A genuine organ specific alcohol dehydrogenase from hamster testes: isolation, characterization and developmental changes.
Testes of golden hamsters (Mesocricetus auratus) contain a unique form of alcohol dehydrogenase. The enzyme purified to homogeneity is a dimer composed of two identical 41000 dalton subunits and was inhibited by 4-methylpyrazole and 1, 10-phenanthroline. The enzyme prefers primary over secondary alcohol substrates and oxidizes vitamin A (retinol) most efficiently. Its activity in the testis increases during the prepubertal development and such increase is concomitant with, but preceding slightly, the increase in testicular weight and plasma testosterone. These results may implicate the involvement of this enzyme in the development of male hamsters' reproductive system.
Keung
W M
WM
Department of Biochemistry, Chinese University of Hong Kong, Shatin, N.T.
D000375:Aging; D000426:Alcohol Dehydrogenase / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D006224:Cricetinae; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008297:Male; D008970:Molecular Weight; D009928:Organ Specificity; D012741:Sexual Maturation; D013379:Substrate Specificity; D013737:Testis / Q000201:enzymology* / Q000254:growth & development; D013739:Testosterone / Q000097:blood
D013739:Testosterone; D000426:Alcohol Dehydrogenase