中文摘要：

本文应用荧光光谱法研究了可可碱（TB）与牛血清白蛋白（BSA）相互作用的光谱特性。测定了18℃、30℃、40℃温度下的结合常数KA分别为1．68×10^4、1．58×10^4、1．45×10^4L／mol，结合位点数咒分别为1．04、1．03、1．03。实验结果表明：TB对BSA内源荧光的猝灭机理主要为静态猝灭；热力学参数探讨其相互作用机理，TB主要以静电力与BSA相互作用；研究了TB对BSA构象的影响，BSA的荧光主要源于色氨酸残基。同时研究了Cu^2＋存在下TB与BSA的相互作用。

英文摘要：

The interactions between theobromine （TB） and bovine serum albumin （BSA） were studied by fluorescence spectroscopy. The binding constants and binding sites were measured at different temperatures. Experimental results revealed that theobromine had strong ability to quench the intrinsic fluorescence of BSA and the interactions had been verified as consistent with the static quenching procedure. According to the thermodynamic parameters, the inter acting forces were determined to be electrostatic force. The effect of various concentrations of Cu^2＋ on the binding for theobromine and bovine serum albumin was illustrated.