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Journal Article

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

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Bochtler,  Matthias
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Citation

Breer, K., Wielgus-Kutrowska, B., Hashimoto, M., Hikishima, S., Yokomatsu, T., Szczepanowski, R. H., et al. (2008). Thermodynamic studies of interactions of calf spleen PNP with acyclic phosphonate inhibitors. Nucleic Acids Symposium Series, 52, 663-664.


Cite as: https://hdl.handle.net/21.11116/0000-0001-0EBA-F
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.