Subcellular localization and biochemical properties of rat testicular alcohol- and aldehyde-dehydrogenase.
The biochemical properties and the subcellular distribution of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) in the rat testis is reported. Both enzymes are NAD-dependent. Testicular ADH activity was found in the nuclear and in the cytosolic fractions. Measurable ALDH was determined in the nuclear, mitochondrial, cytosolic and in the microsomal preparations. The major activity of ADH and ALDH were assayed in cytosol fraction. Cytosolic ALDH possesses lower Km than that determined in the mitochondrial and in the microsomal fractions. The results suggest the presence of multiple active form of testicular ALDH, possibly isoenzymes.
D000375:Aging; D000426:Alcohol Dehydrogenase; D000429:Alcohol Oxidoreductases / Q000378:metabolism*; D000444:Aldehyde Dehydrogenase; D000445:Aldehyde Oxidoreductases / Q000378:metabolism*; D000818:Animals; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D008297:Male; D051381:Rats; D011919:Rats, Inbred Strains; D013347:Subcellular Fractions / Q000201:enzymology; D013696:Temperature; D013737:Testis / Q000201:enzymology*; D014018:Tissue Distribution
D000429:Alcohol Oxidoreductases; D000426:Alcohol Dehydrogenase; D000445:Aldehyde Oxidoreductases; D000444:Aldehyde Dehydrogenase