Chromatographic behaviour of the molecular forms of guinea-pig skeletal muscle cytoplasmic malate dehydrogenase

The isolated molecular forms of guinea-pig skeletal muscle cytoplasmic malate dehydrogenase have a different chromatographic behaviour through affinity or hydrophobic interaction gels; in all cases the retention of the B form is more noticeable. Chromatography of a partly purified preparation through 5' AMP-Sepharose allows both molecular forms of malate dehydrogenase to be separated and obtained free from lactate dehydrogenase.