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邻菲咯啉合铜配合物与牛血清白蛋白的相互作用
引用本文:黄钰婷,任祥祥,刘海峰,乐学义.邻菲咯啉合铜配合物与牛血清白蛋白的相互作用[J].化学研究,2009,20(2):37-40.
作者姓名:黄钰婷  任祥祥  刘海峰  乐学义
作者单位:华南农业大学理学院应用化学系,广东,广州,510642
基金项目:广东省自然科学基金重点项目 
摘    要:利用荧光光谱法研究了两种配合物,Cu(phen)(L-Phe)(H2O)]ClO4(1)(L-Phe为L-苯丙氨酸根)和Cu(phen)(Gly)(H2O)]ClO4·2.5H2O(2)(Cly为甘氨酸根),与牛血清白蛋白(BSA)的相互作用。结果表明,牛血清白蛋白的荧光强度随着配合物浓度的增大而逐渐降低,配合物(2)与BSA的结合常数大于配合物(1)与BSA的结合常数,牛血清白蛋白对配合物的结合位点数为1,荧光猝灭作用机理为静态猝灭.

关 键 词:Cu(Ⅱ)配合物  1  10-邻菲咯啉  氨基酸  牛血清白蛋白  荧光光谱

Interaction Between 1,10-Phenanthroline Aminoacidato Copper(II) Complexes and Bovine Serum Albumin
HUANG Yu-ting,REN Xiang-xiang,LIU Hai-feng,LE Xue-yi.Interaction Between 1,10-Phenanthroline Aminoacidato Copper(II) Complexes and Bovine Serum Albumin[J].Chemical Research,2009,20(2):37-40.
Authors:HUANG Yu-ting  REN Xiang-xiang  LIU Hai-feng  LE Xue-yi
Institution:( Department of Applied Chemistry, South China Agricultural University, Guangzhou 510642, Guangdong, China)
Abstract:The binding interaction between the complexes,ClO4(1)(L-Phe=L-phenylalanine, ClO4·2.5H2O(2)(Gly =glycine) and bovine serum albumin(BSA) was investigated by fluorescence spectroscopy technique.The results showed that the fluorescence strength of BSA decreased with the increase of the complex concentration,and the binding constant K for complex(2) is bigger than that for complex(1),and the binding site number of BSA to the complexes is 1.
Keywords:copper(Ⅱ)complex  1  10-phenanthroline  amino acid  bovine serum albumin  fluorescence spectroscopy
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