Purification and Characterization of Aldehyde Dehydrogenase from Bovine Liver
- 1 February 1978
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 83 (1) , 189-196
- https://doi.org/10.1111/j.1432-1033.1978.tb12083.x
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.This publication has 20 references indexed in Scilit:
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