秋水仙碱与牛血清白蛋白相互作用的光谱性质研究  

Spectroscopy Study on the Interaction between Colchicine and Bovine Serum Albumin(BSA)

作　　者：黄新河[1] 刘鑫[1] 李佳[1] 刘克武[1] 

机构地区：[1]四川大学生命科学学院,成都610064

出　　处：《四川大学学报（自然科学版）》2005年第2期377-381,共5页Journal of Sichuan University(Natural Science Edition)

摘　　要：采用紫外光谱法和荧光光谱法研究了秋水仙碱与牛血清白蛋白(BSA)的结合作用.观测到生理pH7.43条件下秋水仙碱使BSA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BSA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BSA中97.1%的Trp残基.The binding interaction between colchicine and bovine serum albumin(BSA) was studied by ultraviolet absorption and fluorescence spectra. In physiological condition(pH 7.43), colchicine treatment led to the increasing of UV absorption and the quenching of intrinsic fluorescence of BSA. The Stern-Volmer curve shows that the quenching of colchicine to BSA is probably a single static quenching process. 97.1% Trp residues of BSA can be quenched by colchicine when λ(ex )equals 295nm.

关 键 词：秋水仙碱 牛血清白蛋白 紫外光谱 荧光光谱 

分 类 号：Q502[生物学—生物化学]