MULTIPLE FORMS OF DEHYDROGENASES IN THE RAT AS REVEALED BY DISC ELECTROPHORESIS

Abstract

Homogenates of various organs of rats were electrophoresed by the method of Ornstein and Davis and stained with the buffered nitro blue tetrazolium solution containing α-glycerophosphate, glutamate, hydro-cortisone, dehydroepiandrosterone, androsterone, isocitrate, malate, lactate, or 6-phosphogluconate in addition to either nicotinamide adenine dinucleotide or nicotinamide adenine dinucleotide phosphate.
Several bands of dehydrogenase activity were demonstrated with each substrate, but some of them were active even in the absence of substrate. A considerably high activity of nothing dehydrogenase was found in homogenates of rat organs, particularly, kidney, heart, and brain when nicotinamide adenine dinucleotide was used as coenzyme. This complicated the separation of substrate-specific dehydrogenases on gels. Consequently, only the positive reactions of some bands observed with α-glycerophosphate, malate, isocitrate, and 6-phosphogluconate as substrates were regarded as specific for the substrate-specific dehydrogenases.