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2003 | 50 | 3 | 849-855
Article title

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

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EN
Abstracts
EN
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.
Publisher

Year
Volume
50
Issue
3
Pages
849-855
Physical description
Dates
published
2003
received
2003-04-22
revised
2003-07-14
accepted
2003-09-02
Contributors
author
  • Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran
author
  • Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran
author
  • Faculty of Paramedical Science, Shahid-Beheshti University of Medical Science, Tehran, Iran
author
  • 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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Document Type
Publication order reference
Identifiers
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv50i3p849kz
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