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The Comparative Enzymology and Cell Origin of Rat Hepatomas

III. Some Enzymes of Amino Acid Metabolism^*

Henry C. Pitot, Carl Peraino, Richard H. Bottomley and Harold P. Morris

( McArdle Memorial Laboratory, The Medical School, University of Wisconsin, Madison, Wisconsin; and the National Cancer Institute, National Institutes of Health, Bethesda, Maryland)

The activities of several enzymes of amino acid metabolism including tryptophan pyrrolase, threonine and serine dehydrase, proline oxidase, pyrroline-5-carboxylate reductase, tyrosine -ketoglutarate transaminase, and histidase were measured in host livers and a number of minimal-deviation hepatomas. In contrast to previous reports on more anaplastic hepatic neoplasms, the tumors reported here possessed substantial amounts of many of these enzymes. However, all the tumors studied appeared to be unique in that no two possessed an identical enzyme pattern. The significance of a secondary site active in amino acid metabolism in the host-tumor relationship of rats bearing minimal-deviation hepatomas is discussed.

^* This work was supported in part by a grant (No. C-646) from the National Cancer Institute, National Institutes of Health, U.S. Public Health Service.

Postdoctoral fellow (#13,911), National Cancer Institute, United States Public Health Service.

Postdoctoral fellow (#13,610), National Cancer Institute, United States Public Health Service.

Received 7/16/62.