摘要
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(Ⅰ)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.
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.
出处
《化学学报》
SCIE
CAS
CSCD
北大核心
1999年第2期161-165,共5页
Acta Chimica Sinica
基金
国家自然科学基金(29271025)
广西自然科学基金(青9453001)
关键词
荧光猝灭
人血清白蛋白
铜离子
铁离子
quenching fluorescence, human serum albumin, binding sites, non-radiative energy transfer
