substances 0.000 description 2
- 230000002745 absorbent Effects 0.000 description 2
- HMFHBZSHGGEWLO-UHFFFAOYSA-N alpha-D-Furanose-Ribose Natural products OCC1OC(O)C(O)C1O HMFHBZSHGGEWLO-UHFFFAOYSA-N 0.000 description 2
- 125000002837 carbocyclic group Chemical group 0.000 description 2
- 230000006652 catabolic pathway Effects 0.000 description 2
- 230000008859 change Effects 0.000 description 2
- HVYWMOMLDIMFJA-DPAQBDIFSA-N cholesterol Chemical compound C1C=C2C[C@@H](O)CC[C@]2(C)[C@@H]2[C@@H]1[C@@H]1CC[C@H]([C@H](C)CCCC(C)C)[C@@]1(C)CC2 HVYWMOMLDIMFJA-DPAQBDIFSA-N 0.000 description 2
- 238000002983 circular dichroism Methods 0.000 description 2
- 230000019771 cognition Effects 0.000 description 2
- 238000006911 enzymatic reaction Methods 0.000 description 2
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 description 2
- 238000006460 hydrolysis reaction Methods 0.000 description 2
- JVTAAEKCZFNVCJ-UHFFFAOYSA-N lactic acid Chemical compound CC(O)C(O)=O JVTAAEKCZFNVCJ-UHFFFAOYSA-N 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- 108010043671 prostatic acid phosphatase Proteins 0.000 description 2
- 150000003222 pyridines Chemical class 0.000 description 2
- XSCHRSMBECNVNS-UHFFFAOYSA-N quinoxaline Chemical compound N1=CC=NC2=CC=CC=C21 XSCHRSMBECNVNS-UHFFFAOYSA-N 0.000 description 2
- YGSDEFSMJLZEOE-UHFFFAOYSA-N salicylic acid Chemical compound OC(=O)C1=CC=CC=C1O YGSDEFSMJLZEOE-UHFFFAOYSA-N 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- HDTRYLNUVZCQOY-UHFFFAOYSA-N α-D-glucopyranosyl-α-D-glucopyranoside Natural products OC1C(O)C(O)C(CO)OC1OC1C(O)C(O)C(O)C(CO)O1 HDTRYLNUVZCQOY-UHFFFAOYSA-N 0.000 description 1
- 125000006728 (C1-C6) alkynyl group Chemical group 0.000 description 1
- BJEPYKJPYRNKOW-REOHCLBHSA-N (S)-malic acid Chemical compound OC(=O)[C@@H](O)CC(O)=O BJEPYKJPYRNKOW-REOHCLBHSA-N 0.000 description 1
- AFENDNXGAFYKQO-UHFFFAOYSA-N 2-hydroxybutyric acid Chemical compound CCC(O)C(O)=O AFENDNXGAFYKQO-UHFFFAOYSA-N 0.000 description 1
- JPFNWUUUXFFWOQ-UHFFFAOYSA-N 7h-purin-6-amine;1-pyridin-3-ylethanone Chemical compound CC(=O)C1=CC=CN=C1.NC1=NC=NC2=C1NC=N2 JPFNWUUUXFFWOQ-UHFFFAOYSA-N 0.000 description 1
- YYVYAPXYZVYDHN-UHFFFAOYSA-N 9,10-phenanthroquinone Chemical compound C1=CC=C2C(=O)C(=O)C3=CC=CC=C3C2=C1 YYVYAPXYZVYDHN-UHFFFAOYSA-N 0.000 description 1
- PWJFNRJRHXWEPT-UHFFFAOYSA-N ADP ribose Natural products C1=NC=2C(N)=NC=NC=2N1C1OC(COP(O)(=O)OP(O)(=O)OCC(O)C(O)C(O)C=O)C(O)C1O PWJFNRJRHXWEPT-UHFFFAOYSA-N 0.000 description 1
- SRNWOUGRCWSEMX-KEOHHSTQSA-N ADP-beta-D-ribose Chemical compound C([C@H]1O[C@H]([C@@H]([C@@H]1O)O)N1C=2N=CN=C(C=2N=C1)N)OP(O)(=O)OP(O)(=O)OC[C@H]1O[C@@H](O)[C@H](O)[C@@H]1O SRNWOUGRCWSEMX-KEOHHSTQSA-N 0.000 description 1
- 102000000074 ADP-ribosyl Cyclase Human genes 0.000 description 1
- 108010080394 ADP-ribosyl Cyclase Proteins 0.000 description 1
- 102100036475 Alanine aminotransferase 1 Human genes 0.000 description 1
- 108010082126 Alanine transaminase Proteins 0.000 description 1
- QGZKDVFQNNGYKY-UHFFFAOYSA-O Ammonium Chemical compound [NH4+] QGZKDVFQNNGYKY-UHFFFAOYSA-O 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- 241000194107 Bacillus megaterium Species 0.000 description 1
- 241000193388 Bacillus thuringiensis Species 0.000 description 1
- FBPFZTCFMRRESA-KAZBKCHUSA-N D-altritol Chemical compound OC[C@@H](O)[C@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-KAZBKCHUSA-N 0.000 description 1
