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通过荧光光谱法、紫外吸收分光光度法,研究了BSA与茜素黄GG的相互作用。在pH=6.26的Tris-HCI缓冲溶液中,牛血清白蛋白与茜素黄GG相互作用,荧光光谱发生猝灭,其猝灭程度与茜素黄GG用量含量成正比。运用摩尔比法、双倒数法计算了相互作用的结合常数,基于Foerster非辐射能量转移理论估算了牛血清白蛋白与茜素黄GG之间的结合距离r=3.57nm。同步荧光法研究了茜素黄GG加入对BSA构象的影响。
The interaction between BSA and alizarin yellow GG was studied by fluorescence spectroscopy and ultraviolet absorption spectrophotometry. In pH = 6.26 Tris-HCI buffer solution, bovine serum albumin and alizarin yellow GG interaction, fluorescence quenching, the degree of quenching and alizarin yellow GG content is proportional to the content. The binding constants of interactions were calculated by the molar ratio method and the double reciprocal method. The binding distance between bovine serum albumin and alizarin yellow GG was estimated based on Foerster’s theory of non-radiative energy transfer (r = 3.57 nm). The effect of alizarin yellow GG on the conformation of BSA was studied by synchronous fluorescence method.