Mammalian deoxynucleoside kinases. II. Deoxyadenosine kinase: purification and properties.

Abstract Deoxyadenosine kinase was partially purified 140-fold from calf thymus by fractionation with streptomycin, protamine, and ammonium sulfate and by column chromatography on Sephadex G-150 and DEAE-cellulose. The molecular weight was estimated to be about 63,000 by gel filtration chromatography. The enzyme appears to catalyze the phosphorylation of deoxyadenosine, deoxyguanosine, and cytidine to their corresponding nucleoside 5'-monophosphates in the presence of a divalent cation and a nucleoside 5'-triphosphate. All common ribo- and deoxynucleoside 5'-triphosphates, with the exception of deoxycytidine 5'-triphosphate, could act as phosphate donors.