title: Purification and partial characterization of aldehyde dehydrogenase from human erythrocytes.
abstract: Human erythrocyte aldehyde dehydrogenase (aldehyde:NAD+ oxidoreductase, EC 1.2.1.3) was purified to apparent homogeneity. The native enzyme has a molecular weight of about 210,000 as determined by gel filtration, and SDS-polyacrylamide gel electrophoresis of this enzyme yields a single protein and with a molecular weight of 51,500, suggesting that the native enzyme may be a tetramer. The enzyme has a relatively low Km for NAD (15 microM) and a high sensitivity to disulfiram. Disulfiram inhibits the enzyme activity rapidly and this inhibition is apparently of a non-competitive nature. In kinetic characteristic and sensitivity to disulfiram, erythrocyte aldehyde dehydrogenase closely resembles the cytosolic aldehyde dehydrogenase found in the liver of various species of mammalians.
mesh_terms: D000445:Aldehyde Oxidoreductases / Q000037:antagonists & inhibitors / Q000097:blood / Q000302:isolation & purification*; D000447:Aldehydes / Q000494:pharmacology; D002697:Chloral Hydrate / Q000494:pharmacology; D004221:Disulfiram / Q000494:pharmacology; D004912:Erythrocytes / Q000201:enzymology*; D006801:Humans; D007700:Kinetics; D008297:Male; D008970:Molecular Weight; D009243:NAD / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D000447:Aldehydes; D009243:NAD; D002697:Chloral Hydrate; D000445:Aldehyde Oxidoreductases; D004221:Disulfiram