荧光光谱和紫外光谱法研究Cu(Ⅱ)、Cd(Ⅱ)与血清白蛋白的作用  

Study on the Interaction between Cu(Ⅱ),Cd(Ⅱ) and Serum Albumin by Fluorescence and Ultraviolet Spectroscopy

作　　者：梁彦秋[1] 刘婷婷[2] 费洪博[2] 邓斌[2] 孙鹏[2] 臧树良[1] 

机构地区：[1]华东师范大学化学系 [2]辽宁大学化学系,沈阳110036

出　　处：《分析科学学报》2007年第3期303-306,共4页Journal of Analytical Science

基　　金：国家自然科学基金(No.20271024)

摘　　要：本文采用荧光光谱法研究了Cu(Ⅱ)和Cd(Ⅱ)在血清白蛋白上的结合位点,并用紫外光谱法研究了二者与血清白蛋白之间的结合竞争。研究结果表明:Cu(Ⅱ)和Cd(Ⅱ)对血清白蛋白的色氨酸残基和酪氨酸残基均具有荧光猝灭作用,Cu(Ⅱ)的猝灭程度远远强于Cd(Ⅱ)。Cu(Ⅱ)只与214位色氨酸残基发生作用,而Cd(Ⅱ)与牛血清白蛋白的214位和135位色氨酸残基均发生作用。Cu(Ⅱ)与Cd(Ⅱ)同时存在时Cu(Ⅱ)与牛血清白蛋白的结合占主导作用。The interaction of Cu（ Ⅱ ） and Cd（ Ⅱ ） with serum albumin was investigated by fluorescence spectroscopy and the competition between Cu （ Ⅱ ） and Cd （ Ⅱ ） was analyzed by absorption spectra. Results showed that fluorescence emitted by tyrosyl and tryptophanyl could be quenched by Cu（ Ⅱ ） and Cd（ Ⅱ ）. The quenching resulted from Cu（ Ⅱ ） was much stronger than that resulted from Cd （ Ⅱ ）. Cu（Ⅱ ） only bound to the Trp214 in ⅡA subdomain, but Cd（ Ⅱ ） interacted with both Trp214 in ⅡA subdomain and Trp135 in IB subdomain of bovine serum albumin. The binding of Cu（ Ⅱ ） with bovine serum albumin predominated in the presence of both Cu（ Ⅱ ） and Cd（ Ⅱ ）.

关 键 词：Cu(Ⅱ) Cd(Ⅱ) 血清白蛋白 荧光光谱 紫外光谱 

分 类 号：O657.3[理学—分析化学]