- 241000206602 Eukaryota Species 0.000 description 1
- 239000004366 Glucose oxidase Substances 0.000 description 1
- 108010024636 Glutathione Proteins 0.000 description 1
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 1
- 150000008575 L-amino acids Chemical class 0.000 description 1
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 1
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
- 241000124008 Mammalia Species 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- ZOKXTWBITQBERF-UHFFFAOYSA-N Molybdenum Chemical compound [Mo] ZOKXTWBITQBERF-UHFFFAOYSA-N 0.000 description 1
- JLEBZPBDRKPWTD-TURQNECASA-O N-ribosylnicotinamide Chemical group NC(=O)C1=CC=C[N+]([C@H]2[C@@H]([C@H](O)[C@@H](CO)O2)O)=C1 JLEBZPBDRKPWTD-TURQNECASA-O 0.000 description 1
- XJLXINKUBYWONI-NNYOXOHSSA-O NADP(+) 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-NNYOXOHSSA-O 0.000 description 1
- KUFMXPZUZBPFCT-UHFFFAOYSA-N P(O)(OCOP(O)=O)=O Chemical compound P(O)(OCOP(O)=O)=O KUFMXPZUZBPFCT-UHFFFAOYSA-N 0.000 description 1
- 102000004160 Phosphoric Monoester Hydrolases Human genes 0.000 description 1
- 108090000608 Phosphoric Monoester Hydrolases Proteins 0.000 description 1
- 102000007562 Serum Albumin Human genes 0.000 description 1
- 108010071390 Serum Albumin Proteins 0.000 description 1
- 108090000340 Transaminases Proteins 0.000 description 1
- 102000003929 Transaminases Human genes 0.000 description 1
- HDTRYLNUVZCQOY-WSWWMNSNSA-N Trehalose Natural products O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@@H](O)[C@@H](CO)O1 HDTRYLNUVZCQOY-WSWWMNSNSA-N 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 150000003838 adenosines Chemical class 0.000 description 1
- 239000003513 alkali Substances 0.000 description 1
- HDTRYLNUVZCQOY-LIZSDCNHSA-N alpha,alpha-trehalose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 HDTRYLNUVZCQOY-LIZSDCNHSA-N 0.000 description 1
- BJEPYKJPYRNKOW-UHFFFAOYSA-N alpha-hydroxysuccinic acid Natural products OC(=O)C(O)CC(O)=O BJEPYKJPYRNKOW-UHFFFAOYSA-N 0.000 description 1
- 229910000147 aluminium phosphate Inorganic materials 0.000 description 1
- 150000001412 amines Chemical class 0.000 description 1
- 150000001450 anions Chemical class 0.000 description 1
- PYKYMHQGRFAEBM-UHFFFAOYSA-N anthraquinone Natural products CCC(=O)c1c(O)c2C(=O)C3C(C=CC=C3O)C(=O)c2cc1CC(=O)OC PYKYMHQGRFAEBM-UHFFFAOYSA-N 0.000 description 1
- 150000004056 anthraquinones Chemical class 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 235000010323 ascorbic acid Nutrition 0.000 description 1
- 229960005070 ascorbic acid Drugs 0.000 description 1
- 239000011668 ascorbic acid Substances 0.000 description 1
- 235000003704 aspartic acid Nutrition 0.000 description 1
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 1
- 230000002238 attenuated effect Effects 0.000 description 1
- 229940097012 bacillus thuringiensis Drugs 0.000 description 1
- WZJYKHNJTSNBHV-UHFFFAOYSA-O benzo[h]quinolin-1-ium Chemical compound C1=C[NH+]=C2C3=CC=CC=C3C=CC2=C1 WZJYKHNJTSNBHV-UHFFFAOYSA-O 0.000 description 1
- 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 1
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 1
- 125000002619 bicyclic group Chemical group 0.000 description 1
- 210000001124 body fluid Anatomy 0.000 description 1
- 239000010839 body fluid Substances 0.000 description 1
