摘要
研究了AlF_6^(3-)与牛血清白蛋白(BSA)之间相互作用的光谱特性,考察了各种影响因素和适宜的反应条件,确定了体系的荧光光谱强度与牛血清白蛋白浓度之间的关系,建立了测定蛋白质含量的新方法。研究结果表明,在pH 4.0的三羟甲基氨基甲烷-HCl(Tris-HCl)缓冲介质中,以280 nm光激发,在静电引力和疏水力的作用下,AlF_6^(3-)与BSA之间形成的离子缔合物在330 nm处产生1个较强的荧光峰。当BSA的质量浓度在0.10~30.0μg/m L范围内时,体系的荧光强度变化值ΔF与牛血清白蛋白浓度之间有良好的线性关系,其检出限为5.11 ng/m L。方法可直接用于测定人血清中蛋白质的含量,回收率为103.1%~116.5%。
The spectral characteristic of the interaction between AlF6^3- and bovine serum albumin was studied. The various influence factors and suitable reaction conditions were examined. Based on the relationship between the fluorescence intensity and protein content, a new method for the determination of protein content was thus established. The results showed that the ion-association complexes were produced between AlF6^3- and BSA based on electrostatic force and hydrophobic force in Tris-HCl medium of pH 4.0, which produced a strong fluorescence peak at 330 mn at the excitation wavelength of 280 nm. There was good linearity between the intensity of fluorescence and the concentration of bovine serum albumin in the range of 0. 10 ~ 30. 0 μg/mL with the detection limit of 5.11 ng/mL. The method could be used to determine the content of protein in serum with the recovery of 103.1% ~116.5%.
出处
《分析试验室》
CAS
CSCD
北大核心
2017年第5期600-603,共4页
Chinese Journal of Analysis Laboratory