Purification and characterization of aldehyde dehydrogenase from bovine liver

Eur J Biochem. 1978 Feb 1;83(1):189-96. doi: 10.1111/j.1432-1033.1978.tb12083.x.


Aldehyde dehydrogenase from bovine liver has been purified to homogeneity. Amino acid composition showed a high content of cysteine of 32 mol/mol enzyme. The enzyme is composed of four identical subunits as judged by sodium dodecyl sulfate gel electrophoresis and end-group analysis. The molecular weight was determined to be 220 000 +/- 10 000 by sedimentation equilibrium analysis in an analytical ultracentrifuge. The Michaelis constants for NAD+, glyceraldehyde and acetaldehyde were found to be 47 micron, 170 micron and 130 micron, respectively.

MeSH terms

  • Aldehyde Oxidoreductases* / isolation & purification
  • Aldehyde Oxidoreductases* / metabolism
  • Amino Acids / analysis
  • Animals
  • Cattle
  • Kinetics
  • Liver / enzymology*
  • Macromolecular Substances
  • Molecular Weight
  • Spectrophotometry, Ultraviolet


  • Amino Acids
  • Macromolecular Substances
  • Aldehyde Oxidoreductases