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The effects of temperature and common ions on binding (-)-epicatechin gallate  (ECG) to bovine serum albumin (BSA) are investigated. The binding constants  (Ka) between ECG and BSA are 1.20 Ч 106 (17°C), 1.38 Ч 106 (27°C), and 5.69 x  106 L mol-1 (37°C), and the number of binding sites (n) were 1.14, 1.15, and  1.26, respectively. These results showed that the increasing temperature  improves the stability of the ECG-BSA system, which results in a higher  binding constant and the number of binding sites of the ECG-BSA system. The  presence of Co2+ and Zn2+ ions decreased the binding constants (Ka) and the  number of binding sites (n) of ECG-BSA complex. However, the presence of Cu2+  and Ni2+ increased the affinity of ECG for BSA largely. The positive ΔH and  positive ΔS indicated that hydrophobic forces might play a major role in the  binding between ECG and BSA

Investigation of the effects of temperature and ions on the interaction between ECG and BSA by the fluorescence quenching method