Purification and Characterization of Aldehyde Dehydrogenase from Bovine Liver

Abstract

Aldehyde dehydrogenase [EC 1.2.1.3] from bovine liver was purified to homogeneity. Amino acid composition showed a high content of cysteine of 32 mol/mol enzyme. The enzyme is composed of 4 identical subunits as judged by sodium dodecyl sulfate gel electrophoresis and end-group analysis. The MW was determined to be 220,000 .+-. 10,000 by sedimentation equilibrium analysis in an analytical ultracentrifuge. The Km for NAD+, glyceraldehyde and acetaldehyde were found to be 47 .mu.M, 170 .mu.M and 130 .mu.M, respectively.