Binding of Substrates by Purine Nucleoside Phosphorylase (PNP) fromCellulomonas Sp.- Kinetic and Spectrofluorimetric Studies
- 1 April 1999
- journal article
- Published by Taylor & Francis in Nucleosides and Nucleotides
- Vol. 18 (4-5) , 871-872
- https://doi.org/10.1080/15257779908041586
Abstract
Dissociation constants and stoichiometry of binding for interaction of Cellulomonas sp. purine nucleoside phosphorylase with its substrates: inosine/guanosine, orthophosphate, guanine/hypoxanthine and D-ribose-1-phosphate were studied by kinetic and spectrofluorimetric methods.Keywords
This publication has 3 references indexed in Scilit:
- cellulomonas sp. Purine Nucleoside Phosphorylase (PNP)Published by Springer Nature ,1998
- Purine nucleoside phosphorylase: A target for drug designMedicinal Research Reviews, 1993
- Specificity of purine nucleoside phosphorylase from Escherichia coliCollection of Czechoslovak Chemical Communications, 1977