摘要
应用荧光光谱法研究不同离子强度、温度、酸度条件下,血竭总黄酮（tFSD）与血清白蛋白的相互作用。研究表明：tFSD能不同程度地猝灭牛血清白蛋白（BSA）和人血清白蛋白（HSA）的荧光强度,BSA的荧光强度猝灭得更显著;在288～298K间,随着温度的升高,BSA-tFSD和HSA-tFSD两荧光体系的猝灭程度降低,推测tFSD对BSA、HSA的荧光猝灭作用不是动态猝灭,而是静态猝灭;在pH6.0～pH10.0间,随着pH的提高,tFSD对BSA（HSA）的荧光猝灭程度上升,说明tFSD与BSA（HSA）之间以非静电作用为主,并形成了不发荧光的复合物。
The interaction of total flavones in sanguis draconi（tFSD） and serum albumin was investigated by fluorescence spectroscopy under varying ionic strength,temperature and acidity.The fluoresceuse of bovine serum album（BSA） and human serum album（HSA） quenched reguliary with the addition of tFSD,and the change for BSA was more prominent than that for HSA.From 288 K to 298 K,the fluorescence quenching of BSA（HSA）-tFSD system was weakened with increasing temperature,indicating that the florescence quenching of proteins was static instead of dynamic.The fluorescence quenching of BSA（HSA）-tFSD system was enhance when the pH was raised from 6.0 to 10.0,showing that tFSD and BSA（HSA） formed complexes without fluorescence emission and electrostatic interaction did not play a major role in stabilizing the complex.
出处
《化学世界》
CAS
CSCD
北大核心
2008年第7期401-404,443,共5页
Chemical World
基金
国家民委院校科研基金(MJY00004)
关键词
血竭总黄酮
血清白蛋白
荧光
猝灭
total flavones in sanguis draconi（tFSD）
serum albumin
fluorescence
quench
