Abstract：The interaction between salicylic acid and bovine serum albumin has been studied by fluorescence spectroscopy. The results show that the quenching mechanism of the combination of bovine serum albumin with salicylic acid is a static quenching procedure, the quenching constant Ksv is 1.097×104 (mol·L-1)-1, and the equilibrium constant is 7.377×104. The number of binding sites is 1 and it is a strong one. When the ratio of molar concentration of salicylic acid to bovine serum albumin is lower than 1∶1, it binds to Trp residue first but it doesn’t result in any microenvironment changes of Trp residue. The binding distance between salicylic acid and bovine serum albumin and the energy transfer efficiency were obtained based on the theory of Frester spectroscopy energy transfer.
Key words：Fluorescence spectroscopy;Salicylic acid;Bovine serum albumin
肖厚荣，盛良全，施春华，徐小龙，解永树，刘清亮* . 水杨酸与牛血清蛋白相互作用的荧光光谱研究[J]. 光谱学与光谱分析, 2004, 24(01): 78-81.
XIAO Hou-rong, SHENG Liang-quan, SHI Chun-hua, XU Xiao-long, XIE Yong-shu, LIU Qing-liang . Fluorescence Study on the Interaction of Salicylic Acid and Bovine Serum Albumin . SPECTROSCOPY AND SPECTRAL ANALYSIS, 2004, 24(01): 78-81.
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