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阿特拉津与蛋白质结合反应及其在测定蛋白质中的应用 被引量:5

Reaction of Atrazine with Protein and Its Application to Detection of Protein
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摘要 用共振光散射光谱(RLS)和紫外-可见电子吸收光谱研究了阿特拉津与牛血清蛋白(BSA)之间的相互作用。研究表明,在酸性条件下,阿特拉津与牛血清蛋白依靠范德华力和N/O-H…π氢键生成结合物,从而使阿特拉津的紫外吸收有整体红移的趋势,并且产生强烈的共振散射光增强现象。共振光散射光谱特征和强度与溶液的pH、阿特拉津的浓度、反应温度等有关。在优化的实验条件下,阿特拉津与牛血清蛋白体系的共振光散射强度与牛血清蛋白的浓度呈线性关系,据此建立了一种简单、灵敏测定牛血清蛋白的新方法。该方法的检出限(3d)为12ng·mL^-1,线性范围为0.05~100μg·mL^-1。该法用于人工混合样品中牛血清蛋白的测定,取得了令人满意的结果。 The resonance light scattering (RLS) technique and UV-Vis absorption spectra were applied to the investigation of the interaction between atrazine and bovine serum albumin(BSA). Under acidic conditions, the formation of atrazine-BSA supermolecule by Van der Waals force and N/O—H…π hydrogen bonds leads to a red shift of absorption band and strong RLS enhancement of atrazine. The characteristics and intensity of RLS were related to the pH, the concentration of atrazine, and temperature. Under the optimum conditions, the enhanced RLS intensities are in proportion to the concentration of BSA in the range of 0. 05-100μg·mL^-1. Based on the enhancement of the RLS, a simple and sensitive method for the determination of BSA was established. The detection limit (3σ) is 12 ng·mL^-1. Synthesis samples were determined with satisfactory results.
出处 《光谱学与光谱分析》 SCIE EI CAS CSCD 北大核心 2006年第3期509-512,共4页 Spectroscopy and Spectral Analysis
基金 国家自然科学基金(30270786)项目资助
关键词 阿特拉津 蛋白质 相互作用 共振光散射 Atrazine; Protein, Interaction RLS
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参考文献14

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