Malate Dehydrogenase Species in the Cytosolic Fraction of Chicken Liver

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Abstract
The malate dehydrogenase activity in the cytosolic fraction isolated from chicken hepatocytes is resolved by DEAE-Sephacel chromatography in three active, electrophoretically distinct, species obtained in homogeneous form by affinity chromatography on 5''-AMP-Sepharose and Blue-Sepharose. Two of those species, according to the results obtained, might represent different conformational isomers of the enzyme molecule. Their purified preparations show identical amino-acid compositions and physico-chemical properties very similar to those of the cytosolic isoenzyme of other sources. The third one corresponds to a slight contamination of the mitochondrial isoenzyme.