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Studies on Deoxythymidine Kinase of Regenerating Rat Liver and Escherichia coli¹

Department of Pharmacology, Baylor College of Medicine, Houston, Texas 77025

Deoxythymidine kinase was partially purified from regenerating rat liver, and its properties were compared with those of Escherichia coli deoxythymidine kinase. These properties included K_m for deoxythymidine and for ATP, sedimentation in a sucrose density gradient, and migration in an electrophoretic field. The regenerating liver enzyme had a sedimentation constant of approximately 5.0 S, while the enzyme from E. coli sedimented at 3.6 S. The sedimentation constant of the latter enzyme was markedly influenced by dTTP; the sedimentation constant of the regenerating liver enzyme was not influenced by this deoxyribonucleotide. The E. coli enzyme exhibited the greater mobility in disc electrophoresis.

¹ This research was supported by Robert A. Welch Foundation Grant Q 198, National Science Foundation Grant GB 8010, and NIH Grant CA 10893. Manuscript No. 20 from the Cancer Research Center at Baylor College of Medicine.

² Present address: Defiance College, Defiance, Ohio.

Received 3/24/70. Accepted 6/16/70.