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化学学报
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化学学报 ›› 1999, Vol. 57 ›› Issue (2): 161-165. 上一篇    下一篇

研究论文

Cu(II), Fe(III)与人血清白蛋白相互作用的荧光光谱研究

梁宏;邢本刚;吴庆轩;罗济文;周永洽;申泮文   

  1. 广西师范大学化学系.桂林(541004);南开大学化学系.天津(300071)
  • 发布日期:1999-02-15

Study on the interaction of human serum albumin with Cu(II) and Fe (III) by fluorescence method

Liang Hong;Xing Bengang;Wu Qingxuan;Luo Jiwen;Zhou Yongqia;Shen Panwen   

  1. Guangxi Normal Univ, Dept Chem.Guilin(541004);Nankai Univ, Dept Chem. Tianjin(300071)
  • Published:1999-02-15

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通过研究Cu(II),Fe(III)对人血清白蛋白(HSA)内源荧光的猝灭,探讨了Cu(II),Fe(III)与人血清白蛋白的结合机理。基于Forster非辐射能量转移机理。获得了人血清白蛋白第一类Cu(II)结合部位与214位色氨酸残基间的距离为1.8nm,并讨论了Cu(II),Fe(III)与HSA结合的差异。

关键词: 铜, 铁, 血清蛋白, 荧光猝灭, 清蛋白, 荧光谱法, 相互作用

The mechanism of Cu(II) and Fe(III) binding to human serum albumin has been studied through the quenching of the intrinsic fluorescence of HSA. Based on Forster non-radiative energy transfer theory, the distance (1.8nm) between Trp-214 residue of HSA and the first class of binding site was determined. The different interaction of Cu(II), Fe(III) with HSA has also been discussed in this paper.

Key words: COPPER, IRON, SERUM PROTEINS, ALBUMINE, INTERACTIONS

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