Fluorescence Studies of Substrate Binding to Human Recombinant Deoxycytidine Kinase

@article{Mani2004FluorescenceSO,
  title={Fluorescence Studies of Substrate Binding to Human Recombinant Deoxycytidine Kinase},
  author={Rajam S. Mani and Elena V. Usova and Staffan K Eriksson and Carol E. Cass},
  journal={Nucleosides, Nucleotides \& Nucleic Acids},
  year={2004},
  volume={23},
  pages={1343 - 1346}
}
  • R. Mani, E. Usova, C. Cass
  • Published 1 October 2004
  • Biology, Chemistry
  • Nucleosides, Nucleotides & Nucleic Acids
Deoxycytidine kinase (dCK), is responsible for the phosphorylation of deoxynucleosides to the corresponding monophosphates using ATP or UTP as phosphate donors. Steady‐state intrinsic fluorescence measurements were used to study interaction of dCK with substrates in the absence and presence of phosphate donors. Enzyme fluorescence quenching by its substrates exhibited unimodal quenching when excited at 295 nm. Binding of substrates induced conformational changes in the protein, suggesting that… 
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TLDR
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