通过谷胱甘肽树脂亲和层析纯化融合蛋白。
Purification of Fusion Proteins by Affinity Chromatography on Glutathione Resin.
出版信息
Cold Spring Harb Protoc. 2020 Jun 1;2020(6):102202. doi: 10.1101/pdb.prot102202.
PMID:32482903
Abstract
Fusion proteins that contain a glutathione -transferase (GST) moiety can be purified to near homogeneity by affinity chromatography on glutathione-linked resins. Glutathione immobilized on a chromatography matrix, such as agarose or Sepharose, acts as a substrate for the GST moiety of fusion proteins. Contaminating proteins are washed away, and the bound GST fusion proteins are then readily displaced from the resin by elution with buffers containing free glutathione.
摘要
融合蛋白含有谷胱甘肽转移酶（GST）部分，可以通过谷胱甘肽连接树脂的亲和层析进行近乎纯的纯化。固定在层析基质（如琼脂糖或琼脂糖凝胶）上的谷胱甘肽可作为融合蛋白 GST 部分的底物。污染蛋白被洗去，然后通过含有游离谷胱甘肽的缓冲液洗脱，从树脂上容易地置换出结合的 GST 融合蛋白。
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