Al^(3+)-核固红-蛋白质体系的光谱特性及其分析应用  

Spectroscopy characteristic of Al^(3+)-nuclear fast red-proteins and its analytical applications

作　　者：于洁[1,2] 曲崇[1] 冯素玲[1] 

机构地区：[1]河南师范大学化学化工学院,河南新乡453007 [2]新乡医学院化学教研室,河南新乡453003

出　　处：《化学研究与应用》2014年第3期404-408,共5页Chemical Research and Application

摘　　要：在pH为4.0时,Al3+与核固红形成的螯合物能够通过静电作用力和疏水作用力在蛋白质表面聚集形成聚集体。据此,提出了共振瑞利散射光谱法测定蛋白质的新方法。研究了体系的吸收光谱、荧光光谱及共振散射光谱。采用共振光散射技术测定了金属螯合物的组成。探讨了反应机理和共振光散射增强的主要原因。在440 nm处,人血清白蛋白(HSA)和牛血清白蛋白(BSA)的线性范围分别是0.2~12.0μg·mL-1和0.6~26.0μg·mL-1,对应的检测限分别是19.9 ng·mL-1和40.9 ng·mL-1。在584 nm处HSA和BSA的线性范围分别是0.05~6.0μg·mL-1和0.2~14.0μg·mL-1,检测限分别是11.5 ng·mL-1和23.3 ng·mL-1。方法可用于人血清、唾液和尿样中蛋白质含量的测定。将该方法的测定结果与考马斯亮蓝法的测定结果进行对照,经t-检验证明两种方法无显著性差异。In pH 4. 0,the chelate of nuclear fast red with Al3＋ aggregated on the surface of proteins by virtue of electrostatic attrac-tion and hydrophobic force to form congeries. Based on that,a new method for the determination of proteins was proposed. The ab-sorption spectra,fluorescence spectra and resonance light scattering（ RLS） spectra were investigated. The stiochiometry of the com-plex were determined by resonance light scattering technique. The reaction mechanism and reason of RLS enhancement were dis-cussed. At 440 nm,the linear range were 0. 2～12. 0 μg·mL-1 and 0. 6~26. 0 μg·mL-1 for human serum albumin（ HSA） and bo-vine serum albumin（ BSA） ,respectively. The detection limits were 19. 9 ng·mL-1 for HSA and 40. 9 ng·mL-1 for BSA. At 584 nm, the linear range were 0. 05~6. 0μg·mL-1 and 0. 2~14. 0μg·mL-1 for HSA and BSA,respectively. The detection limits were 11. 5 ng·mL-1 for HSA and 23. 3 ng·mL-1 for BSA. The proposed method was used to determine proteins in human serum,urine and sali-va. The results of the method were compared with those of Coomassie brilliant blue method,and the t-test concluded no significant differences between two methods.

关 键 词：共振光散射 Al3+ 核固红 蛋白质 

分 类 号：O657.3[理学—分析化学]