Abstract
Nucleoside kinases phosphorylate endogenous nucleosides and nucleoside analogs which are anticancer and antiviral drugs. dCytidine kinase was purified from cultured human T-lymphoblasts to a specific activity of 8 umol/min/mg protein and 92% purity. The molecular weight was 60 kD and the stokes radius was 32 A. The subunit molecular weight was 30.5 kD. dGuanosine, dadenosine and cytidine phosphorylating activities copurified with dcytidine kinase to final specific activities of 7.2, 13.5 and 4 umol/min/mg protein, respectively. This enzyme had apparent Km values of 1.5, 430, 500, 450 and 40 uM for dcytidine, dguanosine, dadenosine, cytidine and cytosine arabinoside, respectively. The pH optimum ranged from 6.5-9.0. Mg2+ and Mn2+ were the preferred divalent cations. ATP, GTP, dGTP, ITP, dITP, TTP and XTP were substrates for the enzyme. This highly purified enzyme will facilitate our delineation of the role for this enzyme in nucleoside or nucleoside analog phosphorylation and the structural basis for the regulation of this enzyme.
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Datta, N., Shewach, D., Hurley, M. et al. 34 PURIFICATION AND PROPERTIES OF HUMAN T-LYMPHOBLAST DEOXYCYTIDINE KINASE. Pediatr Res 24, 116 (1988). https://doi.org/10.1203/00006450-198807000-00058
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DOI: https://doi.org/10.1203/00006450-198807000-00058