about
Glutathione reductase from germinated peasThe ALD6 gene of Saccharomyces cerevisiae encodes a cytosolic, Mg(2+)-activated acetaldehyde dehydrogenase.Modification of pig M4 lactate dehydrogenase by pyridoxal 5'-phosphate. Demonstration of an essential lysine residueAlkyl-dihydroxyacetonephosphate synthase. Presence and role of flavin adenine dinucleotideQuenching of alkaline phosphatase phosphorescence by O2 and NO. Evidence for inflexible regions of protein structureCloned Drosophila alcohol dehydrogenase genes are correctly expressed after transfection into Drosophila cells in culture.The interpretation of kinetic data for enzyme-catalysed reactions involving three substrates.The role of an essential histidine residue of yeast alcohol dehydrogenase.Kinetic studies of dogfish liver glutamate dehydrogenaseThe specificities and configurations of ternary complexes of yeast and liver alcohol dehydrogenases.Glycerol kinase activities in rat heart and adipose tissue.The inhibition of skeletal-muscle fructose 1,6-diphosphatase by adenosine monophosphate.The purification and properties of 6-phosphogluconate dehydrogenase from sheep liver.A study of the oxidation of butan-1-ol and propan-2-ol by nicotinamide-adenine dinucleotide catalysed by yeast alcohol dehydrogenase.Horse liver alcohol dehydrogenase. A study of the essential lysine residue.Reversible modification of pig heart mitochondrial malate dehydrogenase by pyridoxal 5'-phosphate.Some properties of an alcohol dehydrogenase partially purified from baker's yeast grown without added zinc.Some properties of aldehyde dehydrogenase from sheep liver mitochondria.Estimation of rate and dissociation constants involving ternary complexes in reactions catalysed by yeast alcohol dehydrogenase.The kinetic mechanism of ox liver glutamate dehydrogenase in the presence of the allosteric effector ADP. The oxidative deamination of L-glutamate.A study of the kinetics and mechanism of yeast alcohol dehydrogenase with a variety of substrates.Purification and properties of 6-phosphogluconate dehydrogenase from sheep liver.Is pyridoxal 5'-phosphate an affinity label for phosphate-binding sites in proteins?: The case of bovine glutamate dehydrogenase.The binding of dihydronicotinamide--adenine dinucleotide and pyridine-3-aldehyde--adenine dinucleotide by yeast alcohol dehydrogenase.The mechanisms of reductive carboxylation reactions. Carbon dioxide or bicarbonate as substrate of nicotinamide-adenine dinucleotide phosphate-linked isocitrate dehydrogenase and malic enzyme.The separation of sheep liver cytoplasmic and mitochondrial aldehyde dehydrogenases by isoelectric focusing, and observations on the purity of preparations of the cytoplasmic enzyme, and their sensitivity towards inhibition by disulfiram.The nature of the carbon dioxide substrate and equilibrium constant of the 6-phosphogluconate dehydrogenase reactionEffect of disulfiram on the pre-steady-state burst in the reactions of sheep liver cytoplasmic aldehyde dehydrogenase.The AdhS alleloenzyme of alcohol dehydrogenase from Drosophila melanogaster. Variation of kinetic parameters with pHThe equilibrium position of the reaction of bovine liver glutamate dehydrogenase with pyridoxal5'-phosphate. A demonstration that covalent modification with this reagent completely abolishes catalytic activityThe purification and some properties of the Mg(2+)-activated cytosolic aldehyde dehydrogenase of Saccharomyces cerevisiae.Protection of glutamate dehydrogenase by nicotinamide-adenine dinucleotide against reversible inactivation by pyridoxal 5'-phosphate as a sensitive indicator of conformational change induced by substrates and substrate analogues.The coenzyme-binding characteristics of highly purified preparations of sheep liver cytoplasmic aldehyde dehydrogenaseThe effects of starvation and alloxan-diabetes on the contents of citrate and other metabolic intermediates in rat liver.A pH-dependent activation-inactivation equilibrium in glutamate dehydrogenase of Clostridium symbiosum.Kinetic studies of the mechanism of pig kidney aldehyde reductase.Purification and properties of rabbit muscle L-glycerol 3-phosphate dehydrogenaseTHE ACTIVITY OF LIVER ALCOHOL DEHYDROGENASE WITH NICOTINAMIDE-ADENINE DINUCLEOTIDE PHOSPHATE AS COENZYME.Some observations on the preparation and properties of dihydronicotinamide-adenine dinucleotide.A study of the coenzyme-binding characteristics of rabbit muscle L-glycerol 3-phosphate dehydrogenase.
