JBC Transcription and Nuclear Factor Monoclonals

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Kinetics and Electrophoretic Properties of the Isozymes of Aspartate Aminotransferase from Pig Heart

J. S. Nisselbaum 1 and Oscar Bodansky 1

From the 1 From the Division of Biochemistry, Sloan-Kettering Institute for Cancer Research, Department of Biochemistry, Memorial Hospital, and Sloan-Kettering Division of Cornell University Graduate School of Medical Sciences, New York, New York 10021

Cationic aspartate aminotransferase from pig heart was completely destroyed by heating to 75° for 20 min in the purification procedure of Jenkins, Yphantis, and Sizer (11). Chromatography of the partially purified enzyme preparation on carboxymethyl cellulose according to the method of Henson and Cleland (8) yielded two enzyme fractions both of which migrated toward the anode upon starch gel electrophoresis. These two fractions were also kinetically and immunochemically indistinguishable from each other. Pig heart mitochondrial aspartate aminotransferase migrated toward the cathode upon starch gel electrophoresis. It differed both kinetically and immunochemically from the anionic isozyme of pig heart.

Submitted on January 7, 1966


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