Study on the Mechanism of Interaction Between Chrysophanol and Bovine Serum Albumin by UV-Absorptiospectrometry and Fluorospectrometry

Mechanism of the interaction between chrysophanol and bovine serum albumin (BSA) under different external circumstances was studied by UV-absorptiospectrometry and fluorospectrometry.It was found that fluorescence quenching of the interaction either in nearly neutral,weakly acidic or weakly alkaline medium was due to static quenching.The binding constants,number of binding sites,types of the binding force and binding distances were found by applying the equation of model of site-binding,thermodynamic equations,and Foster theory of transfer of non-radiation energy.It was also shown that the binding constants were affected by the presence of trace amounts of metal ions and of several organic solvents.