Brain Aldehyde Dehydrogenase

Brain aldehyde dehydrogenase. Localization, purification, and properties.

Horse Liver Aldehyde Dehydrogenase

Horse liver aldehyde: NAD oxidoreductase (EC 1.2.1.3) has been purified to homogeneity by a procedure consisting of salt fractionation, ion exchange chromatography, and isoelectric focusing. The purif?ed material has a turnover number of 1.85 pmoles of NADH per min per mg of protein when assayed at pH 9.0 with propionaldehyde as substrate. Values obtained for the molecular weight of the native ...

Human Liver Aldehyde Dehydrogenase

Human liver aldehyde dehydrogenase has been found to be capable of hydrolyzing p-nitrophenyl esters. Esterase and dehydrogenase activities exhibited identical ion exchange and affinity properties, indicating that the same protein catalyzes both reactions. Competitive inhibition of esterase activity by glyceraldehyde and chloral hydrate furnished evidence that p-nitrophenyl acetate was hydrolyze...

Yeast Aldehyde Dehydrogenase

The potassium-activated, pyridine nucleotide-linked aldehyde dehydrogenase from yeast has been purified to the stage of homogeneity as judged by ultracentrifugation and gel electrophoresis. The enzyme has been crystallized, although this is not a recommended step in purification because loss of catalytic activity is thereby incurred. At least three separable, active fractions were obtained with...

Rat Liver Aldehyde Dehydrogenase

From normal rat liver mitochondrial and microsomal fractions, 4 distinct aldehyde dehydrogenase isozymes with millimolar substrate K,,, values have been purified and characterized. Two isozymes were isolated from mitochondria and 2 from microsomes. A mitochondrial aldehyde dehydrogenase with a substrate K,,, in the micromolar range was also identified. Subunit molecular weights for all millimol...