P2860
Q24532145-8AA7A823-394B-4DBC-896C-95B49D20495BQ27933408-3C019E4E-6345-45A5-AD3F-325B18D1F9B0Q28341607-C0BF9663-46AA-47F2-B6CC-B6B28CE801BDQ28371785-9FA1910F-9053-46A5-AD85-17F8B4494F56Q30404341-37BB3CD9-6FC8-432E-B959-25BDD9786013Q36255372-9A259578-CC59-4A7A-81FF-25749A6D81DDQ36575263-8471F5C7-F0A5-418A-9A0E-921ED3F71D7BQ39159266-9162E3DC-D8F0-4DB7-B616-5B7EBD3AE86EQ39246368-127AEE0B-ADDD-44E3-8906-35B864B8B156Q39273959-C8240A95-EBEB-4C6E-A834-091FB5A53FC7Q39275008-FB78580D-6E9C-46AE-935D-FF08FAEEDCD3Q39275560-737A2079-FC3D-4E6B-8ED7-EB10843B0F6EQ39301736-1F98CBF2-46D0-4900-9CEA-AF194C0CB08FQ39955775-E5BCD1F8-1592-4A48-A896-0D83D41C6C6DQ39966573-7B8ED40B-CCE4-4525-A603-B3FD633CE9E3Q39977618-E39A12D8-EE5F-4F33-BD58-D184937FF3A3Q39993822-874D154C-DD69-4EE7-B36D-9E683C80F6B6Q40077265-35E2D8A4-C6E7-4FB4-B835-45C42FBE9284Q40156912-FEAA800C-FD28-4838-B5E6-F05ACDAE9159Q41821061-D5450762-B7C1-453B-8272-7EABC1A9035EQ41821553-D30BAB75-49D2-4728-B805-37F4CD43E3A0Q41826416-E13EAB5D-08AF-454C-A984-85CA7542F6CBQ41842424-F5A7A274-370A-43F2-AEED-BAC4BF9163AFQ41847017-A6809083-014A-43F0-997E-B8F6542A9FA3Q41863504-F71DD628-96DE-4648-8A03-430811928D7CQ41884062-89F97622-60D5-4248-B6C4-3D1BBB6EBD5CQ41897087-7355E21F-08C1-47DC-9B7E-54D425EF0955Q41917374-78DC0C8A-BFEA-40F6-94A4-BAA49FFCF8FEQ41940703-5A5ED475-D9D6-4B3D-A17B-0FFD996CEF56Q41964880-D8E413C4-B318-492B-8A8B-926030542224Q41998162-A00E8535-48B3-4B6F-B99A-64D7049336BCQ42104198-7127DD1C-0ED7-4623-A558-907EB855728EQ42148887-6643C116-DD54-4B18-8445-3A03E38A5EAAQ42173732-9F9D71D5-B3DD-4FC6-AC98-B6B7435026C0Q42181034-97EFF8DA-975F-45AF-887B-E433E23E47A5Q42246484-22E29E3F-9E3F-4FF2-B9BD-C5436E3804C9Q42253340-91F108A0-553C-4439-8A64-E9DD82DDFE27Q42274091-7B76BBCD-774D-4533-8FD2-B824C0D427FAQ42553887-45154979-A342-4CE6-A5A0-D000C5B6DAEAQ42584833-3F6EDE7C-4000-486B-A1D0-8818AAD4C5B1
P2860
description
1962 nî lūn-bûn
@nan
1962年の論文
@ja
1962年論文
@yue
1962年論文
@zh-hant
1962年論文
@zh-hk
1962年論文
@zh-mo
1962年論文
@zh-tw
1962年论文
@wuu
1962年论文
@zh
1962年论文
@zh-cn
name
Kinetic studies of liver alcohol dehydrogenase.
@en
Kinetic studies of liver alcohol dehydrogenase.
@nl
type
label
Kinetic studies of liver alcohol dehydrogenase.
@en
Kinetic studies of liver alcohol dehydrogenase.
@nl
prefLabel
Kinetic studies of liver alcohol dehydrogenase.
@en
Kinetic studies of liver alcohol dehydrogenase.
@nl
P2860
P356
P1433
P1476
Kinetic studies of liver alcohol dehydrogenase.
@en
P2093
P2860
P304
P356
10.1042/BJ0840244
P407
P577
1962-08-01T00:00:00Z