在生理pH值条件下， 用荧光光谱法(FS)研究了芦丁钐配合物（rutin-Sm）与牛血清白蛋白（BSA）和人血清白蛋白（HSA）之间的结合反应。 探讨了rutin-Sm对BSA 和HSA的荧光猝灭过程的猝灭机理,　以Lineweaver-Burk双倒数方程分别计算了不同温度下rutin-Sm与BSA和HSA的结合常数（KLB）和热力学参数， 并判断rutin-Sm与BSA和HSA结合的作用力类型； 实验结果表明： rutin-Sm与BSA和HSA结合形成复合物， 导致BSA（HSA）内源性荧光猝灭是由于分子内的非辐射能量转移而引起的静态猝灭； 以Lineweaver-Burk方程计算rutin-Sm与HSA和BSA的结合常数KLB分别为： rutin-Sm-HSA, 295　K: 6.830×105 L·mol-1; 310　K: 4.665×105 L·mol-1; rutin-Sm-BSA, 295　K: 6.540×105 L·mol-1; 310　K: 3.265×105 L·mol-1； 芦丁钐配合物与BSA之间的作用力主要为范德华力、 氢键；　而与HSA之间的作用力主要为静电引力。 同时用同步荧光光谱法探讨了rutin-Sm对BSA和HSA构象的影响。 进一步证明芦丁钐配合物在体内能够被血清白蛋白存储和转运。

The binding reaction of rutin-Sm with serum albumin (SA) was investigated by the fluorescence method in physiological condition. The authors studied mainly the quenching mechanism of the fluorescence of SA by rutin-Sm, and calculation of the binding constants KLB of human serum albumin （HSA） and bovine serum albumin（BSA）with rutin-Sm by Lineweaver-Burk equation at different temperatures respectively, then obtained the thermodynamic parameters of HSA and BSA with rutin-Sm according to the calculated binding constants KLB at different temperature, meanwhile the type of binding forces of HSA and BSA with rutin-Sm was determined. The results showed that the emission spectra of BSA（HSA）in the presence and absence of rutin-Sm are different. The emission spectra of BSA（HSA）in the presence of rutin-Sm can be quenched. The quenching mechanism of rutin-Sm to SA was static quenching with non-radiation energy transfer for new complex of SA and rutin-Sm. The binding constants KLB （L·moL-1）were 6.540×105 and 3.265×105 for BSA, and 6.830×105 and 4.665×105 for HSA at 295 K and 310 K respectively. And the type of bonding forces was estimated by the calculation of thermodynamic parameters of the reaction of rutin-Sm with SA at different temperatures, and the result showed that the binding forces were mainly H-bond and Van der Waals between BSA and rutin-Sm due to the ΔH＜0 and ΔS＜0, and the main electrostatic interaction of rutin-Sm and HSA because of ΔH＜0 and ΔS＞0. The effect of rutin-Sm on the conformation of serum albumin was also studied by using synchronous fluorescence spectroscopy. Results indicated that rutin-Sm could be deposited and transported by serum protein in vivo.