中文摘要：

应用荧光光谱法研究了6-苄氨基嘌呤（6-BA）与牛血清白蛋白（BSA）相互作用的荧光特性。测得了6-BA与BSA在10、27、40℃温度下的结合常数KA为：0.21×10^5、1.37×10^5、5.53×10^5L/mol,结合位点数n为：1.0、1.2、1.3。6-BA对BSA内源荧光的猝灭机理主要为静态猝灭,6-BA主要以疏水作用与BSA相互作用,BSA的荧光主要源于色氨酸残基,6-BA对BSA的构象有影响。

英文摘要：

The interactions between 6-benzyl-amino-purine and bovine serum albumin was studied by fluoremetry. The binding constants KA（10 ℃： 0.21 × 10^5, 27 ℃： 1.37 × 10^5, 40℃： 5.53 ×10^5） and binding sites n （10℃： 1.0, 27℃： 1.2, 40℃： 1.3） were measured at different temperatures. The experimental results revealed that 6- benzyl-amino-purine had strong ability to quench the intrinsic fluorescence of BSA and the interactions was verified to be the static quenching procedure. According to themodynamic parameters, the main interaction is hydrophobic force.