Some properties of aldehyde dehydrogenase from sheep liver mitochondria.
Aldehyde dehydrogenase from sheep liver mitochondria was purified to homogeneity as judged by electrophoresis on polyacrylamide gels, and by sedimentation-equilibrium experiments in the analytical ultracentrifuge. The enzyme has a molecular weight of 198000 and a subunit size of 48000, indicating that the molecule is a tetramer. Fluorescence and spectrophotometric titrations indicate that each subunit can bind 1 molecule of NADH. Enzymic activity is completely blocked by reaction of 4mol of 5,5'-dithiobis-(2-nitrobenzoate)/mol of enzyme. Excess of disulfiram or iodoacetamide decreases activity to only 50% of the control value, and only two thiol groups per molecule are apparently modified by these reagents.
D000445:Aldehyde Oxidoreductases / Q000032:analysis* / Q000037:antagonists & inhibitors; D000818:Animals; D008930:Mitochondria, Liver / Q000201:enzymology*; D008970:Molecular Weight; D009243:NAD / Q000378:metabolism; D012756:Sheep; D015032:Zinc / Q000032:analysis
D009243:NAD; D000445:Aldehyde Oxidoreductases; D015032:Zinc