摘要
用荧光光谱法、紫外光谱法研究了生理条件下维生素C(Vc)与牛血清白蛋白(BSA)相互作用的光谱特性。测定了Vc与BSA在21、34℃两个温度下的结合常数KA(21℃:4.381×105L/mol,34℃:4.061×105L/mol)和结合位点数n(21℃:1.08,34℃:1.10)。结果表明:Vc对BSA有明显的猝灭作用,其方式为静态猝灭。通过热力学分析得出Vc与BSA之间主要作用力是静电引力。同步荧光分析发现Vc的存在改变了牛血清白蛋白的分子构象。
The interaction between vitamin C and bovine serum albumin（BSA） was studied by fluorescence and uhraviolet-visible absorption spectroscopy under physiological conditions. The binding constants KA （ 21 ℃ ： 4. 381 × 10^5 L · mol^-1 ,34 ℃：4. 061 × 10^5 L·mol^-1） and binding sites n（21 ℃ ：1.08,34 ℃ ： 1. 10） were measured at different tempera- tures. The results indicated that the fluorescence of BSA was strongly quenched by Vc. The quenching mechanism was a static quenching procedure. Thermodynamic analysis indicated that the electrostatic attraction played a major role in the binding of Vc to BSA. It is found that the conformation of BSA was changed in the presence of Vc by means of synchronous fluorescence analysis.
出处
《化学试剂》
CAS
CSCD
北大核心
2011年第8期697-700,共4页
Chemical Reagents
基金
山东省教育厅科技计划资助项目(J08LG15)
关键词
维生素C
牛血清白蛋白
荧光光谱法
热力学分析
vitamin C
bovine serum albumin
fluorescent spectrum
thermodynamic analysis
