Abstract
In the partial purification of uridine kinase (ATP:uridine 5′-phosphotransferase, EC 2.7.1.48) from Ehrlich ascites tumor cells, two active fractions were obtained by chromatography on Sepharose 6B. Their molecular weights, as determined by a gel filtration and sucrose density centrifugation, were approximately 120 000 and 30 000. The larger molecular weight species was less stable on incubation at 60° and slightly less sensitive to CTP inhibition than the lower molecular weight fraction. Both fractions were stabilized against heat inactivation by ATP and CTP.The two fractions displayed similar apparent Km values for uridine and ATP, similar specificities for substrates and inhibitors, and similar divalent cation requirements.In the partial purification of uridine kinase from mouse intestine, only the larger molecular weight fraction was obtained by chromatography on Sepharose 6B.In addition, some preliminary evidence for a monomer–polymer relationship between the two molecular weight species is presented.
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