Abstract:The characteristics of the binding reaction of titan yellow(TY) with bovine serum albumin(BSA) were studies by fluorescence and ultraviolet-visible absorption spectra. It was shown that TY has a powerful ability to quench the fluorescence intensity of BSA. The fluorescence quenching data were analyzed according to Stern-Volmer equation and Line weaver-Burk equation and the binding constant, and thermodynamic parameters were obtained. According to the thermodynamic parameters the main sorts of binding force were determined. The binding distance and energy transfer efficiency between the donor (BSA) and the acceptor (TY) were obtained by Frster’s non-radiative energy transfer mechanism. It is confirmed that the combination reaction of TY with BSA is a single static quenching process, and their interaction may be interpreted with energy transfer mechanism.
毕欣颖,迟燕华*. 达旦黄与牛血清白蛋白结合的热力学研究[J]. 光谱学与光谱分析, 2006, 26(11): 2097-2100.
BI Xin-ying,CHI Yan-hua*. Studies on the Thermodynamics and Mechanism of Combination Reaction of Titan Yellow with Bovine Serum Albumin. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2006, 26(11): 2097-2100.