摘要
用荧光光谱法和紫外吸收光谱法研究了在生理pH值条件下氨与牛血清白蛋白(BSA)的相互作用。结果表明:氨对BSA的荧光有较强的猝灭作用,该猝灭属于同时具有动态猝灭和静态猝灭特征的联合猝灭,但以静态猝灭为主。根据猝灭结果求得了不同温度下氨与BSA相互作用的结合位点数、结合常数及反应热力学参数,并据此推测它们之间主要的相互作用力为范德华力和氢键。计算出当氨与BSA处于等摩尔浓度时两种分子间的作用距离为6.3126nm,它们之间发生了非辐射能量转移。同步荧光光谱图显示,氨对BSA的构象有影响。
The Interaction between ammonia and bovine serum albumin（BSA） was studied by fluorescence Spectroscopy and ultraviolet absorbance spectroscopy at the physiological pH condition.The results showed that ammonia strongly quenched the fluorescence of BSA via a combination quenching which had the features of the dynamic and static quenching,and the main process was static quenching.The average number of binding sites,the binding constant and the thermodynamic parameters for binding ammonia to BSA at different temperatures were determined.From the result,it can be judged that the main action forces between ammonia and BSA were van der Waals force and hydrogen bond.The distance between molecules of ammonia and BSA was estimated to be 6.3126nm when mole concentrations of ammonia and BSA were same,and fluorescence energy was transferred from BSA to ammonia.Synchronous fluorescence spectra showed that ammonia could change the conformation of BSA.
出处
《光谱实验室》
CAS
CSCD
北大核心
2011年第5期2158-2162,共5页
Chinese Journal of Spectroscopy Laboratory
基金
国家科技部863课题(2006AA06Z354)
公益性行业(农业)科研专项资助项目(201003064-4
201003043-02)
公益性行业(林业)科研专项资助项目(201004037)
关键词
氨
牛血清白蛋白
相互作用
荧光光谱
紫外吸收光谱
Ammonia
Bovine Serum Albumin
Interaction
Fluorescence Spectroscopy
Ultraviolet Absorbance Spectroscopy
