D. Chuan
2006
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Journal
Journal of Shanxi University
Abstract
The binding reaction between Tetrabromofluorescein(TBF) and bovine serum albumins(BSA) in aqueous solution was studied by fluorescence and ultraviolet-visible abosorption spectra.The results indicates that the binding sites is 1.266 and the equilibrium constant K_A is 2.05×10~7 L/mol.The Stern-Volmer curve on the fluorescence of BSA quenched by series of concentrations shows good linear relationship,which illustrates the combination reaction of TBF and BSA is a single static quenching progress.The shortest binding distance(r=2.06 nm)and energy transfer efficiency(E=0.76) between donor(BSA) and acceptor(TBF) were obtained by Forster's nonradiative energy transfer mechanism.