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Adenosine Triphosphate: Adenosine Monophosphate Phosphotransferase Isozymes in Rat Liver and Hepatomas¹

Fels Research Institute, Temple University School of Medicine, Philadelphia, Pennsylvania 19140 [W. E. C., G. L., S. W.], and Department of Biochemistry, Howard University, Washington, D. C. 20001 [H. P. M.]

Adenylate kinase (ATP:AMP phosphotransferase, EC 2.7.4.3) activity was measured in rat liver and in a series of Morris hepatomas. The adenylate kinase activity was 128 units/g tissue in a group of highly differentiated hepatomas, 65 units/g in well-differentiated hepatomas, and 16 units/g in a group of poorly differentiated hepatomas. Rat liver adenylate kinase activity was 148 units/g. It increased to 287 units/g upon fasting and decreased to 92 units/g upon refeeding of a glucose diet. However, adenylate kinase activity in highly, well-, and poorly-differentiated hepatomas did not respond significantly to dietary alterations in the host animals.

Four electrophoretically distinct forms of adenylate kinase were found in supernatants from rat liver and hepatomas. The four isozymes have isoelectric points at pH's 5.9 (I), 7.0 (II), 7.6 (III), and 8.2 (IV) and were found in all tumors examined. The activities of Isozymes I, III, and IV were reasonably constant in liver and hepatomas, but the activity of Isozyme III decreased from 121 units/g in normal liver to 14 units/g in the poorly differentiated Novikoff hepatoma. Isozyme III was the major adenylate kinase isozyme in rat liver. It increased to 220 units/g in the liver of fasted rats and decreased to 80 units/g in the liver of refed rats. Isozyme III is the predominant form of adenylate kinase which, in liver, is susceptible to dietary regulation, and the form which, in the tumors, decreases with decreasing differentiation.

¹ This work was aided by NIH Grants CA-10439, CA-10906-08, CA-10729, AM-08350, and the American Cancer Society Grant P202.

² Career Development Awardee, 3K3-AM-16, 568, National Institute of Arthritis and Metabolic Diseases.

Received 5/23/69. Accepted 7/16/69.

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