光谱学与光谱分析 |
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Fluorescence Study on the Interaction of Salicylic Acid and Bovine Serum Albumin |
XIAO Hou-rong, SHENG Liang-quan, SHI Chun-hua, XU Xiao-long, XIE Yong-shu, LIU Qing-liang |
Department of Chemistry, University of Science and Technology of China, Hefei 230026,China |
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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.
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Received: 2002-09-13
Accepted: 2003-01-20
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Corresponding Authors:
LIU Qing-liang
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Cite this article: |
XIAO Hou-rong,SHENG Liang-quan,SHI Chun-hua, et al. Fluorescence Study on the Interaction of Salicylic Acid and Bovine Serum Albumin [J]. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2004, 24(01): 78-81.
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URL: |
http://www.gpxygpfx.com/EN/Y2004/V24/I01/78 |
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