秋水仙碱与胃蛋白酶相互作用的光谱性质研究  

Spectroscopy study on the interaction between colchicine and pepsin

作　　者：喻东[1] 黄新河[1] 刘鑫[1] 胡源[1] 姜骅[1] 唐成康[1] 贾旭[1] 刘克武[1] 

机构地区：[1]四川大学生命科学学院,四川成都610064

出　　处：《化学研究与应用》2005年第4期474-476,共3页Chemical Research and Application

摘　　要：采用紫外光谱法和荧光光谱法研究了秋水仙碱与胃蛋白酶的结合作用。观测到秋水仙碱使胃蛋白酶的紫外吸收峰增强,特征荧光峰淬灭。Stern-Volmer淬灭曲线显示,秋水仙碱对胃蛋白酶的荧光淬灭很可能是一个单一的静态淬灭过程。当λex=295nm时,秋水仙碱可以淬灭胃蛋白酶中95.5%的Trp残基。The binding interaction between colchicine and pepsin was studied by ultmviolet absorption and fluorescence spectra. Colchicine treatment led to the increasing of UV absorption and the quenching of intrinsic fluorescence of pepsin. The Stern-Volmer curve shows that the quenching of colchicine to pepsin is probably a single static quenching process. 95.5% Trp residue of pepsin can be quenched by colchicine when λex=295nm.

关 键 词：秋水仙碱 胃蛋白酶 紫外光谱 荧光光谱 

分 类 号：O657.3[理学—分析化学]