摘要
运用荧光光谱、紫外吸收光谱探讨了Fe3+对灯盏花素(BR)与牛血清白蛋白(BSA)相互作用的影响;从Fe3+与BSA的静电作用、配位结合以及Fe3+与BR的配位作用等方面分析了影响BR与BSA相互作用的因素.结果表明,Fe3+不改变BSA与BR的作用机制,但使得二者结合的猝灭常数、结合常数及结合位点数减小.
The effect of ferric iron (Fe3+ ) on the interaction between breviscapinun (BR) and bovine serum albumin (BSA) was investigated by means of fluorescence spectrometry and ul- traviolet absorption spectrometry. The factors influencing the interaction between BR and BSA were analyzed in relation to the static action and coordination of Fe3+ and BSA as well as the coordination action between Fe3+ and BR. Results indicate that Fea+ does not change the mech- anism for BSA to interact with BR, but it contributes to reduce the quenching constant, bind ing constant and binding sites of BSA with BR.
出处
《化学研究》
CAS
2013年第3期224-227,共4页
Chemical Research
基金
山东省高等学校科技计划资助项目(J12LD55)
滨州医学院科研专项资助项目(BY2009KJ30)