Reduction of 3-mercaptopyruvate in rat liver is catalyzed by lactate dehydrogenase.
It has been assumed that the in vivo reduction of 3-mercaptopyruvate, an intermediate of cysteine metabolism, to 3-mercaptolactate is catalyzed by lactate dehydrogenase (EC 1.1.1.27) though no definitive evidence has been presented. In order to examine this assumption, reduction of 3-mercaptopyruvate and its inhibition were studied using rat liver homogenate, lactate dehydrogenase purified from rat liver and anti-lactate dehydrogenase antiserum. Reduction of 3-mercaptopyruvate was actively catalyzed by rat liver homogenate and by the purified lactate dehydrogenase. This reducing activity was completely inhibited by anti-lactate dehydrogenase antiserum. These results indicate that the reduction of 3-mercaptopyruvate to 3-mercaptolactate in rat liver is catalyzed by lactate dehydrogenase.
Ohta
J
J
Department of Biochemistry, Okayama University Medical School, Japan.
Ubuka
T
T
D000818:Animals; D002846:Chromatography, Affinity; D002852:Chromatography, Ion Exchange; D003545:Cysteine / Q000031:analogs & derivatives* / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D005779:Immunodiffusion; D007770:L-Lactate Dehydrogenase / Q000302:isolation & purification / Q000378:metabolism*; D008099:Liver / Q000201:enzymology*; D010084:Oxidation-Reduction; D051381:Rats
C008366:3-mercaptopyruvic acid; D007770:L-Lactate Dehydrogenase; D003545:Cysteine