- 125000001369 canonical nucleoside group Chemical group 0.000 description 1
- 239000004202 carbamide Substances 0.000 description 1
- 239000001569 carbon dioxide Substances 0.000 description 1
- 229910002092 carbon dioxide Inorganic materials 0.000 description 1
- 239000001913 cellulose Substances 0.000 description 1
- 229920002678 cellulose Polymers 0.000 description 1
- 238000007385 chemical modification Methods 0.000 description 1
- 235000012000 cholesterol Nutrition 0.000 description 1
- 238000001816 cooling Methods 0.000 description 1
- 238000004132 cross linking Methods 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 229960002433 cysteine Drugs 0.000 description 1
- 238000000354 decomposition reaction Methods 0.000 description 1
- 238000002405 diagnostic procedure Methods 0.000 description 1
- XPPKVPWEQAFLFU-UHFFFAOYSA-J diphosphate(4-) Chemical compound [O-]P([O-])(=O)OP([O-])([O-])=O XPPKVPWEQAFLFU-UHFFFAOYSA-J 0.000 description 1
- 235000011180 diphosphates Nutrition 0.000 description 1
- 239000006185 dispersion Substances 0.000 description 1
- 238000000840 electrochemical analysis Methods 0.000 description 1
- 238000000835 electrochemical detection Methods 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 238000006345 epimerization reaction Methods 0.000 description 1
- 235000019441 ethanol Nutrition 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 230000005284 excitation Effects 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 238000013213 extrapolation Methods 0.000 description 1
- 238000001917 fluorescence detection Methods 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 235000001727 glucose Nutrition 0.000 description 1
- 229940116332 glucose oxidase Drugs 0.000 description 1
- 235000019420 glucose oxidase Nutrition 0.000 description 1
- 125000000291 glutamic acid group Chemical class N[C@@H](CCC(O)=O)C(=O)* 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 229960003180 glutathione Drugs 0.000 description 1
- 235000003969 glutathione Nutrition 0.000 description 1
- 235000011187 glycerol Nutrition 0.000 description 1
- 125000003630 glycyl group Chemical group [H]N([H])C([H])([H])C(*)=O 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 150000004820 halides Chemical class 0.000 description 1
- 125000005843 halogen group Chemical group 0.000 description 1
- FBPFZTCFMRRESA-UHFFFAOYSA-N hexane-1,2,3,4,5,6-hexol Chemical compound OCC(O)C(O)C(O)C(O)CO FBPFZTCFMRRESA-UHFFFAOYSA-N 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 125000001165 hydrophobic group Chemical group 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- 239000004310 lactic acid Substances 0.000 description 1
- 235000014655 lactic acid Nutrition 0.000 description 1
- 125000001909 leucine group Chemical group [H]N(*)C(C(*)=O)C([H])([H])C(C([H])([H])[H])C([H])([H])[H] 0.000 description 1
- 239000001630 malic acid Substances 0.000 description 1
- 235000011090 malic acid Nutrition 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 239000002207 metabolite Substances 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 229910052750 molybdenum Inorganic materials 0.000 description 1
- 239000011733 molybdenum Substances 0.000 description 1
- 238000012544 monitoring process Methods 0.000 description 1
- 230000002107 myocardial effect Effects 0.000 description 1
- KOOMFXGDLMRWSN-UHFFFAOYSA-N n-phenylnitrous amide Chemical class O=NNC1=CC=CC=C1 KOOMFXGDLMRWSN-UHFFFAOYSA-N 0.000 description 1
