Thermodynamic studies of interactions of calf spleen PNP with acyclic phosphonate inhibitors

Abstract The Gibbs binding energy and entropy/enthalpy contributions to the interaction of calf spleen purine nucleoside phosphorylase (PNP) with the novel multisubstrate analogue DFPP-DG, as well as with DFPP-G and (S)-PMP-DAP were determined by fluorescence and calorimetric studies. Results were c...

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Published in:Nucleic Acids Symposium Series 2008, Vol.52 (1), p.663-664
Main Authors: Breer, Katarzyna, Wielgus-Kutrowska, Beata, Hashimoto, Mariko, Hikishima, Sadao, Yokomatsu, Tsutomu, Szczepanowski, Roman H., Bochtler, Matthias, Girstun, Agnieszka, Staroń, Krzysztof, Bzowska, Agnieszka
Format: Article
Language:English
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Summary:Abstract The Gibbs binding energy and entropy/enthalpy contributions to the interaction of calf spleen purine nucleoside phosphorylase (PNP) with the novel multisubstrate analogue DFPP-DG, as well as with DFPP-G and (S)-PMP-DAP were determined by fluorescence and calorimetric studies. Results were compared with findings for guanine - a natural reaction product and inhibitor.
ISSN:0261-3166
1746-8272
DOI:10.1093/nass/nrn335