秋水仙碱与胰蛋白酶相互作用的光谱性质研究  

Spectra Study on the Interaction between Colchicine and Trypsin

作　　者：赵巍[1] 陆珊[1] 刁家志[1] 雷芳[1] 谢光[1] 刘克武[1] 

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

出　　处：《天然产物研究与开发》2006年第3期369-372,共4页Natural Product Research and Development

摘　　要：采用紫外光谱法和荧光光谱法研究了秋水仙碱与牛胰蛋白酶的相互作用。观测到秋水仙碱使胰蛋白酶的特征荧光峰猝灭。SternVolmer猝灭曲线显示,秋水仙碱对胰蛋白酶的荧光猝灭机制属于静态猝灭,猝灭常数Kq为6.60×1012(mol/L)1·s1;秋水仙碱与胰蛋白酶的结合常数为1.06×104L·mol1,结合位点数为1,作用力类型主要为疏水作用力。The interaction between colchicine and trypsin was studied by UV spectra and fluorescence spectra. Colchicine treatment led to the quenching of intrinsic fluorescence of trypsin . The Stem-Volmer plots showed that the quenching of colchicine to trypsin was probably a static quenching process, the quenching constant Kq was 6.60×10^12（mol/L）^-1·s^-1. The binding constant was 1.06× 10^4 L-mol^-1, the number of binding sites was 1, the binding power between colchicine and trypsin was mainly hydrophobic power.

关 键 词：秋水仙碱 胰蛋白酶 光谱性质 

分 类 号：R963[医药卫生—微生物与生化药学]