- 229960003966 nicotinamide Drugs 0.000 description 1
- 235000005152 nicotinamide Nutrition 0.000 description 1
- 239000011570 nicotinamide Substances 0.000 description 1
- 229940101270 nicotinamide adenine dinucleotide (nad) Drugs 0.000 description 1
- 235000016709 nutrition Nutrition 0.000 description 1
- 230000035764 nutrition Effects 0.000 description 1
- 239000001301 oxygen Substances 0.000 description 1
- 125000000636 p-nitrophenyl group Chemical group [H]C1=C([H])C(=C([H])C([H])=C1*)[N+]([O-])=O 0.000 description 1
- FJKROLUGYXJWQN-UHFFFAOYSA-N papa-hydroxy-benzoic acid Natural products OC(=O)C1=CC=C(O)C=C1 FJKROLUGYXJWQN-UHFFFAOYSA-N 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- QWFWWDPVTISWMX-UHFFFAOYSA-N phenazine-1-sulfonic acid Chemical compound C1(=CC=CC2=NC3=CC=CC=C3N=C12)S(=O)(=O)O QWFWWDPVTISWMX-UHFFFAOYSA-N 0.000 description 1
- 150000002988 phenazines Chemical class 0.000 description 1
- 229910052698 phosphorus Inorganic materials 0.000 description 1
- 239000011574 phosphorus Substances 0.000 description 1
- 210000002381 plasma Anatomy 0.000 description 1
- 229920003023 plastic Polymers 0.000 description 1
- 230000010287 polarization Effects 0.000 description 1
- 125000003367 polycyclic group Chemical group 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 239000001267 polyvinylpyrrolidone Substances 0.000 description 1
- 235000013855 polyvinylpyrrolidone Nutrition 0.000 description 1
- 229920000036 polyvinylpyrrolidone Polymers 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 108090000765 processed proteins & peptides Proteins 0.000 description 1
- 125000004076 pyridyl group Chemical group 0.000 description 1
- 229940107700 pyruvic acid Drugs 0.000 description 1
- 230000009257 reactivity Effects 0.000 description 1
- 238000010188 recombinant method Methods 0.000 description 1
- 238000006479 redox reaction Methods 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 238000011946 reduction process Methods 0.000 description 1
- 238000002310 reflectometry Methods 0.000 description 1
- 230000027756 respiratory electron transport chain Effects 0.000 description 1
- 238000012552 review Methods 0.000 description 1
- 229960004889 salicylic acid Drugs 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 239000002689 soil Substances 0.000 description 1
- 239000003381 stabilizer Substances 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 230000002195 synergetic effect Effects 0.000 description 1
- 150000003505 terpenes Chemical class 0.000 description 1
- 230000009466 transformation Effects 0.000 description 1
- 238000002834 transmittance Methods 0.000 description 1
- ITMCEJHCFYSIIV-UHFFFAOYSA-M triflate Chemical compound [O-]S(=O)(=O)C(F)(F)F ITMCEJHCFYSIIV-UHFFFAOYSA-M 0.000 description 1
- UFTFJSFQGQCHQW-UHFFFAOYSA-N triformin Chemical compound O=COCC(OC=O)COC=O UFTFJSFQGQCHQW-UHFFFAOYSA-N 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- 210000002700 urine Anatomy 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/0004—Oxidoreductases (1.)
- C12N9/0006—Oxidoreductases (1.) acting on CH-OH groups as donors (1.1)
-
- 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.)
- C12N9/0012—Oxidoreductases (1.) acting on nitrogen containing compounds as donors (1.4, 1.5, 1.6, 1.7)
-
- 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.)
