人血清蛋白与重金属离子相互作用的荧光光谱  被引量:2

Fluorescence spectra on interaction between human serum albumin and heavy metal ions

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作  者:赵淑慧[1] 徐鑫伟 陈华才[1] 

机构地区:[1]中国计量大学光学与电子科技学院,浙江杭州310018

出  处:《中国计量学院学报》2016年第3期291-294,共4页Journal of China Jiliang University

基  金:浙江省家具检测技术研究重点实验室开放基金资助项目(No.2016J06)

摘  要:通过荧光光谱技术研究重金属离子与人血清蛋白(HSA)间的结合作用机制.测量了人血清蛋白与重金属离子Pb2+,Cr6+,Cu2+在290K和300K温度下相互作用的荧光光谱,建立猝灭方程.3种重金属离子与HSA的猝灭均属于静态猝灭,根据静态猝灭方程Stern-Volmer分别计算出290K和300K温度下HSA与3种重金属离子相互作用结合常数,290K下结合常数Ksv分别为1.731×103,5.580×103,4.461×104;300K下结合常数Ksv分别为1.354×103,5.418×103,4.461×104,结合位点数分别为1.237,1.528,0.506.证明了重金属离子Pb2+,Cr6+,Cu2+与HSA之间的相互作用是自发的.The interactions between Pb2+,Cr6+,Cu2+and human serum albumin(HSA)were studied by using the fluorescence spectroscopy.The fluorescence spectra of HSA with heavy metal ions were measured under 290 K and 300 K,and the quenching equations were established.The interactions between the three heavy metal ions and HSA were static quenching.According to the static quenching equation Stern-Volmer,we can calculated the binding constant Ksv and the binding sites.The binding constants Ksv of the three heavy ions were 1.731×10^3,5.580×10^3,4.461×10^4under 290 K,and 1.354×10^3,5.418×10^3,4.461×10^4under300K,respectively.The binding sites of the three heavy ions were 1.237,1.528,0.506.The interaction between the heavy metal ions Pb2+,Cr6+,Cu2+and HSA was proved to be spontaneous.

关 键 词:人血清蛋白 重金属离子 荧光光谱 静态猝灭 

分 类 号:TN253[电子电信—物理电子学]

 

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