The use of pH-gradient ion-exchange chromatography to separate sheep liver cytoplasmic aldehyde dehydrogenase from mitochondrial enzyme contamination, and observations on the interaction between the pure cytoplasmic enzyme and disulfiram
about
The binding of NADH to cytoplasmic aldehyde dehydrogenase after modification with p-nitrophenyl dimethylcarbamateAldehyde dehydrogenase catalyses acetaldehyde formation from 4-nitrophenyl acetate and NADHThe activation of aldehyde dehydrogenase by diethylstilboestrol and 2,2'-dithiodipyridine.Effects of Mg2+, Ca2+ and Mn2+ on sheep liver cytoplasmic aldehyde dehydrogenase.Effect of disulfiram on the pre-steady-state burst in the reactions of sheep liver cytoplasmic aldehyde dehydrogenase.The purification and some properties of the Mg(2+)-activated cytosolic aldehyde dehydrogenase of Saccharomyces cerevisiae.High concentrations of aldehydes slow the reaction of cytoplasmic aldehyde dehydrogenase with thiol-group modifiers.Identification of a catalytically essential nucleophilic residue in sheep liver cytoplasmic aldehyde dehydrogenase.The coenzyme-binding characteristics of highly purified preparations of sheep liver cytoplasmic aldehyde dehydrogenaseThe effects of Mg2+ on certain steps in the mechanisms of the dehydrogenase and esterase reactions catalysed by sheep liver aldehyde dehydrogenase. Support for the view that dehydrogenase and esterase activities occur at the same site on the enzyme.Cellular distribution and properties of human blood aldehyde dehydrogenase.Kinetic properties of highly purified preparations of sheep liver cytoplasmic aldehyde dehydrogenase.Correlation of loss of activity of human aldehyde dehydrogenase with reaction of bromoacetophenone with glutamic acid-268 and cysteine-302 residues. Partial-sites reactivity of aldehyde dehydrogenaseStudies on the unusual behaviour of bovine liver UDP-glucose dehydrogenase in assays at acid and neutral pH and on the presence of tightly bound nucleotide material in purified preparations of this enzyme.Kinetics of p-nitrophenyl pivalate hydrolysis catalysed by cytoplasmic aldehyde dehydrogenase.The removal of cytosolic-type aldehyde dehydrogenase from preparations of sheep liver mitochondrial aldehyde dehydrogenase and the unusual properties of the purified mitochondrial enzyme in assays.Studies on the mechanism of sheep liver cytosolic aldehyde dehydrogenase.Studies on the mechanism of sheep liver cytosolic aldehyde dehydrogenase. The effect of pH on the aldehyde binding reactions and a re-examination of the problem of the site of proton release in the mechanism.Inactivation of horse liver mitochondrial aldehyde dehydrogenase by disulfiram. Evidence that disulfiram is not an active-site-directed reagent.Effect of some thiocarbamate compounds on aldehyde dehydrogenase and implications for the disulfiram ethanol reaction.Mechanism of inactivation of sheep liver cytoplasmic aldehyde dehydrogenase by disulfiram.Bovine lens aldehyde dehydrogenase. Kinetics and mechanism.Further studies of the action of disulfiram and 2,2'-dithiodipyridine on the dehydrogenase and esterase activities of sheep liver cytoplasmic aldehyde dehydrogenase.Studies of the esterase activity of cytosolic aldehyde dehydrogenase with resorufin acetate as substrate.Overview of the role of alcohol dehydrogenase and aldehyde dehydrogenase and their variants in the genesis of alcohol-related pathology
P2860
Q28360132-C8C91963-6994-4D08-B74C-6D707E1AC5DCQ28362174-281FCCDB-53F0-4A9C-9D5A-9CE9FA1F0AD0Q41833394-13713BAB-4AE7-437F-A070-F10EE1576EF5Q41870190-E6E81FD6-95EB-4E91-BEED-5778B6BE689FQ41917374-8A6B204D-13D9-4BFA-8B02-556AEECAC64BQ41998162-3E306F34-FA68-4E9D-B6A7-501FA31FCED4Q42005010-39B1255A-5DD8-4B14-BBFB-FDCC7ADEF07BQ42112633-D5CB21D5-08B9-413C-BC9E-935701F33133Q42148887-9BCA477A-F4DA-4779-97C4-6EF5CB3EFFD6Q42161493-53BF66DD-1473-4913-815D-3B61E8A9D069Q42216994-DF752188-1D71-4BB1-8B1F-47DB09AE596EQ42584860-B0B18FEC-6AB9-4703-AABB-B1389638EB6EQ42793662-BCD35BEA-B34C-45A0-BC0F-D10839A5876CQ42819043-5AD7F349-AED4-4AEA-A88E-E13A7FC7715DQ42821200-D7A2E31C-9438-414C-9BD0-8B83F288B30BQ42848436-C622C566-9318-4163-9F67-AB9412CEB1EEQ42848784-4B2C617B-F84D-45B5-BA44-D80DCA4BFE56Q42854322-B98720A4-B0CF-4CC8-94A5-C6FCEFBC3937Q42855550-365BA498-BCAB-4D36-B7E9-FFCC3C6F10D8Q42862586-4D11EE1B-B381-434E-86DF-4CB232B0D9AFQ42864578-EE8B91D7-1412-4DCB-94AA-A6DCC063AAC6Q42865564-F63AAE4C-D07A-4A0D-AD54-79E23546AF93Q42874760-16136F39-C5BB-45FA-A115-9CF441F6FD79Q42985895-3C33FF22-E597-4B0B-9468-293F36C70D1BQ56866441-389B5646-F1B9-4D04-B8AB-D4E82ECC6690
P2860
The use of pH-gradient ion-exchange chromatography to separate sheep liver cytoplasmic aldehyde dehydrogenase from mitochondrial enzyme contamination, and observations on the interaction between the pure cytoplasmic enzyme and disulfiram
description
1981 nî lūn-bûn
@nan
1981年の論文
@ja
1981年論文
@yue
1981年論文
@zh-hant
1981年論文
@zh-hk
1981年論文
@zh-mo
1981年論文
@zh-tw
1981年论文
@wuu
1981年论文
@zh
1981年论文
@zh-cn
name
The use of pH-gradient ion-exc ...... oplasmic enzyme and disulfiram
@en
type
label
The use of pH-gradient ion-exc ...... oplasmic enzyme and disulfiram
@en
prefLabel
The use of pH-gradient ion-exc ...... oplasmic enzyme and disulfiram
@en
P2093
P2860
P356
P1433
P1476
The use of pH-gradient ion-exc ...... oplasmic enzyme and disulfiram
@en
P2093
P2860
P304
P356
10.1042/BJ1990573
P407
P577
1981-12-01T00:00:00Z