Coronel C E, Burgos C, Gerez de Burgos N M, Rovai L E, Blanco A
J Exp Zool. 1983 Mar;225(3):379-85. doi: 10.1002/jez.1402250305.
A comparative study of catalytic properties of the sperm-specific lactate dehydrogenase (EC 1.1.1.27) isozyme X or C4 from a variety of animals (boar, bull, goat, Guinea pig, man, mouse, pigeon, rabbit, and rat) is presented. Optimum concentration and Km values for pyruvate, inhibition by substrate, and activity against analog substrates (alpha-ketoacids with linear and branched chains from 4 to 6 carbon atoms) for isozyme X of different species showed significant differences. The observed properties are correlated with available evidence on the metabolic role of the enzyme.
本文对多种动物(野猪、公牛、山羊、豚鼠、人类、小鼠、鸽子、兔子和大鼠)的精子特异性乳酸脱氢酶(EC 1.1.1.27)同工酶X或C4的催化特性进行了比较研究。不同物种同工酶X对丙酮酸的最佳浓度和Km值、底物抑制作用以及对类似底物(具有4至6个碳原子的直链和支链α-酮酸)的活性存在显著差异。观察到的这些特性与该酶代谢作用的现有证据相关。