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A Product Inhibition Study on Adenosine Deaminase by Spectroscopy and Calorimetry
(Ali Akbar Saboury),(Ghasem Ataie Jafari),(Ali Akbar Moosavi Movahedi),(Mohammad Reza Housaindokht),(Gholam Hosain Hakimelahi),(Adeleh Divsalar) 생화학분자생물학회 2002 BMB Reports Vol.35 No.3
Kinetic and thermodynamic studies have been made on the effect of the inosine product on the activity of adenosine deaminase in a 50 mM sodium phosphate buffer, pH 7.5, at 27oC using UV spectrophotometry and isothermal titration calorimetry (ITC). A competitive inhibition was observed for inosine as a product of the enzymatic reaction. A graphical-fitting method was used for determination of the binding constant and enthalpy of inhibitor binding by using isothermal titration microcalorimetry data. The dissociation-binding constant is equal to 140 μM by the microcalorimetry method, which agrees well with the value of 143 μM for the inhibition constant that was obtained from the spectroscopy method.