Abstract
Publisher Summary This chapter describes the purification procedure of deoxythymidine (TdR) kinase enzyme from regenerating rat liver. This enzyme is responsible for recycling endogenous deoxythymidine through the pyrimidine salvage pathway and for the utilization of exogenous deoxythymidine within tissues. TdR kinase activity within mammalian cells is closely correlated with their proliferation capacity. The enzyme is not only affected by induction at the transcriptional level but also is markedly influenced by the concentration of deoxyribonucleotides. The assay method is based upon the binding potential of the cationic support, diethylaminoethanol (DEAE)-cellulose, for anions, for example, deoxythymidylate phosphohydrolase (dTMP). TdR kinase fulfills an important role in the activation of a number of pyrimidine analogs for chemotherapeutic efficacy, particularly the halogenated pyrimidine deoxyribonucleosides. TdR kinase is end-product inhibited by deoxythymidine triphosphate (dTTP) in a noncompetitive fashion that is markedly dependent upon the adenosine triphosphate (ATP) concentration. Apart from the cytosolic TdR kinase described in the chapter, a second set of enzymes are also reported to be associated with mitochondria.
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