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基于泰洛明的放大共振光散射信号测定纳克级蛋白质。

Determination of nanograms of proteins based on the amplified resonance light scattering signals of Tichromine.

机构信息

College of Chemistry, Xiangtan University, Key Laboratory of Environmentally Friendly Chemistry and Applications of Ministry of Education, Xiangtan, Hunan, PR China.

出版信息

Spectrochim Acta A Mol Biomol Spectrosc. 2010 Mar;75(3):1057-60. doi: 10.1016/j.saa.2009.12.053. Epub 2009 Dec 22.

Abstract

A new high-sensitivity detection of protein assay at the nanogram level is developed based on the amplified resonance light scattering signals (RLS) of Tichromine (TCM). In Walpole (NaAc-HCl) buffer (pH 4.05), TCM reacts with proteins to form large particles, which results in remarkable enhanced RLS signals characterized by three peaks at 293 nm, 399 nm and 553 nm. Mechanistic studies showed that the enhanced RLS stems from a large complex of TCM-BSA formed for the electrostatic effect between TCM and BSA. With the enhanced RLS signals at the three wavelengths, the enhanced RLS intensity is proportional to the concentration of proteins in an appropriate range. The lowest limit of determination was 7.4 ng mL(-1). The proposed method was successfully applied to determine total protein in human serum samples.

摘要

基于泰洛明(TCM)的放大共振光散射信号(RLS),开发了一种新的纳克级蛋白质检测的高灵敏度检测方法。在沃尔波尔(NaAc-HCl)缓冲液(pH 4.05)中,TCM 与蛋白质反应形成大颗粒,导致 RLS 信号显著增强,特征为在 293nm、399nm 和 553nm 处有三个峰。机理研究表明,增强的 RLS 源于 TCM 和 BSA 之间的静电作用形成的 TCM-BSA 大复合物。在三个波长处的增强 RLS 信号下,增强的 RLS 强度与蛋白质的浓度在适当范围内成正比。检测的最低限为 7.4ng/mL。该方法成功应用于人血清样品中总蛋白的测定。

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