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Survey of Some Enzyme Patterns in Transplantable Reuber Mouse Hepatomas¹

McArdle Laboratory, University of Wisconsin Medical Center, Madison, Wisconsin 53706

A series of spontaneously arising, transplantable hepatomas has been developed in C3H x Y hybrid mice by Reuber. Tyrosine aminotransferase, serine dehydratase, glucose 6-phosphate dehydrogenase, and citrate cleavage enzyme activity levels were studied in the hepatomas and host livers of mice bearing these hepatomas. Tyrosine aminotransferase activity was higher in the host livers than in the corresponding hepatomas. This enzyme in hepatomas MH1, MH2, MH3, and MH15 responded positively when a high-protein diet was fed to the host, but in hepatoma MH1 and MH15 the enzyme activity was not increased after a low-protein diet was fed to the host. Serine dehydratase activity was present at substantial levels in all host livers studied but was virtually absent in all hepatomas in mice fed a high-protein diet with the exception of hepatoma MH15, Generation 4. However, serine dehyratase in the previous generation of that hepatoma line was virtually absent. Glucose 6-phosphate dehydrogenase and citrate cleavage enzyme activities were present in all host livers and hepatomas studied but with less diversity in their activity levels compared to the activity levels of tyrosine aminotransferase and serine dehydratase. In general, the Reuber transplantable mouse hepatomas (MH1, MH2, MH3, MH4, and MH15) were biochemically similar to the diploid Morris rat hepatomas on the basis of the enzymes reported.

¹ Support was provided in part by Departmental Grant CA-07175 and Training Grant T01-CA5002 from the NIH, USPHS.

² Present address: Biochemisches Institut der Universitat, Hermann-Herder Strasse 7, 78 Freiburg, Germany.

³ To whom reprint requests should be addressed.

⁴ Career Development Awardee (CA-29,405) of the National Cancer Institute.

⁵ NIH, Bethesda, Md. 20014.

Received 12/ 7/70. Accepted 2/23/71.