Isolation of deoxycytidine kinase from Ehrlich carcinoma cells by affinity chromatography based on a substrate analog, 2'-C-cyano-2'-deoxy-1-beta-D-arabinofuranosyl-N4-palmitoylcytosine++ +

Biological & Pharmaceutical Bulletin
H UchidaT Sasaki

Abstract

Deoxycytidine kinase from Ehrlich carcinoma cells was purified 10400-fold by ammonium sulfate fractionation and affinity chromatography using Sepharose 4B coupled to 2'-C-cyano-2'-deoxy-1-beta-D-arabinofuranosyl-N4-palmitoylcytosine , with a yield of 45%. The purified enzyme preparation showed a single major band with a molecular weight of 32000 on SDS-PAGE. The enzyme phosphorylated deoxyadenosine, deoxyguanosine, cytidine, and several deoxycytidine analogues as well as deoxycytidine. Also, the kinetic parameters of the enzyme for the substrates were estimated.

References

Feb 18, 2004·Cancer Science·A Matsuda, Takuma Sasaki
Jul 28, 2001·Japanese Journal of Cancer Research : Gann·T ObataT Sasaki
Jul 1, 2010·Drug Metabolism and Disposition : the Biological Fate of Chemicals·Takahiro YoshidaTakuma Sasaki

Related Concepts

Arabinonucleosides
SDS-PAGE
Cytosine
DCK gene
Enzyme agent
Chemical Fractionation
2'-deoxyadenosine
Deoxyguanosine
Deoxycytidine Kinase
Sepharose 4B

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