No abstract

The interactions of F(-), Br(-) and I(-) with ovalbumin (OVA) were studied in acetate buffers of pH 5.68, at 288.15 K, 298.15 K and 308.15 K, using ion-selective electrodes. The data for the ion-protein systems were treated according to the Klotz equation, and the number of binding sites and the binding constants were determined. It is shown that the binding sites of F(-) on OVA molecule are more than those of Br(-) and I(-), and that the binding sites of F(-), Br(-) and I(-) on OVA molecule decreases with increasing temperature. At the same time, our studies indicate that the binding constants for the interactions of F(-), Br(-) and I(-) with OVA show a same trend: They decrease as temperature increases. These were reasonably interpreted with the structural and thermodynamic factors. The thermodynamic functions (DeltaG(), DeltaH(), DeltaS()) at different temperatures were calculated with thermodynamic equations, and the enthalpy change for the interactions were also determined by isothermal titration calorimetry (ITC) at 298.15 K, which indicate that the interactions of F(-), Br(-) and I(-) with OVA are mainly electrostatic interaction. Simultaneously, there are also partial desolvation of solutes and solvent reorganization effect.