摘要
通过研究Co2+对人血清白蛋白内源荧光的辞灭,探讨了Co2+对人血清白蛋白的荧光碎灭机理,并得到了人血清白蛋白第一类Co(Ⅱ)结合部位与214位色氨酸残基间的距离.
The interaction of Co balt(I ) ion with human serum albumin had been inves tl-g4ted by the fluores cence spectroscpy. The results showed that Co2+ may bind to HSA andthat the fluores cence of HSA may be quenched by non radiative energy transfer,ln mecha-nism of Forster non radiative energy transfer,the distance between Trp-214 residue and thefirst binding site was calculated.
基金
国家自然科学基金
广西省自然科学基金
关键词
人血清白蛋白
非辐射能量转移
荧光光谱
钴离子
haman serum albumin
non-radiative energy transfer
fluorescence spectros copy
binling site
Co balt (Ⅱ)