Cu(Ⅱ)-核固红螯合物与蛋白质的相互作用及其应用

The interaction of Cu(Ⅱ)-nuclear fast red chelate with proteins and its analytical application

在pH 3.7时,核固红与Cu2+形成2:1的螯合物,该螯合物在蛋白质表面通过静电作用力和疏水作用力聚集形成聚集体。该现象不仅导致吸收光谱、荧光光谱发生变化,而且共振瑞利散射明显增强。据此,建立了共振光散射光谱法测定痕量蛋白质的新方法。在430 nm处人血清白蛋白(HSA)和牛血清白蛋白(BSA)分别在0.1～8.0μg/mL和0.19～11.4μg/mL的浓度范围内与增强的共振光散射强度呈良好的线性关系,对应的检测限分别是0.076μg/mL和0.105μg/mL。在598 nm处HSA和BSA分别在0.05～3.0μg/mL和0.096～4.78μg/mL范围内与增强的共振光散射强度呈良好的线性关系,对应的检测限分别是0.026μg/mL和0.033μg/mL。方法可用于人血清样品中蛋白质含量的测定。

the obvious enhancement of the resonance light scattering （RLS）. At 430 nm, the enhanced intensities of RLS are proportional to the concentration of human serum albumin （HSA） and bovine serum albumin （BSA） in the range of 0. 1- 8.0 μg/mLand 0. 19 - 11.4 μg/mL, respectively. The detection limits are 0. 076 μg/mL for HSA and 0. 105μg/mL for BSA. And the enhanced intensities of RLS at 598 nm are proportional to the concentration of protein in the range of 0. 05 - 3.0 μg/mL for HSA and 0. 096 - 4. 78 μg/mL for BSA, the detection limits are 0. 026 μg/mL for HSA and 0. 033 μg/mLfor BSA. Based on that, a method for the determination of trace amounts of proteins by resonance light scattering technique has been developed. It can be applied to the determination of proteins in human serum samples.