以Eu^(3+)为探针研究吸附状态蛋白质的金属离子结合性质  

Using Eu^(3+) as a Probe to Investigate the Metal Ion Binding Activity of Adsorbed Proteins

作　　者：荣志江 孙红艳[1] 郝春燕[1] 张跃忠 杨斌盛[2] RONG Zhijiang;SUN Hongyan;HAO Chunyan;ZHANG Yuezhong;YANG Binsheng(School of Chemical and Biological Engineering,Taiyuan University of Science and Technology,Taiyuan 030024,China;Institute of Molecular Science,Shanxi University,Taiyuan 030006,China)

机构地区：[1]太原科技大学化学与生物工程学院,山西太原030024 [2]山西大学分子科学研究所,山西太原030006

出　　处：《山西大学学报（自然科学版）》2021年第6期1138-1145,共8页Journal of Shanxi University(Natural Science Edition)

基　　金：国家自然科学基金(21571117,31401319);山西省重点研发计划项目(201903D221066);山西省高等学校科技创新项目(2019L0655);山西省自然科学基金(201901D211310);太原科技大学博士科研基金(20162018)。

摘　　要：文章应用循环伏安法比较了铜伴侣蛋白(CopC)、牛血清白蛋白(BSA)和N端中心蛋白(N-EoCen)的电极吸附作用,并进一步以Eu^(3+)为探针研究了其与吸附状态蛋白质的相互作用。研究发现CopC基本不吸附,而BSA和N-EoCen具有较强的吸附性,经拟合得到的BSA一级吸附速率常数[(0.056 9±0.004 2)s^(-1)]明显大于N-EoCen[(0.012 8±0.001 3)s^(-1)]。以Eu^(3+)为探针的电化学滴定实验显示与Eu;对N-EoCen的S型滴定曲线完全不同,Eu;与BSA的滴定曲线呈弧线型上升,计算可得Eu^(3+)在BSA结合位点数n为1,表观结合常数K=4.26×10^(6)L·mol^(-1)。实验证明吸附状态BSA和N-EoCen依然保留了其与金属离子的结合功能。The adsorption of copper companion protein(CopC), bovine serum albumin(BSA) and N-terminal centrin(N-EoCen) on electrodes was compared by cyclic voltrometry, and the interaction between BSA, N-Eocen and Eu^(3+) was further investigated. It is found that CopC is basically non-adsorptive, while BSA and N-EoCen have strong adsorbability. The fitted BSA first-order adsorption rate constant [(0. 056 9 ± 0. 004 2) s^(-1)]is significantly greater than N-EoCen [(0. 012 8 ± 0. 001 3) s^(-1)]. The electrochemical titration experiment using Eu;as a probe showed that the S-type titration curve of N-EoCen was completely different from an arc increased shape of BSA. The number of binding sites of Eu^(3+) to N-EoCen is 1 and the apparent binding constant K=4. 26×10^(-6)L·mol^(-1).The experimental results proved that BSA and N-EoCen in adsorption state had retain their binding function with metal ions.

关 键 词：CopC 循环伏安 BSA 吸附性 

分 类 号：O647[理学—物理化学]