Schmitt J, Hess H, Stunnenberg H G
European Molecular Biology Laboratory, Gene Expression Programme, Heidelberg, Germany.
Mol Biol Rep. 1993 Oct;18(3):223-30. doi: 10.1007/BF01674434.
Expression of recombinant proteins is a standard technique in molecular biology and a wide variety of prokaryotic as well as eukaryotic expression systems are currently in use. A limiting step is often the purification of the expressed recombinant protein, particularly if mammalian expression systems that yield low expression levels are employed. Here, we discuss the advantages and restrictions of tagging recombinant proteins with histidines and purifying them by Ni(2+)-NTA chromatography.
重组蛋白的表达是分子生物学中的一项标准技术，目前广泛使用各种原核和真核表达系统。一个限制步骤通常是表达的重组蛋白的纯化，特别是如果采用产生低表达水平的哺乳动物表达系统时。在此，我们讨论用组氨酸标记重组蛋白并用Ni(2+)-NTA色谱法纯化它们的优点和限制。
