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Disulfiram labeled with carbon-14 reacts specifically with human liver aldehyde dehydrogenase E1 with loss of catalytic activity and no incorporation of label. Carbon-14-labeled diethyldithiocarbamate is formed and the number of enzyme sulfhydryl groups decreases from 34 to 30 during this process. Activity is recovered by-mercaptoethanol but not by(More)
Three human post-mortem brains were dissected into seventeen areas and assayed for aldehyde dehydrogenase (EC activity employing two assay systems: one at 68 microM and another at 13.6 mM propionaldehyde. The levels of activity with 68 microM propionaldehyde were significantly higher in cerebellum and putamen. The same brain areas were also(More)
The histamine H2-receptor antagonists have been identified as inhibitors of human liver aldehyde dehydrogenase (EC isozymes, E1, E2, and E3. Inhibition was strongest with the E3 isozyme, whose substrates include gamma-aminobutyraldehyde, the aldehyde metabolites of polyamines, and betaine aldehyde. Burimamide, metiamide, cimetidine guanidine,(More)
Two equivalents of symmetrically labeled [14C]-disulfiram (tetraethylthiuram disulfide, Antabuse) interact with human liver cytoplasmic aldehyde dehydrogenase (ALDH) E1 (E.C. inhibiting ca. 90% of total catalytic activity. Inhibition occurs without labeling of the enzyme but is associated with disappearance of four SH groups per molecule of enzyme.(More)
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