title: Interactions of trimeric purine nucleoside phosphorylases with ground state analogues--calorimetric and fluorimetric studies.
abstract: 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.
authors.affiliation: Department of Biophysics, Institute of Experimental Physics, University of Warsaw, Warsaw, Poland.
authors.forename: Beata
authors.initials: B
authors.lastname: Wielgus-Kutrowska
authors.forename: Joachim
authors.initials: J
authors.lastname: Frank
authors.forename: Antonin
authors.initials: A
authors.lastname: Holý
authors.forename: Gertraud
authors.initials: G
authors.lastname: Koellner
authors.forename: Agnieszka
authors.initials: A
authors.lastname: Bzowska
mesh_terms: 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
chemical_list: D011684:Purine Nucleosides; D011683:Purine-Nucleoside Phosphorylase