中文摘要：

应用荧光光谱法研究了甲苯胺蓝（TB）与牛血清白蛋白（BSA）相互作用的光谱特性．测定了TB与BSA在20℃，30℃和40℃3个温度下的结合常数K^分别为8．94×103，1．75×10^4，1．74×10^4L／mol，结合位点数n分别为0．66，0．71和0．93．实验表明：TB与BSA的荧光猝灭主要为静态猝灭；利用Gibbs-Helmholtz方程计算得到热力学参数△H为49．416kJ，△S为244．876J·mol^-1·K^-1，探讨了它们的相互作用机理，结果表明TB主要以氢键作用力与BSA相互作用；应用同步荧光技术研究了TB对BSA构象的影响．

英文摘要：

By using fluorescence spectroscopy, the spectral characteristics of the interaction for toluidine blue （TB） and bovine serum albumin （BSA） have been investigated. The combination constant KA for TB and BSA at 20 ℃, 30 ℃ and 40 ℃ was 8.94 ×103, 1.75 × 104,1.74 × 104 L/mol; binding sites were 0.66, 0. 71,0.93 respectively. Experimental results showed that TB and the BSA fluorescence quenching is mainly due to static quenching. The thermodynamic parameters ΔH calculated by using Gibbs-Helmholtz equation is 49. 416 kJ, ΔS is 244. 876 J-1 mol-1. K-1. The interactions between TB and BSA is ascribed to the hydrogen bonding. The effect on the conformation of BSA indued by TB was studied by synchronous fluorescence.