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Comparative Study of Mitochondrial Malate Dehydrogenase from Normal Rat Liver and Morris Hepatomas in Vivo and in Culture¹

Department of Biochemistry, The University of Iowa, Iowa City, Iowa 52242

Mitochondrial malate dehydrogenase [L-malate, nicotin-amide adenine dinucleotide oxidoreductase (EC 1.1.1.37)] from Morris rat hepatomas grown in vivo and from Morris rat hepatoma 7288C grown in cell culture (hepatic tumor cells) has been maximally purified for comparison with mitochondrial malate dehydrogenase from normal rat liver. A rabbit antiserum directed against normal rat liver mitochondrial malate dehydrogenase has been used for immunochemical characterization. Other studies included comparing rates of inactivation by proteolytic enzymes, behavior on polyacrylamide gel, and profiles of isoelectric focusing. By the criteria used, the comparisons revealed enzyme identity. The only difference is in the initial extractable total activity of the enzyme (IU/g tissue) which is lower in hepatomas.

¹ Supported by a research grant from the National Cancer Institute, NIH (CA 07617).

² Present address: Department of Human Biology, John Curtin School of Medical Research, P. O. Box 334, Canberra City, A.C.T. 2601, Australia.

Received 8/11/80. Accepted 9/18/80.