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中文摘要：
应用荧光和紫外光谱法研究了茶碱（TH）与牛血清白蛋白（BSA）相互作用的光谱特性.测定了TH与BSA在10℃、28℃和40℃温度下的结合常数KA分别为1.96×104L/mol、3.80×10^4L/mol,1.57×10^5L/mol,结合位点数n分别为1.0,1.1,1.2.实验表明：TH对BSA内源荧光的猝灭机理主要为静态猝灭;计算得到热力学参数H为26.229KJ/mol,S为174.809J/（mol·K）.TH主要以疏水作用力与BSA相互作用;同步荧光技术研究表明,BSA的荧光主要源于TH色氨酸残基,表明TH对BSA的构象有影响.
英文摘要：
The interactions between Theophylline and bovine serum albumin（BSA） were studied by fluorescence and UV absorption spectroscopy.The binding constants KA（1.96×104,3.80×104,1.57×105） and binding sites n（1.0,1.1,1.2） were measured at different temperatures of 10 ℃,28 ℃ and 40 ℃.The results revealed that Theophylline has strong ability to quench the intrinsic fluorescence of BSA and the interactions has been verified as static quenching procedure.According themodynamic parameters the acting forces were determined to be hydrophobic force.
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