Vikis Haris G, Guan Kun-Liang
Department of Biological Chemistry, University of Michigan, Ann Arbor, MI, USA.
Methods Mol Biol. 2004;261:175-86. doi: 10.1385/1-59259-762-9:175.
Glutathione-S-transferase (GST)-fusion proteins have become an effective reagent to use in the study of protein-protein interactions. They can be produced in bacterial and mammalian cells in large quantities and purified rapidly. Given that GST can be coupled to a glutathione matrix permits its use as an effective affinity column to study interactions in vitro or to purify protein complexes in cells expressing the GST-fusion. Here we provide a technical description on the utilization of GST-fusion proteins as both a tool to studying protein-protein interactions and also as a means to purify interacting proteins.
谷胱甘肽-S-转移酶（GST）融合蛋白已成为蛋白质-蛋白质相互作用研究中一种有效的试剂。它们可以在细菌和哺乳动物细胞中大量产生并快速纯化。由于GST可以与谷胱甘肽基质偶联，这使得它能够用作一种有效的亲和柱，用于体外研究相互作用或在表达GST融合蛋白的细胞中纯化蛋白质复合物。在这里，我们提供了关于利用GST融合蛋白作为研究蛋白质-蛋白质相互作用的工具以及纯化相互作用蛋白的方法的技术描述。
