荧光猝灭法研究刚果红与人血清白蛋白的相互作用

在0.050mol.L-1的Tris-HCl缓冲介质中（内含0.10mol.L-1NaCl）,用荧光光谱法在模拟生理条件下,研究了刚果红与人血清白蛋白的相互作用。在不同温度和不同pH值下,刚果红对人血清白蛋白的荧光猝灭作用为静态猝灭机制。根据荧光猝灭双倒数曲线和位点结合模型计算出的刚果红与人血清白蛋白之间的结合常数相当,且结合常数与结合位点数都随温度升高而减小,在pH7.4时最大。根据热力学方法讨论了两者间主要的作用力类型,由重叠积分面积,得出两者的结合距离。由此可见,刚果红与人血清白蛋白之间有很强的结合作用。

Interaction Between Congo Red and Human Serum Albumin by Fluorescence Quenching Method

At 0.050mol·L-1 Tris-HCl buffer medium（containing 0.10mol·L-1 NaCl）,the interaction between congo red and human serum albumin（HAS） was studied by fluorescence spectroscopy under simulated physiological conditions.At different temperatures and different pH values,the fluorescence quenching effect of congo red on human serum albumin was a static quenching mechanism.The binding constants of congo red and human serum albumin calculated by fluorescence quenching-double reciprocal curves and site binding model are comparable.The binding constant and binding sites are decreased with the increase of temperature,and reach the largest values at pH 7.4.The main types of force were discussed acccoding to thermodynamic method.The binding distance was obtained by the overlap integral area.This method shows that congo red and human serum albumin have a strong interactions.