中文摘要：

利用荧光光谱、紫外吸收光谱法研究了香豆素-3-羧酸与牛血清白蛋白（ BSA ）的相互作用．结果表明：香豆素-3-羧酸对BSA的荧光猝灭为静态猝灭，香豆素-3-羧酸与BSA 1∶1结合形成复合物，结合常数与结合位点分别为3．21×104 L· moL－1，0．9746（298 K）和2．00×104 L· moL－1，0．9495（310 K），两者之间的作用力以氢键和范德华力为主．同步荧光光谱表明，香豆素-3-羧酸与色氨酸残基发生了作用，从而使其所处的微环境发生了改变．

英文摘要：

The interaction of coumarin-3-carboxylic acid with bovine serum albumin （ BSA） was investigated by flu-orescence and UV spectroscopy .The results showed that coumarin-3-carboxylic acid could quench the intrinsic fluores-cence of BSA , and the quenching mechanism was a static quenching process .The number of binding points demonstra-ted that coumarin-3-carboxylic acid and BSA formed the complex of mole ratio 1∶1.The binding constants and the number of binding sites were determined to be 3.21 ×104 L· moL -1,0.974 6（298 K） and 2.00 ×104 L· moL-1, 0.949 5（310 K）,respectively.The driving forces were mainly hydrogen bond and Vander Waals .Synchronous spectra showed that coumarin-3-carboxylic acid binded to tryptophan residue and changed the microenvironment of tryptophan residue.