芦丁与胰蛋白酶相互作用的光谱性质研究  

Spectroscopic Study on the Interaction between Rutin and Trypsin

作　　者：邓静[1] 贾旭[1] 杨娟[1] 刘雯[1] 裘晓丹[1] 刘克武[1] 

机构地区：[1]四川大学生命科学学院教育部生物资源与生态环境重点实验室,成都610064

出　　处：《天然产物研究与开发》2006年第6期968-971,共4页Natural Product Research and Development

摘　　要：利用紫外光谱和荧光光谱研究了芦丁和胰蛋白酶的相互作用机制。结果表明,生理pH 7.40条件下芦丁使胰蛋白酶的紫外吸收峰增强,特征荧光峰淬灭。并利用荧光淬灭反应测得芦丁和胰蛋白酶之间结合常数KA=6.8786×104(mol/L)-1,结合位点数n=1.0173。The interaction between mtin and trypsin has been studied by ultraviolet（UV） absorption spectra and fluorescence spectra. The result shows that rutin treatment led to the increasing of UV absorption and the quenching of intrinsic fluorescence of trypsin in physiological condition （pH 7.40 ）. With fluorescence quenching method, the binding constant KA was found to be 6.8786 × 10^4（mol/L）^-1 and the number of binding site n was 1.0173.

关 键 词：芦丁 胰蛋白酶 荧光光谱 紫外光谱 

分 类 号：Q518.1[生物学—生物化学] R969.1[医药卫生—药理学]