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Department of Pharmacology [E. B., K. D. M.] and Pathology [E. D. M.] Baylor College of Medicine, Houston, Texas 77025, and Department of Biochemistry [H. P. M.], Howard University College of Medicine, Washington, D. C. 20001
The activities of a group of enzymes involved in the de novo synthesis of pyrimidines and of deoxythymidine kinase have been determined in host kidney, control kidney cortex, and in the slowly growing rat kidney adenocarcinomas, 8997K, 9786K, and 9789K. The age of the kidney adenocarcinomas varied from approximately 80 days to over 400 days. Deoxythymidine kinase activity in the tumors was augmented by a factor of 25 over the value found in kidney cortex; aspartate transcarbamylase, orotidine-5'-phosphate pyrophosphorylase and decarboxylase, and dihydroorotase and dihydroorotic dehydrogenase activities were elevated by a factor of approximately 2 in the adenocarcinoma preparations.
1 Supported by Robert A. Welch Foundation Grants; Q-198; HE-05435-09, P-6; CA-10729; NSF GB 8010; and CA-10893. Publication No. 7 from the Cancer Research Center, Baylor College of Medicine.
Received 11/ 4/68. Accepted 4/ 1/69.
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