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Title: Purification and characterization of aldehyde dehydrogenase from bovine liver. Author: Leicht W, Heinz F, Freimüller B. Journal: Eur J Biochem; 1978 Feb 01; 83(1):189-96. PubMed ID: 627210. Abstract: 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.[Abstract] [Full Text] [Related] [New Search]