Polyacrylamide disc electrophoresis of human semen lactate dehydrogenase in the presence of sulfur compounds.
Total LDH-P and isozymes of ejaculates from virile men were ascertained following incubation at 37 degrees with solutions of various sulfur compounds (pH 7.2: initial concentrations up to 0.40 M) for periods of at least 18-24 hr. As based on polyacrylamide disc electrophoresis, inactivation of the testicular isozyme, LDH-X, was almost complete with penicillamine and its disulfide, somewhat less with GSH and GSSG, least with thioglycolate and its disulfide and inconsistent with cysteine, 2-mercaptoethanol and 2-mercaptoethylamine. The inactivation may stem from conformational changes rather than simple redox considerations, the findings being negative with 3-mercatopropionate, N-acetyl-penicillamine and thiodiglycolate. Thiophenoxyacetate, levamisole and dimethyl sulfoxide depressed total LDH and LDH-X was the principal component in the respective patterns for ejaculate concentrates. Sub-banding of LDH-1, LDH-2 and LDH-3 occurred in several of the gels employing phthalyltetrathioacetate to the exclusion of any effect on LDH-X; splitting was minimal in LDH-4 but was more prominent in gels from aspermic men. As in prior studies with serum, the sulfhdryl and disulfide compounds had little effect on LDH-P nor on the relative distribution of the isozymes in ejaculates from vasectomized men in which LDH-X was absent.
D000328:Adult; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007527:Isoenzymes; D007770:L-Lactate Dehydrogenase / Q000032:analysis*; D008297:Male; D012661:Semen / Q000201:enzymology*; D013455:Sulfur
D007527:Isoenzymes; D013455:Sulfur; D007770:L-Lactate Dehydrogenase