摘要
在pH=4．0的Britton-Robinson（B-R）缓冲体系中，应用循环伏安法、示差脉冲伏安法和紫外光谱法对大黄酚与牛血清白蛋白（BSA）相互作用的电化学／光谱性质进行研究．结果表明，二者结合生成了一种非电活性的超分子化合物．BSA的存在导致大黄酚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．线性范围为5．0×10^-6～1．0×10^-7mol／L，检出限为3×10^-7mol／L．
In pH = 4.0 Britton-Robinson （B-R） buffer solution, eleetrochemical/spectral properties of the interaction between chrysophanol and bovine serum albumin （BSA） were studied by using CV, differential pulse voltammetry （DPV） and UV. The results showed that Chrysophanol 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 chrysophanol decreased 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^-7 mol/L,and the detection limit was 3×10^-7 mol/L.
出处
《分子科学学报》
CAS
CSCD
2008年第6期411-415,共5页
Journal of Molecular Science
基金
黑龙江省自然科学基金资助项目(B200609)
黑龙江省教育厅科技项目(10541221)
佳木斯大学科技项目(L2007-89)
黑龙江省教育厅重点实验室项目
关键词
大黄酚
牛血清白蛋白
电化学
光谱
chrysophanol
bovine serum albumin
electrochemistry
spectrum
