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

• Autorzy: Saboury A. A. , Divsalar A. , Ataie G. , Amanlou M. , Moosavi-Movahedi A.A. , Hakimelahi G.H.
• Języki publikacji: EN

Abstrakty

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 uM by the microcalorimetry method, which agrees well with the value of 342 uM for the inhi­bition constant that was obtained from the spectroscopy method. Positive dependence of caffeine binding on temperature indicates a hydrophobic interaction.

Słowa kluczowe

EN

caffeine; hydrophobic interaction; calorimetry; inhibition; spectroscopy; adenosine deaminase

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2003
• Tom: 50
• Numer: 3
• Opis fizyczny: p.849-855,fig.

Twórcy

autor

Saboury A. A.

• University of Tehran, Tehran, Iran

autor

Divsalar A.

autor

Ataie G.

autor

Amanlou M.

autor

Moosavi-Movahedi A.A.

autor

Hakimelahi G.H.

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