大黄素甲醚和牛血清蛋白相互作用的电化学性质研究

Interaction between rheochrysidin and bovine serum albumin:A electrochemical study

在pH4.0的Britton-Robinson（B-R）缓冲体系中,应用循环伏安法和示差脉冲伏安法对大黄素甲醚与牛血清白蛋白（BSA）相互作用的电化学性质进行研究。结果表明,二者结合生成了一种非电活性的超分子化合物,同时对结合反应的机理进行了探讨。BSA的存在导致大黄素甲醚氧化还原峰电流降低,峰电位基本不变,峰电流的下降值同所加入的BSA浓度在一定范围内呈线性关系。线性范围5.0×10-6-1.0×10^-7mol/L,检出限3×10^-7mol/L。

In pH 4.0 Britton--Robinson（B-R） buffer solution, electrochemical property of me interaction between rheochrysidin and bovine serum albumin （BSA） was studied by using cyclic voltammetry（CV） and dif- ferential pulse voltammetry（DPV）. The results showed that rheochrysidin and bovine serum protein generated a electrochemical inactive super-molecular compound. At the same time, the combined reaction mechanism was discussed. The redox peak current of rheochrysidin declined and the electric potential changed little as a result of the presence of BSA. The relationship between the peak current decline and the concentration of BSA was linear in the range of 5.0 × 10-6-1.0 × 10 ^-7mol/L, and the detection limit was 3 ×10^-7mol/L.