- C12N9/0012—Oxidoreductases (1.) acting on nitrogen containing compounds as donors (1.4, 1.5, 1.6, 1.7)
- C12N9/0014—Oxidoreductases (1.) acting on nitrogen containing compounds as donors (1.4, 1.5, 1.6, 1.7) acting on the CH-NH2 group of donors (1.4)
- C12N9/0016—Oxidoreductases (1.) acting on nitrogen containing compounds as donors (1.4, 1.5, 1.6, 1.7) acting on the CH-NH2 group of donors (1.4) with NAD or NADP as acceptor (1.4.1)
-
- 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
- C12N9/96—Stabilising an enzyme by forming an adduct or a composition; Forming enzyme conjugates
-
- 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
- C12Q1/26—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving oxidoreductase
- C12Q1/32—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving oxidoreductase involving dehydrogenase
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y101/00—Oxidoreductases acting on the CH-OH group of donors (1.1)
- C12Y101/01—Oxidoreductases acting on the CH-OH group of donors (1.1) with NAD+ or NADP+ as acceptor (1.1.1)
- C12Y101/01001—Alcohol dehydrogenase (1.1.1.1)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y101/00—Oxidoreductases acting on the CH-OH group of donors (1.1)
- C12Y101/01—Oxidoreductases acting on the CH-OH group of donors (1.1) with NAD+ or NADP+ as acceptor (1.1.1)
- C12Y101/01006—Glycerol dehydrogenase (1.1.1.6)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y101/00—Oxidoreductases acting on the CH-OH group of donors (1.1)
- C12Y101/01—Oxidoreductases acting on the CH-OH group of donors (1.1) with NAD+ or NADP+ as acceptor (1.1.1)
- C12Y101/01027—L-Lactate dehydrogenase (1.1.1.27)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y101/00—Oxidoreductases acting on the CH-OH group of donors (1.1)
- C12Y101/01—Oxidoreductases acting on the CH-OH group of donors (1.1) with NAD+ or NADP+ as acceptor (1.1.1)
- C12Y101/01028—D-Lactate dehydrogenase (1.1.1.28)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y101/00—Oxidoreductases acting on the CH-OH group of donors (1.1)
- C12Y101/01—Oxidoreductases acting on the CH-OH group of donors (1.1) with NAD+ or NADP+ as acceptor (1.1.1)
- C12Y101/01037—Malate dehydrogenase (1.1.1.37)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y101/00—Oxidoreductases acting on the CH-OH group of donors (1.1)
- C12Y101/01—Oxidoreductases acting on the CH-OH group of donors (1.1) with NAD+ or NADP+ as acceptor (1.1.1)
- C12Y101/01047—Glucose 1-dehydrogenase (1.1.1.47)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y104/00—Oxidoreductases acting on the CH-NH2 group of donors (1.4)
- C12Y104/01—Oxidoreductases acting on the CH-NH2 group of donors (1.4) with NAD+ or NADP+ as acceptor (1.4.1)
- C12Y104/01005—L-Amino-acid dehydrogenase (1.4.1.5)
Landscapes
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Genetics & Genomics (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Biotechnology (AREA)
- Molecular Biology (AREA)
- Microbiology (AREA)
- Medicinal Chemistry (AREA)
- Biomedical Technology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Physics & Mathematics (AREA)
- Analytical Chemistry (AREA)
- Biophysics (AREA)
- Immunology (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Enzymes And Modification Thereof (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP08003054A EP2093284A1 (de) | 2008-02-19 | 2008-02-19 | Stabilisierung von Dehydrogenasen mit stabilen Coenzymen |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| TW200951222A TW200951222A (en) | 2009-12-16 |
