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连翘苷与牛血清白蛋白的相互作用
引用本文:张玉霖,陈莉.连翘苷与牛血清白蛋白的相互作用[J].咸宁医学院学报,2014(6):475-477.
作者姓名:张玉霖  陈莉
作者单位:湖北科技学院药学院,湖北咸宁437100
摘    要:目的研究连翘苷与牛血清白蛋白(BSA)的相互作用。方法采用荧光光谱法测定不同温度(302K、310K)时连翘苷对BSA的猝灭光谱,根据Stern-Volmer方程求得302K、310K时连翘苷与BSA相互作用的荧光猝灭速率常数kq,并计算二者的结合位点数n。结果 302K、310K时连翘苷与BSA相互作用的荧光猝灭速率常数kq分别为1.26541×10^12L/(mol·s),1.24196×10^12L/(mol·s),二者的结合位点数n分别为0.9410、1.0395。结论连翘苷对BSA荧光的猝灭属静态猝灭,两者之间形成了一个结合位点。

关 键 词:荧光光谱法  连翘苷  牛血清白蛋白  静态猝灭

Study of Interaction between Phillyrin and Bovine Serum Albumin
ZHANG Yu-lin,CHEN Li.Study of Interaction between Phillyrin and Bovine Serum Albumin[J].Journal of Xianning Medical College,2014(6):475-477.
Authors:ZHANG Yu-lin  CHEN Li
Institution:( Department of Pharmacology, Hubei University of Science and Technology, Xianning Hubei 437100, China)
Abstract:Objective To study the interaction between phillyrin and bovine serum albumin through the fluorescence spectroscopy. Methods The fluorescence quenching spectra of BSA was measured with treatment of phillyrin at the temperature of 302 K and 310 K. The fluorescence quenching rate constants kqand the combination n of interaction between BSA and phillyrin were calculated according to the stern-Volmer equation. Results Fluorescence quenching rate constants kqof BSA were 1. 26541 × 10^12 L /( mol·s) and 1. 24196 × 10^12 L /( mol·s) with treatment of phillyrin at the temperature of 302 K and 310 K. And the number of binding sites n were 0. 9410 and 1. 0395. Conclusion Fluorescence quenching of BSA induced by phillyrin was static quenching and there was a binding site between BSA and phillyrin.
Keywords:Fluorescence spectrometry  Phillyrin  Bovine serum albumin  Static quenching
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