Mechanism of inactivation of sheep liver cytoplasmic aldehyde dehydrogenase by disulfiram
Trevor M. Kitson
Abstract
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Trevor M. Kitson
Abstract
Open-access reader
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.
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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.
Key concepts: Disulfiram, Aldehyde dehydrogenase, Aldehyde, Enzyme, ALDH2, Chemistry, Biochemistry, Cytoplasm