This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Davis, J. L. Articles by Morris, H. P. Search for Related Content PubMed PubMed Citation Articles by Davis, J. L. Articles by Morris, H. P.

Two Enzymes of Serine Metabolism in Rat Liver and Hepatomas¹

Department of Biochemistry [J. L. D., H. J. F.] and Department of Medicine [H. J. F.], University of North Carolina School of Medicine, Chapel Hill, North Carolina 27514, and Laboratory of Biochemistry, National Cancer Institute, Bethesda, Maryland 20014 [H. P. M.]

Two enzymes of serine metabolism, 3-P-glycerate dehydrogenase and L-serine dehydratase, were measured in four Morris hepatoma lines and in the corresponding host livers of rats that had been fed normal or low-protein diets. The activities of these enzymes in normal rat liver are altered by changes in dietary protein content.

3-P-glycerate dehydrogenase activity was greater in the tumor lines than in normal rat liver or host livers of rats fed a 25% casein diet ad libitum. The level of 3-P-glycerate dehydrogenase was higher in the two rapidly growing tumor lines, 9121 and 5123TC, than in the slower-growing 7794B and 7793. No correlation between tumor growth rate and serine dehydratase was demonstrated. The 3-P-glycerate dehydrogenase and serine dehydratase activity of the hepatomas did not respond to changes in protein intake in the same manner as the normal and host livers.

¹ This research was supported by USPHS Grants AM-09000 and ES-00129.

² Present address: Department of Agricultural Chemistry, Oregon State University, Corvallis, Ore. 97331.

³ Present address: Department of Biochemistry, College of Medicine, Howard University, Washington, D. C. 20001. Supported in part by USPHS Grant CA-10729.

Received 6/29/70. Accepted 9/ 1/70.