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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(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 was studied by studying the quenching of endogenous fluorescence of human serum albumin (HSA) by Cu (Ⅱ) and Fe (Ⅲ) The mechanism of energy transfer was obtained.The distance between Cu (Ⅰ) binding site of human serum albumin and the tryptophan residue at position 214 was 1.8nm, and the binding of Cu (Ⅱ) and Fe (Ⅲ) to HSA difference.