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机构地区:[1]黑龙江中医药大学药学院,黑龙江哈尔滨150040
出 处:《化学工程师》2017年第11期23-25,19,共4页Chemical Engineer
基 金:黑龙江省科学院科学研究基金项目(XKJJ1601)
摘 要:运用荧光光谱法,分别考察了Zn^(2+)、Ca2^(2+)对槲皮素与牛血清白蛋白(BSA)相互作用的影响,两种金属离子是否影响槲皮素对BSA的荧光猝灭作用机理、槲皮素与BSA结合作用常数、结合位点数、作用力类型等。结果表明,Zn^(2+)和Ca^(2+)存在时,不改变槲皮素对BSA的荧光猝灭机理、不改变槲皮素与BSA结合作用的作用力类型、结合位点数基本不变。但Zn^(2+)存在时,会导致槲皮素对BSA的结合常数减小;Ca^(2+)存在时,会导致槲皮素与BSA的结合常数增大。说明两种离子会影响槲皮素的蛋白质结合浓度。The interaction between quercetin and bovine serum albumin (BSA) was studied in the presence of Zn^2+ or Ca^2+ by using fluorescence spectroscopy. Investigate whether the presence of Zn^2+ or Ca^2+ has an influence on the fluorescence quenching mechanism of quercetin on BSA, the binding constants between quercetin and BSA, the binding site number and the type of force. The results indicated that Zn^2+ or Ca^2+ does not change the mechanism of fluorescence quenching mechanism of quercetin on BSA, does not change the type of force between quercetin and BSA. The number of binding sites is almost unchanged. But when Zn^2+ is present, the binding constant between quercetin and BSA decreases. And when Ca^2+ is present, the binding constant between quercetin and BSA will increase. So the two ions affect the protein binding concentration of quercetin.
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