花旗松素与牛血清白蛋白相互作用的光谱和电化学

采用紫外光谱法、荧光光谱法和循环伏安法，研究了牛血清白蛋白(BSA)与花旗松素（taxifolin）的相互作用。 用荧光法和循环伏安法测得花旗松素与BSA的结合常数K分别为1.3×106和1.6×106 L/mol，结合位点数均接近1.3。花旗松素对牛血清白蛋白是静态猝灭。BSA荧光强度的降低与花旗松素浓度在一定范围内呈线性关系，其线性范围为6.00×10-7~2.00×10-5 mol/L，检出限为2.00×10-7 mol/L。花旗松素氧化峰电流的下降与BSA浓度在一定范围内呈线性关系，其线性范围为7.00×10-7~1.00×10-4 mol/L，检出限为3.00×10-7 mol/L。用于合成样品中花旗松素和BSA的测定，结果满意。

Studies on the Interaction of Taxifolin and Bovine Serum Albumin by Spectroscopic and Voltammetric Methods

The interaction between taxifolin and bovine serum albumin(BSA) was investigated using UV, fluorescence and cyclic voltammetry. The binding constants of 1.3×106 L/mol and 1.6×106 L/mol can be calculated from the data obtained from fluorescence quenching experiments and cyclic voltammetry, respectively. And the number of the binding sites is nearly 1.3. The interaction of bovine serum albumin with taxifolin is a single static quenching procedure. The fluorescence intensity changes of BSA correlate linearly with the concentrations of taxifolin, and the linear range is 6.00×10-7~2.00×10-5 mol/L with a limit of detection at 2.0×10-7 mol/L. The redox peak current of taxifolin is proportional to the concentration of BSA. The linear range is 7.00×10-7~1.00×10-4 mol/L with a limit of detection at 3.0×10-7 mol/L. This method has been applied to the determination of BSA and taxifolin with satisfactory results.