Interactions of trimeric purine nucleoside phosphorylases with ground state analogues--calorimetric and fluorimetric studies.
Binding enthalpies, dissociation constants and stoichiometry of binding for interaction of trimeric calf spleen and Cellulomonas sp. purine nucleoside phosphorylases with their ground state analogues (substrates and inhibitors) were studied by calorimetric and spectrofluorimetric methods. Data for all ligands, with possible exception of hypoxanthine, are consistent with three identical non-interacting binding sites.
Wielgus-Kutrowska
Beata
B
Department of Biophysics, Institute of Experimental Physics, University of Warsaw, Warsaw, Poland.
Frank
Joachim
J
Holý
Antonin
A
Koellner
Gertraud
G
Bzowska
Agnieszka
A
D000818:Animals; D002151:Calorimetry; D002417:Cattle; D040143:Cellulomonas / Q000201:enzymology; D011684:Purine Nucleosides / Q000737:chemistry* / Q000378:metabolism*; D011683:Purine-Nucleoside Phosphorylase / Q000737:chemistry* / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D013154:Spleen / Q000201:enzymology; D013379:Substrate Specificity
D011684:Purine Nucleosides; D011683:Purine-Nucleoside Phosphorylase