摘要
应用荧光光谱研究了岩白菜素与牛血清白蛋白（BSA）分子间的相互作用.结果表明,岩白菜素对BSA内源荧光的猝灭机制属于形成化合物所引起的静态猝灭,猝灭常数Ksv为1.905×10^4L.mol^-1;岩白菜素与BSA反应的结合常数为2.083×10^4,结合位点数为1.由热力学参数确定了岩白菜素与牛血清白蛋白的结合作用主要为静电作用.实验还发现随着岩白菜素的加入,BSA的猝灭值与岩白菜素浓度在1.5×10^-5~1.5×10^-4mol.L^-1的范围内呈良好的线性关系,检出限2.0×10^-6mol.L^-1,可用于岩白菜素的测定.
The mechanism of interaction between bergenin （BER） and bovine serum albumin （BSA） was investigated with fluorescence spectrometry. The experiments showed that the selected bergenin strongly quenched the fluorescence of protein, and this fluorescence quenching could be interpreted in terms of statistic quenching. With fluorescence quenching method, the quenching constant K was found to be 1.905 × 10^4L· mol^-1, the binding constant was found to be 2. 083 ×10^4, and the number of binding site n was 1.0. The interaction between BER and protein was attributed to the static electricity gravitation which was also confirmed by the calculation results of enthalpy and entropy for these reactions. Adding bergenin into the BSA solution results in the decrease of fluorescence intensity. The decrease of fluorescence intensity is proportional to BER concentration from 1.5 ×10^ -5 ~ 1.5 ×10^ -4mg· L^-1 The limit of the detection is 2.0 × 10^ -6 mol · L^-1 This method can be applied to the determination of BER.
出处
《化学研究》
CAS
2007年第3期87-90,共4页
Chemical Research
基金
福建省教育厅科研基金资助项目(2005K051)
福建省卫生厅青年科研基金资助项目(2005123)
关键词
荧光光谱
岩白菜素
牛血清白蛋白
fluorescence spectrometry
bergenin
bovine serum albumin
