Binding properties of adenosine deaminase interacted with theophylline.

Abstract:

:Thermodynamic studies were carried out to evaluate the binding of theophylline on adenosine deaminase (ADA) in 50 mM sodium phosphate buffer pH 7.5, at 300 K, using isothermal titration calorimetry (ITC). A simple method for determination of binding isotherm in the drug--ADA interaction was applied using ITC data. ADA has two binding sites for theophylline, which show positive cooperativity in its sites. The intrinsic association equilibrium constants are 6 and 52 mM(-1) in the first and second binding sites, respectively. Hence, occupation of the first site has produced an appreciable enhancement by 8.7 of the binding affinity of the second site. The molar enthalpies of binding are -12.2 and -14.9 kJ/mol in the first and second binding sites, respectively.

authors

Saboury AA,Bagheri S,Ataie G,Amanlou M,Moosavi-Movahedi AA,Hakimelahi GH,Cristalli G,Namaki S

doi

10.1248/cpb.52.1179

subject

Has Abstract

pub_date

2004-10-01 00:00:00

pages

1179-82

issue

10

eissn

0009-2363

issn

1347-5223

pii

JST.JSTAGE/cpb/52.1179

journal_volume

52

pub_type

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