Binding properties of adenosine deaminase interacted with theophylline.

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

Binding properties of adenosine deaminase interacted with theophylline.

Chem Pharm Bull (Tokyo). 2004 Oct;52(10):1179-82.

PubMed ID

15467230 [ View in PubMed

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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.

DrugBank Data that Cites this Article

Drug Enzymes

Drug	Enzyme	Kind	Organism	Pharmacological Action	Actions
Theophylline	Adenosine deaminase	Protein	Humans	Unknown	Inhibitor Inducer	Details