Lactic dehydrogenases: subfractionation of isozymes

Abstract

Electrophoresis in polyacrylamide gel of homogenates of various organs from the mouse yields five major lactic dehydrogenase bands. If the gels are treated with beta-mercaptoethanol, subsequent electrophoresis produces 15 bands which show lactic dehydrogenase activity. This could be explained if one molecule of nicotinamide adenine dinucleotide (coenzyme) is attached to each of the monomeric subunits of lactic dehydrogenase and if mercaptoethanol can remove the coenzyme only from the muscle type. This is consistent with the hypothesis that intact lactic dehydrogenase is a tetramer.