| TWI482860B true TWI482860B (zh) | 2015-05-01 |
Family
ID=39768713
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| TW098105120A TWI482860B (zh) | 2008-02-19 | 2009-02-18 | 利用安定之輔酶使去氫酶安定之方法 |
Country Status (15)
| Country | Link |
|---|---|
| US (2) | US9896666B2 (enExample) |
| EP (2) | EP2093284A1 (enExample) |
| JP (2) | JP5758128B2 (enExample) |
| KR (3) | KR20120134142A (enExample) |
| CN (3) | CN104450659A (enExample) |
| AR (1) | AR070436A1 (enExample) |
| AU (1) | AU2009216908B9 (enExample) |
| BR (1) | BRPI0907839A2 (enExample) |
| CA (1) | CA2721718C (enExample) |
| HK (1) | HK1208703A1 (enExample) |
| MX (1) | MX2010008920A (enExample) |
| RU (1) | RU2499834C2 (enExample) |
| TW (1) | TWI482860B (enExample) |
| WO (1) | WO2009103540A1 (enExample) |
| ZA (1) | ZA201006638B (enExample) |
Families Citing this family (27)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP4786451B2 (ja) * | 2005-07-28 | 2011-10-05 | エフ ホフマン−ラ ロッシュ アクチェン ゲゼルシャフト | Ｎａｄ／ｎａｄｈの安定化 |
| EP2093284A1 (de) | 2008-02-19 | 2009-08-26 | F.Hoffmann-La Roche Ag | Stabilisierung von Dehydrogenasen mit stabilen Coenzymen |
| WO2010094632A1 (de) * | 2009-02-19 | 2010-08-26 | F. Hoffmann-La Roche Ag | Schnelle reaktionskinetik von enzymen mit niedriger aktivität in trockenen chemieschichten |
| CN102325496B (zh) | 2009-02-19 | 2015-10-07 | 霍夫曼-拉罗奇有限公司 | 分析辅助工具的节省空间的储存 |
| EP2398909B1 (de) | 2009-02-19 | 2015-07-22 | F. Hoffmann-La Roche AG | Schnelle reaktionskinetik von enzymen mit niedriger aktivität in trockenen chemieschichten |
| EP2226008A1 (de) | 2009-02-19 | 2010-09-08 | Roche Diagnostics GmbH | Verfahren zur Herstellung eines analytischen Magazins |
| EP2226007A1 (de) | 2009-02-19 | 2010-09-08 | Roche Diagnostics GmbH | Testelementmagazin mit abgedeckten Testfeldern |
| EP2292751A1 (de) * | 2009-08-20 | 2011-03-09 | Roche Diagnostics GmbH | Stabilisierung von Enzymen mit stabilen Coenzymen |
| JP5777633B2 (ja) * | 2009-12-16 | 2015-09-09 | エフ ホフマン−ラ ロッシュ アクチェン ゲゼルシャフト | 保護された分析物の制御された放出によるテストエレメントにおける酵素の分解の検出 |
| EP2636750A1 (en) * | 2012-03-06 | 2013-09-11 | Roche Diagniostics GmbH | Compatible solute ectoine as well as derivatives thereof for enzyme stabilization |
| CA2872215C (en) | 2012-06-22 | 2018-03-13 | F. Hoffmann-La Roche Ag | Method and device for detecting an analyte in a body fluid |
| US8920628B2 (en) | 2012-11-02 | 2014-12-30 | Roche Diagnostics Operations, Inc. | Systems and methods for multiple analyte analysis |
| US8921061B2 (en) | 2012-11-02 | 2014-12-30 | Roche Diagnostics Operations, Inc. | Reagent materials and associated test elements |
| WO2014096174A1 (en) | 2012-12-20 | 2014-06-26 | Roche Diagnostics Gmbh | Method for evaluating medical measurement curves |
| CN104854457B (zh) | 2012-12-20 | 2016-09-14 | 霍夫曼-拉罗奇有限公司 | 用于分析体液样本的方法 |
| EP2781919A1 (en) | 2013-03-19 | 2014-09-24 | Roche Diagniostics GmbH | Method / device for generating a corrected value of an analyte concentration in a sample of a body fluid |
| WO2014180939A1 (en) | 2013-05-08 | 2014-11-13 | Roche Diagnostics Gmbh | Stabilization of enzymes by nicotinic acid |
| JP2016528175A (ja) * | 2013-06-04 | 2016-09-15 | エフ．ホフマン−ラ ロシュ アーゲーＦ． Ｈｏｆｆｍａｎｎ−Ｌａ Ｒｏｃｈｅ Ａｋｔｉｅｎｇｅｓｅｌｌｓｃｈａｆｔ | Ｆｒｅｔに有用な新規化合物およびそれに関連する方法 |
| WO2015063025A1 (en) | 2013-10-29 | 2015-05-07 | F. Hoffmann-La Roche Ag | Nano-enzyme containers for test elements |
