双核铜(Ⅱ)-β-丙氨酸缩水杨醛席夫碱配合物与血清蛋白相互作用的共振瑞利散射光谱  

Resonance Rayleigh scattering spectra of Binuclear β-Alanine Salicylic Schiff Base Copper(Ⅱ)with serum protein

作　　者：张晓亮[1] 陈亚东[1] 徐伟民[1] 杨欣[1] 干宁[1] 

机构地区：[1]宁波大学材化学院新型功能材料及其制备科学国家重点实验室

出　　处：《光谱实验室》2008年第5期939-942,共4页Chinese Journal of Spectroscopy Laboratory

基　　金：浙江省自然科学基金(Y106725);浙江省科技攻关项目(No2006C31040);宁波市自然科学基金(No2008A610043&2008A610072);宁波大学王宽城幸福基金资助项目

摘　　要：合成了双核铜-β-丙氨酸缩水杨醛席夫碱配合物([Cu2(HL)2](NO3)2·2H2O,简称CuL)。在与血清白蛋白相互作用的过程中,发现它们结合会引起蛋白共振瑞利散射(RRS)的急剧增强。最大RRS峰位于470/470nm。对体系的适宜反应条件、影响因素及散射强度与蛋白质浓度的关系进行了研究。结果表明,在一定浓度范围内,蛋白质浓度与散射强度成正比。该方法有较高的灵敏度,对牛血清白蛋白(BSA)和人血清蛋白(HSA)的检测范围为5.0—30.5ng/mL。考察了共存物质的干扰影响,并对蛋白质合成样品和实际样品进行分析,结果满意。In sulfuric acid medium,the reaction of heteropoly compounds with proleins results in the enhancement of Resonance Rayleigh scattering（RRS）. A novel method for the determination of trace amounts of protein by using the RRS method has been established. Their maximum scattering wavelengths, λex/λem, appear at 470/470nm. In the certain range, the concentration of proteins is directly proportional to the enhanced intensity of RRS. The suitable reaction conditions, affecting factors as well as the influence of some coexisiting substances were investigated. The methods give high sensitivity,and the detection range for proteins were 5.0-30. 5ng/mL. The method had good selectivity ,and was applied to the determination of protein in synthetic samples and practical samples with satisfactory results.

关 键 词：双核铜(Ⅱ)-β-丙氨酸缩水杨醛席夫碱配合物 血清蛋白 共振瑞利散射 

分 类 号：O657.32[理学—分析化学]