中山大学学报（自然科学版）2009，Vol.48Issue(6)：73-78,82,7.
山梨酸钾与蛋白质相互作用的荧光和共振光散射光谱研究
Interaction between Potassium Sorbate and Bovine Serum Albumin Revealed by Fluorescence and Resonance Light Scattering Spectra
摘要
Abstract
The interaction between potassium sorbate (PSA) and bovine serum albumin (BSA) was investigated by fluorescence spectroscopy, resonance light-scattering (RLS) spectroscopy. The quenching mechanism was analyzed referring to PSA against the fluorescence and the resonance light scattering spectra of BSA. The apparent binding constants (K_A) between PSA and BSA were 2.23 × 10~3 L·mol~(-1) (288 K) , and 2.74 × 10~3 L·mol~(-1) (293 K) , respectively. The corresponding binding sites values (n) were 1.02 and 0.99.The changes of negative entropy change and enthalpy indicate that the interaction of PSA and BSA was driven mainly by electrostatic interactions. The binding process was a spontaneous process in which Gibbs free energy change was negative. The effect of PSA on the conformation of BSA was analyzed by synchronous fluorescence spectroscopy. Furthermore, the binding distance r =2.83 nm between PSA and BSA was obtained based on the mechanism of Forster non-radiation energy transfer.关键词
山梨酸钾/牛血清白蛋白/相互作用/荧光光谱/共振散射光谱Key words
potassium sorbate/ bovine serum albumin/ interaction/ fluorescence spectra/ resonance light scattering spectra分类
化学引用本文复制引用
胡勇,扶雄,陈旭东,杨连生,章明秋..山梨酸钾与蛋白质相互作用的荧光和共振光散射光谱研究[J].中山大学学报（自然科学版）,2009,48(6):73-78,82,7.基金项目
国家自然科学基金资助项目(50673104) （50673104）