| WO2015078899A1 (en) | 2013-11-27 | 2015-06-04 | Roche Diagnostics Gmbh | Composition comprising up-converting phosphors for detecting an analyte |
| EP2927319A1 (en) | 2014-03-31 | 2015-10-07 | Roche Diagnostics GmbH | High load enzyme immobilization by crosslinking |
| JP6522003B2 (ja) | 2014-04-14 | 2019-05-29 | エフ．ホフマン−ラ ロシュ アーゲーＦ． Ｈｏｆｆｍａｎｎ−Ｌａ Ｒｏｃｈｅ Ａｋｔｉｅｎｇｅｓｅｌｌｓｃｈａｆｔ | フェナジニウムメディエーター |
| EP3757096B1 (en) | 2014-08-22 | 2025-03-12 | Roche Diagnostics GmbH | Redoxindicators for a use in cell viability testing |
| CN107779459B (zh) * | 2016-08-31 | 2021-06-08 | 安琪酵母股份有限公司 | 葡萄糖脱氢酶dna分子、载体和菌株及应用 |
| CA3035874C (en) | 2016-10-05 | 2025-09-09 | F. Hoffmann-La Roche Ag | DETECTION REAGENTS AND ELECTRODE ARRANGEMENTS FOR MULTI-ANALYTICAL DIAGNOSTIC TEST ELEMENTS, AS WELL AS THEIR METHODS OF USE |
| EP3339431A1 (en) | 2016-12-22 | 2018-06-27 | Roche Diabetes Care GmbH | Glucose dehydrogenase variants with improved properties |
| HUE064713T2 (hu) | 2018-02-28 | 2024-04-28 | Hoffmann La Roche | Biokompatibilitási bevonat folyamatos analitméréshez |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2001049247A2 (en) * | 1999-12-30 | 2001-07-12 | Specialty Assays, Inc. | Assays for analytes and enzymes practiced in the presence of nad and nadp analogues, and related assay kits |
| WO2007012494A1 (de) * | 2005-07-28 | 2007-02-01 | F.Hoffmann-La Roche Ag | Stabile nad/nadh-derivate |
Family Cites Families (14)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| SU1043568A1 (ru) * | 1981-06-11 | 1983-09-23 | Московский Ордена Ленина,Ордена Октябрьской Революции И Ордена Трудового Красного Знамени Государственный Университет Им.М.В.Ломоносова | Способ определени активности дегидрогеназ крови |
| DE19543493A1 (de) * | 1995-11-22 | 1997-05-28 | Boehringer Mannheim Gmbh | Stabilisierte Coenzym-Lösungen und deren Verwendung zur Bestimmung von Dehydrogenasen bzw. deren Substrate im alkalischen Milieu |
| US5801006A (en) | 1997-02-04 | 1998-09-01 | Specialty Assays, Inc. | Use of NADPH and NADH analogs in the measurement of enzyme activities and metabolites |
| WO2001094370A1 (en) | 2000-06-07 | 2001-12-13 | Wako Pure Chemical Industries, Ltd. | Coenzyme derivatives and enzymes appropriate therefor |
| WO2002036779A1 (fr) | 2000-10-31 | 2002-05-10 | Koji Sode | Nouvelle glucose deshydrogenase et procede de production de la deshydrogenase |
| JP2003310274A (ja) * | 2002-04-30 | 2003-11-05 | Amano Enzyme Inc | グルコース脱水素酵素およびそれをコードする遺伝子 |
| AU2003240260B2 (en) | 2002-05-16 | 2008-05-22 | F. Hoffmann-La Roche Ag | Method and reagent system having a non-regenerative enzyme-coenzyme complex |
| EP1660648B1 (en) | 2003-08-11 | 2013-10-09 | Codexis, Inc. | Improved glucose dehydrogenase polypeptides and related polynucleotides |
| PT2705792E (pt) | 2004-03-06 | 2015-07-07 | Hoffmann La Roche | Dispositivo de amostragem de fluido corporal |
| US7172890B2 (en) * | 2004-10-28 | 2007-02-06 | Roche Diagnostics Gmbh | Inactivated enzyme variants and associated process and reagent system |
| JP4786451B2 (ja) | 2005-07-28 | 2011-10-05 | エフ ホフマン−ラ ロッシュ アクチェン ゲゼルシャフト | Ｎａｄ／ｎａｄｈの安定化 |
| EP2093284A1 (de) * | 2008-02-19 | 2009-08-26 | F.Hoffmann-La Roche Ag | Stabilisierung von Dehydrogenasen mit stabilen Coenzymen |
| US20110313009A1 (en) | 2008-07-17 | 2011-12-22 | Horizon Pharma Usa, Inc. | Nsaid dose unit formulations with h2-receptor antagonists and methods of use |
| EP2398909B1 (de) | 2009-02-19 | 2015-07-22 | F. Hoffmann-La Roche AG | Schnelle reaktionskinetik von enzymen mit niedriger aktivität in trockenen chemieschichten |
