人血清白蛋白与金属离子作用的荧光光谱研究

FLUORESCENCE QUENCHING STUDIES ON THE ACTION OF METAL IONS WITH HUMAN SERUM ALBUMIN

通过金属离子对人血清白蛋白内源荧光的猝灭,探讨了金属离子Cu^(2+),Mn^(2+),Ni^(2+),Co^(2+),Cr^(3+)等与人血清白蛋白的结合;基于Forster无辐射能量转移机理,得出了人血清白蛋白第一类Cu^(2+)结合部位与214位色氨酸残基间的距离。

In the paper, the action of metal ions on the human serum albumin had been investigated by fluorescence quenching method. The results showed that Cu^(2+), Mn^(2+), Co^(2+), Cr^(3+),Eu^(3+),Ni^(2+) may bind to human serum albumin and that the fluorescence of human serum albumin may be quenched by nonradiative energy transfer. In terms of Forster type dipoledipole nonradiative energy transfer the distance between the Trp-214 and the bound Cu^(2+) in the first copper-binding site was calculated and found to be about 1.20nm.