论文部分内容阅读
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 characteristics of the interaction between AlF_6 ~ (3-) and bovine serum albumin (BSA) were investigated. Various influencing factors and suitable reaction conditions were investigated, and the relationship between the fluorescence intensity of the system and the concentration of bovine serum albumin Between the establishment of a new method for the determination of protein content. The results showed that AlF_6 ~ (3-) and BSA at pH 4.0 in Tris-HCl buffering medium were excited by 280 nm light under electrostatic attraction and hydrophobic force The resulting ion-association products produced a strong fluorescence peak at 330 nm. When the concentration of BSA was in the range of 0.10 ~ 30.0μg / m L, there was a good linear relationship between the change of fluorescence intensity ΔF and the concentration of bovine serum albumin, and the detection limit was 5.11 ng / m L. The method can be directly used to determine the content of human serum protein, the recovery rate was 103.1% ~ 116.5%.