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一种用于2-氧代戊二酸受体和结合蛋白的“点击”化学构建的亲和系统。

A "click" chemistry constructed affinity system for 2-oxoglutaric acid receptors and binding proteins.

作者信息

Wang Yang, Assaf Zeinab, Liu Xinjun, Ziarelli Fabio, Latifi Amel, Lamrabet Otmane, Quéléver Gilles, Qu Fanqi, Zhang Cheng-Cai, Peng Ling

机构信息

Aix-Marseille Université and CNRS, Centre Interdisciplinaire de Nanoscience de Marseille, UMR 7325, 13288, Marseille, France.

出版信息

Org Biomol Chem. 2014 Sep 7;12(33):6470-5. doi: 10.1039/c4ob01005a.

Abstract

An ingenious and specific affinity resin designed to capture the 2-oxoglutaric acid (2-OG) binding proteins was constructed by appending a 2-OG tag to the solid resin via a Cu-catalyzed Huisgen "click" reaction. The so-obtained affinity resin was able to recognize, retain and separate the established 2-OG binding protein NtcA in both the pure form and crude cellular extract, thus constituting a valuable means of searching for novel 2-OG receptors with a view to exploring the signalling pathways of 2-OG, a key Krebs cycle intermediate with unprecedented signalling functions.

摘要

通过铜催化的惠斯根“点击”反应将2-氧代戊二酸(2-OG)标签连接到固体树脂上,构建了一种巧妙且特异的亲和树脂,用于捕获与2-OG结合的蛋白质。如此获得的亲和树脂能够识别、保留并分离纯形式和粗细胞提取物中的已确定的2-OG结合蛋白NtcA,从而构成了一种寻找新型2-OG受体的有价值手段,以期探索2-OG的信号通路,2-OG是三羧酸循环的关键中间产物,具有前所未有的信号功能。

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