Mechanism of inactivation of sheep liver cytoplasmic aldehyde dehydrogenase by disulfiram
- 1 August 1983
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 213 (2) , 551-554
- https://doi.org/10.1042/bj2130551
Abstract
Stoicheiometric amounts of [14C]disulfiram react rapidly with sheep liver cytoplasmic aldehyde dehydrogenase to give loss of catalytic activity and incorporation of the expected amount of radioactivity. In a subsequent slower reaction the label is lost from the enzyme without re-emergence of enzymic activity. The results imply that in vivo disulfiram may act as an oxidation-reduction catalyst for the inactivation of aldehyde dehydrogenase.Keywords
This publication has 16 references indexed in Scilit:
- Human Aldehyde Dehydrogenase: Mechanism of Inhibition of DisulfiramScience, 1982
- 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 disulfiramBiochemical Journal, 1981
- The inactivation of aldehyde dehydrogenase by disulfiram in the presence of glutathioneBiochemical Journal, 1981
- Purification and Properties of Sheep‐Liver Aldehyde DehydrogenasesEuropean Journal of Biochemistry, 1979
- Studies on the interaction between disulfiram and sheep liver cytoplasmic aldehyde dehydrogenaseBiochemical Journal, 1978
- The disulfiram--ethanol reaction: a review.Journal of Studies on Alcohol, 1977
- ENZYMATIC OXIDATION OF DIETHYLDITHIOCARBAMATE BY XANTHINE OXIDASE AND ITS COLORIMETRIC ASSAY*Annals of the New York Academy of Sciences, 1976
- The effect of disulfiram on the aldehyde dehydrogenases of sheep liverBiochemical Journal, 1975
- Methaemoglobin formation induced by thiolsBiochemical Pharmacology, 1963
- Inhibitory action of dithiocarbamates on enzymes of animal tissuesToxicology and Applied Pharmacology, 1961