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A Comparative Study of Rat Liver, Muscle, and Hepatoma 3924A Phosphofructokinase Isozymes¹

Department of Pharmacology, Indiana University School of Medicine, Indianapolis, Indiana 46202 [G. A. D., G. W.], and Department of Biochemistry, Howard University College of Medicine, Washington, D. C. 20001 [H. P. M.]

Two phosphofructokinase isozymes are present in rat liver representing 85 and 15% of the total activity, respectively. The single isozyme observed in muscle is distinct from the two in liver. In hepatoma 3924A three isozymes were detected that were 5, 20, and 75% of the total activity. The major liver and hepatoma isozymes were judged to be identical on the basis of the following criteria: diethylaminoethyl cellulose chromatography, starch gel electrophoresis, and kinetic and immunological properties. The major isozyme was elevated two- to threefold in hepatoma 3924A on the basis of total activity and amount of antiserum required for complete neutralization. The minor liver isozyme is probably also present in hepatoma, but in addition a nonhepatic isozyme also appears to be present which is quite similar to, but distinct from, the muscle isozyme. This nonhepatic isozyme could not be detected in embryonic liver. Although the alteration in gene expression observed with the hepatoma phosphofructokinase isozyme pattern is not as drastic a change as was found for the other two key glycolytic isozymes (adenosine 5'-triphosphate-glucose phosphotransferases and adenosine 5'-triphosphate-pyruvate phosphotransferases), the increase in total activity agrees with the prediction of the molecular correlation concept.

¹ This study was supported by grants from the American Cancer Society (Institutional Grant IN-46-L); USPHS, National Cancer Institute (CA-05034 and CA-13526); and Damon Runyon Memorial Fund for Cancer Research, Inc.

² Present address: Biology Department, State University of New York, Buffalo, N. Y. 14214.

Received 2/19/74. Accepted 5/ 7/74.