Interactions of Trimeric Purine Nucleoside Phosphorylases with Ground State Analogues—Calorimetric and Fluorimetric Studies

Autor:	Gertraud Koellner, Beata Wielgus-Kutrowska, Antonín Holý, Joachim Frank, Agnieszka Bzowska
Rok vydání:	2003
Předmět:	Chemistry Stereochemistry Purine nucleoside phosphorylase Isothermal titration calorimetry Purine Nucleosides General Medicine Calorimetry Biochemistry Fluorescence Substrate Specificity Dissociation constant chemistry.chemical_compound Spectrometry Fluorescence Purine-Nucleoside Phosphorylase Genetics Animals Molecular Medicine Cattle Binding site Ground state Spleen Hypoxanthine Stoichiometry Cellulomonas
Zdroj:	Nucleosides, Nucleotides and Nucleic Acids. 22:1695-1698
ISSN:	1532-2335 1525-7770
DOI:	10.1081/ncn-120023116
Popis:	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.
Databáze:	OpenAIRE
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