Interactions of potent multisubstrate analogue inhibitors with purine nucleoside phosphorylase from calf spleen--kinetic and spectrofluorimetric studies.
Dissociation constants and stoichiometry of binding for interaction of trimeric calf spleen purine nucleoside phosphorylase with potent multisubstrate analogue inhibitors were studied by kinetic and spectrofluorimetric methods.
Iwanow
Monika
M
Department of Biophysics, Institute of Experimental Physics, University of Warsaw, Warsaw, Poland.
Magnowska
Lucyna
L
Yokomatsu
Tsutomu
T
Shibuya
Shiroshi
S
Bzowska
Agnieszka
A
D000818:Animals; D002417:Cattle; D004791:Enzyme Inhibitors / Q000493:pharmacokinetics* / Q000494:pharmacology; D007700:Kinetics; D011683:Purine-Nucleoside Phosphorylase / Q000037:antagonists & inhibitors* / Q000378:metabolism; D013050:Spectrometry, Fluorescence; D013154:Spleen / Q000201:enzymology*; D013379:Substrate Specificity
D004791:Enzyme Inhibitors; D011683:Purine-Nucleoside Phosphorylase