Purification and partial characterization of aldehyde dehydrogenase from human erythrocytes

Biochim Biophys Acta. 1979 Aug 15;569(2):117-23. doi: 10.1016/0005-2744(79)90046-9.


Human erythrocyte aldehyde dehydrogenase (aldehyde:NAD+ oxidoreductase, EC 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

  • Aldehyde Oxidoreductases / antagonists & inhibitors
  • Aldehyde Oxidoreductases / blood
  • Aldehyde Oxidoreductases / isolation & purification*
  • Aldehydes / pharmacology
  • Chloral Hydrate / pharmacology
  • Disulfiram / pharmacology
  • Erythrocytes / enzymology*
  • Humans
  • Kinetics
  • Male
  • Molecular Weight
  • NAD / metabolism
  • Substrate Specificity


  • Aldehydes
  • NAD
  • Chloral Hydrate
  • Aldehyde Oxidoreductases
  • Disulfiram