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A Novel method for Thermodynamic Study on the Binding of Milk Carrier protein of BLG-A with Cr+3

100%
Behbehania G., Divsalar A., Saboury A.
Polish Journal of Chemical Technology
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2009
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vol. 11
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issue 4
24-29
EN
Thermodynamics of the interaction between Cr3+ with β-lactoglobulin type A (BLG-A) was investigated at pH 7.0 and 37°C by isothermal titration calorimetry. A new method to follow the effect of Cr3+ on the stability of BLG-A was introduced. The new solvation model was used to reproduce the enthalpies of BLG-A+ Cr3+ interactions over the whole range of Cr3+ concentrations. The solvation parameters recovered from the new equation are attributed to the structural change of BLG-A and its biological activity. The results obtained indicate that there is a set of two identical binding sites for Cr3+ ions with positive cooperativity. The association equilibrium constants are 14.39 and 0.49 mM-1 for the first and second binding site, respectively. The enthalpy of binding for one mole of Cr+3 ion to one mole of the binding site on BLG-A (ΔH=104.60 kJ mol-1) is obtained.
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Inhibition study of adenosine deaminase by caffeine using spectroscopy and isothermal titration calorimetry.

76%
Saboury A. A., Divsalar A., Ataie G., Amanlou M., Moosavi-Movahedi A. A., Hakimelahi G. H.
Acta Biochimica Polonica
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2003
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vol. 50
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issue 3
849-855
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.
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