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Inhibition study of adenosine deaminase by caffeine using spectroscopy and isothermal titration calorimetry.

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Kinetic and thermodynamic studies were made on the effect of caffeine on the activity of adenosine deaminase in 50 mM sodium phosphate buffer, pH 7.5, using UV spectrophotometry and isothermal titration calorimetry (ITC). An uncompetitive inhibition was observed for caffeine. A graphical fitting method was used for determination of binding constant and enthalpy of inhibitor binding by using isothermal titration microcalorimetry data. The dissociation-binding constant is equal to 350 μM by the microcalorimetry method, which agrees well with the value of 342 μM for the inhibition constant that was obtained from the spectroscopy method. Positive dependence of caffeine binding on temperature indicates a hydrophobic interaction.
Physical description
  • Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran
  • Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran
  • Faculty of Paramedical Science, Shahid-Beheshti University of Medical Science, Tehran, Iran
  • Department of Medical Chemistry, Tehran University of Medical Science, Tehran, Iran
  • Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran
  • Institute of Chemistry, Academia Sinica Taipei, Taipei, Taiwan, ROC
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