Organ-specific human alcohol dehydrogenase: isolation and characterization of isozymes from testis.
Class III alcohol dehydrogenase (ADH) predominates in human testis. The two isozymes of this class were isolated jointly by affinity and conventional ion exchange chromatography. They display anodic electrophoretic mobility at pH 8.2, are completely insensitive to 4-methylpyrazole inhibition and oxidize ethanol and other short-chain primary alcohols very poorly. Thus, their kinetic and inhibition characteristics are identical to human liver class III ADH. In contrast, class I ADH is a barely detectable component of testicular alcohol dehydrogenase. The physicochemical characteristics of class III ADH are virtually identical to those of alcohol dehydrogenases found in other organs.
D000426:Alcohol Dehydrogenase; D000429:Alcohol Oxidoreductases / Q000302:isolation & purification*; D002846:Chromatography, Affinity; D002848:Chromatography, DEAE-Cellulose; D004592:Electrophoresis, Starch Gel; D006801:Humans; D007527:Isoenzymes / Q000302:isolation & purification*; D007700:Kinetics; D008297:Male; D009928:Organ Specificity; D013379:Substrate Specificity; D013737:Testis / Q000201:enzymology*
D007527:Isoenzymes; D000429:Alcohol Oxidoreductases; D000426:Alcohol Dehydrogenase