作　　者： ; ;

机构地区： 华南师范大学化学与环境学院

出　　处： 《华南师范大学学报（自然科学版）》 2007年第2期73-78,共6页

摘　　要： 在pH9.25 Britton-Robinson（B-R）缓冲介质中,牛血清白蛋白（BSA）对酸性染料偶氮氯膦Ⅰ（CPⅠ）的荧光有猝灭,使CPⅠ最大荧光峰从578 nm红移至610 nm,对荧光猝灭的实验条件进行了优化,建立了蛋白质定量的线性方程△F=20.8C-6.8（μg/mL）,线性响应范围0.04～30.0μg/mL、检出限0.031μg/mL（r=0.995 6）,并应用于样品中BSA含量的分析.对荧光猝灭机理进行了探讨,认为两者之间的猝灭是由于生成不发荧光的复合物,属于静态猝灭过程,求得不同温度下的形成常数及热力学函数ΔH、ΔG、ΔS分别为-2.3 kJ,-31.2 kJ,98.6 J,根据热力学函数确定了两者是通过静电作用力结合的. At pH9.25 Britton - Robinson buffer solution, the interaction between Chlorophosphonazo Ⅰ （CP Ⅰ）and proteins has been studied by using fluorescence spectroscopy method. The emission spectrum of CP Ⅰ - BSA shows a bathochromic shift from 578 nm to 610 nm. The optimum condition of fluorimetric determination of protein was studied. The linear equation was △F =20.8C - 6.8 （ μg/mL）. The detection limit of this method was 0.031μg/mL with the linear range of 0.04 - 30.0 μg/mL（ r = 0.995 6 ）. The developed method was successfully applied to the determination of protein in sample. In addition, the formation constant at different temperatures and the thermodynamic functions（ such as △G, △H and △S） of CP Ⅰ with BSA were obtained. The mechanism of the fluorescence quenching was also explored. It is considered that the quenching is mainly due to generating quenchable complex and that interaction of CP Ⅰ and proteins was static electricity forces.

关 键 词： 偶氮氯膦 牛血清白蛋白质 荧光猝灭

领　　域： [理学] [理学]