BSA与CTAB相互作用的荧光光谱研究  

Studies on the Interaction for Bovine Serum Albumin with Cetyltrimethylammonium Bromide by Fluorescence Spectrometry

作　　者：涂逢樟[1] 俞芸[1] 上官昌汾 

机构地区：[1]龙岩学院化学与材料学院,福建龙岩364000

出　　处：《广州化工》2013年第24期55-58,共4页GuangZhou Chemical Industry

基　　金：龙岩学院第二批教育教学改革立项项目(岩学院教[2009]40号)资助

摘　　要：在模拟生理条件下,用荧光光谱法研究了十六烷基三甲基溴化铵(CTAB)与牛血清白蛋白(BSA)的相互作用。结果表明:BSA分子中色氨酸和酪氨酸残基具有荧光发射性质,以280 nm激发BSA,在341 nm处有很强的荧光发射。在加入CTAB后,发现CTAB-BSA强荧光峰的位置蓝移,且荧光强度随着CTAB浓度的增大而明显减弱,说明CTAB对BSA有荧光猝灭现象,猝灭以静态猝灭为主,由Stern-Volmer方程求得CTAB表观猝灭常数K q=1.469×1013L·mol-1·s-1。得到了CTAB与牛血清白蛋白分子间的结合常数和热力学参数。利用已有的计算方法,建立了相应的计算机程序,使计算结果更合理。通过与常见公式计算的结果进行比较,所建立的方法得到了比较满意的结果。The interaction of cetyltrimethylammonium bromide （CTAB） and bovine serum albumin （BSA） was studied under conditions similar to those in human bodies by fluorescence spectra. The results indicated that CTAB, which was located in BSA, had a max fluorescence emission peak at 341 nm with an excitation wavelength of 280 nm. It showed that CTAB had a powerful ability to quench the BSA fluorescence with a mechanism of a static process rather than a dynamic one. The apparent quenching constant Kq was obtained to be1.469×10^13L·mol^-1·s^-1 by Stern - Volmer equation. The binding and thermodynamic parameters were obtained. The reasonable results were obtained by programmed calculation process based on the calculating equation established. By comparison with the results obtained by other calculating methods, it was proved that the satisfactory results can be obtained by the proposed method.

关 键 词：荧光光谱 牛血清白蛋白 十六烷基三甲基溴化铵 相互作用 

分 类 号：O616[理学—无机化学]