中文摘要：

在pH7．40的Tris-HCl缓冲体系中，采用荧光光谱技术研究了橙皮甙与牛血清白蛋白（BSA）的相互作用。随着温度升高，橙皮甙与BSA的猝灭常数逐渐增加。实验表明：橙皮甙对BSA的荧光猝灭为动态猝灭过程。由热力学参数焓变（△H=70．71kJ／mol）大于零和熵变[AS=316．29J／（mol·K）]大于零，推断出橙皮甙与BSA之间主要靠疏水作用力相结合，生成自由能变（AG）为负值，表明橙皮甙与BSA的作用过程是一个自发过程，并利用同步荧光光谱考察了橙皮甙对BSA构象的影响：

英文摘要：

The interaction behavior between hesperidinum and bovine serum albumin（BSA） in phYsiological buffer（ pH 7.4） was studied by fluorescence spectroscopy. The quenching constants were obtained at 295K, 303K, 310K and 315K. The results indicated that the fluorescence quenching mechanism for BSA through hesperidinum binding was likely a dynamic quenching process. The thermodynamic parameters, enthalpy change （AH） and entropy change （AS） were calculated to be 70.71 kJ/mol and 316.29 J/（mol·K）, respectively, which indicated that the interachon of hesperidinum with BSA was driven mainly by hydrophobic interaction. The process of binding was a spontaneous process in which Gibbs free energy change was negative. The effect of hesperidinum on the conformation of BSA was analyzed using synchronous fluorescence spectroscopy.