Breer Katarzyna, Wielgus-Kutrowska Beata, Hashimoto Mariko, Hikishima Sadao, Yokomatsu Tsutomu, Szczepanowski Roman H, Bochtler Matthias, Girstun Agnieszka, Starón Krzysztof, Bzowska Agnieszka
Department of Biophysics, Institute of Experimental Physics, University of Warsaw, Zwirki i Wigury 93, 02-089 Warsaw, Poland.
Nucleic Acids Symp Ser (Oxf). 2008(52):663-4. doi: 10.1093/nass/nrn335.
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.
通过荧光和量热研究确定了吉布斯结合能以及熵/焓对小牛脾嘌呤核苷磷酸化酶(PNP)与新型多底物类似物DFPP-DG、DFPP-G和(S)-PMP-DAP相互作用的贡献。将结果与鸟嘌呤(一种天然反应产物和抑制剂)的研究结果进行了比较。