-
2008
- 2008-02-19 EP EP08003054A patent/EP2093284A1/de not_active Ceased
-
2009
- 2009-02-18 TW TW098105120A patent/TWI482860B/zh not_active IP Right Cessation
- 2009-02-19 KR KR1020127027270A patent/KR20120134142A/ko not_active Ceased
- 2009-02-19 AR ARP090100571A patent/AR070436A1/es not_active Application Discontinuation
- 2009-02-19 CN CN201410680334.8A patent/CN104450659A/zh active Pending
- 2009-02-19 BR BRPI0907839-8A patent/BRPI0907839A2/pt not_active Application Discontinuation
- 2009-02-19 EP EP09712033.1A patent/EP2245152B1/de active Active
- 2009-02-19 WO PCT/EP2009/001206 patent/WO2009103540A1/de not_active Ceased
- 2009-02-19 JP JP2010547110A patent/JP5758128B2/ja not_active Expired - Fee Related
- 2009-02-19 RU RU2010138610/10A patent/RU2499834C2/ru not_active IP Right Cessation
- 2009-02-19 CA CA2721718A patent/CA2721718C/en not_active Expired - Fee Related
- 2009-02-19 AU AU2009216908A patent/AU2009216908B9/en not_active Revoked
- 2009-02-19 KR KR1020107020894A patent/KR101381004B1/ko not_active Expired - Fee Related
- 2009-02-19 KR KR1020137013118A patent/KR20130081300A/ko not_active Withdrawn
- 2009-02-19 CN CN200980105640.6A patent/CN101945999B/zh not_active Expired - Fee Related
- 2009-02-19 MX MX2010008920A patent/MX2010008920A/es active IP Right Grant
-
2010
- 2010-02-12 CN CN2010800085457A patent/CN102325896A/zh active Pending
- 2010-02-12 JP JP2011550531A patent/JP6113405B2/ja not_active Expired - Fee Related
- 2010-08-19 US US12/859,654 patent/US9896666B2/en active Active
- 2010-09-16 ZA ZA2010/06638A patent/ZA201006638B/en unknown
-
2015
- 2015-09-23 HK HK15109305.4A patent/HK1208703A1/xx unknown
-
2018
- 2018-01-11 US US15/868,055 patent/US11220674B2/en active Active
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2001049247A2 (en) * | 1999-12-30 | 2001-07-12 | Specialty Assays, Inc. | Assays for analytes and enzymes practiced in the presence of nad and nadp analogues, and related assay kits |
| WO2007012494A1 (de) * | 2005-07-28 | 2007-02-01 | F.Hoffmann-La Roche Ag | Stabile nad/nadh-derivate |
Non-Patent Citations (2)
| Title |
|---|
| Min-Hung Liao & Dong-Hwang Chen, "Characteristics of magnetic nanoparticles-bound YADH in water/AOT/isooctane microemulsions.", J. Molecul. Catal. B: Enzymatics, 13 Sep. 2002, Vol.18 Issue 1-3, page 81-87 * |
| T. Nagao, et al., "Stability-increasing mutants of glucose dehydrogenase.", FEBS Letters, Aug. 1989, Vol.253, Number 1,2, page 113-116 * |
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| TWI482860B (zh) | 利用安定之輔酶使去氫酶安定之方法 | |
| JP5851401B2 (ja) | 安定な補酵素による酵素の安定化 | |
| CA2750474C (en) | Fast reaction kinetics of enzymes having low activity in dry chemistry layers | |
| AU2012203453B2 (en) | Stabilization of dehydrogenases using stable coenzymes | |
| US6884416B2 (en) | Stable PQQ-dependent glucose dehydrogenase composition | |
| HK1152728A (en) | Stabilization of dehydrogenases using stable coenzymes | |
| HK1152728B (en) | Stabilization of dehydrogenases using stable coenzymes | |
| NZ587397A (en) | Stabilization of dehydrogenases using stable chemically modified coenzymes | |
| HK1170770A (en) | Stabilization of enzymes using stable coenzymes | |
| HK1170770B (en) | Stabilization of enzymes using stable coenzymes | |
| HK1166353A (en) | Fast reaction kinetics of enzymes having low activity in dry chemistry layers |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| MM4A | Annulment or lapse of patent due to non-payment of fees |