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通过紫外-可见吸收光谱法和荧光光谱法在近生理条件下研究双酚A对牛血清白蛋白的毒性作用。实验结果表明,双酚A溶液对牛血清白蛋白有荧光猝灭作用,猝灭机理为静态猝灭,二者的结合常数为2.541 61×103,结合位点数为0.655 931。紫外可见光谱的结果说明双酚A可以使牛血清白蛋白的结构发生变化从而显示其毒性效应。
The toxicity of bisphenol A to bovine serum albumin (BSA) was investigated by UV-Vis absorption spectroscopy and fluorescence spectroscopy under near physiological conditions. The experimental results show that the bisphenol A solution has a fluorescence quenching effect on bovine serum albumin and the quenching mechanism is quiescent quenching. The binding constants of the two are 2.541 61 × 103 and the number of binding sites is 0.655 931. UV-visible spectroscopy results suggest that bisphenol A can change the structure of bovine serum albumin to show its toxic effects.