【摘要】 应用荧光光谱研究了胆红素(BR)及铜与牛血清白蛋白(BSA)的相互作用机制。结果表明,BSA-BR的光谱图在有Cu2+存在时,发生了明显的变化,表明能够形成BSA-Cu2+-BR三元络合物。胆红素主要以静态猝灭的方式使得牛血清白蛋白荧光强度显著降低,胆红素和牛血清白蛋白主要凭借范德华力和氢键作用结合。测定了BSA-BR、BSA-Cu2+以及BSA-Cu2+-BR体系的组成和结合常数。探讨了铜离子及胆红素与牛血清白蛋白间的结合反应,阐明了铜离子浓度对胆红素和蛋白质结合的影响。更多还原

【Abstract】 The interaction of bilirubin,Cu2+ and bovine serum albumin(BSA) was studied using fluorescence spectroscopy.The fluorescence spectrum of BSA-BR changed apparently in the presence of Cu2+,which showed that BSA-Cu2+-BR ternary complex had been formed.The fluorescence intensity of bovine serum albumin could be quenched by bilirubin by static quenching style.The binding was mainly enthalpy-driven and the entropy was unfavorable for it,van der Waals interactions and hydrogen bonds played major role in the reaction.In addition,the reaction for bovine serum albumin between Cu2+ and bilirubin was discussed.The compositions and resultant constants of the BSA-BR,BSA-Cu2+ and BSA-Cu2+-BR systems were determined.The effect of concentration of Cu2+ on the binding of bilirubin and bovine serum albumin was illustrated.更多还原