Protein fusions as an aid to purification

作者: A. J. Whitmarsh , D. P. Hornby

DOI: 10.1007/978-94-011-1322-9_7

关键词: BiochemistryCodon usage biasMolecular cloningRecombinant DNAEscherichia coliTranslation (biology)Expression vectorGeneGlycosylationBiology

摘要: The ability to engineer high-level expression of almost any polypeptide in a number different host organisms (or cell types) has greatly facilitated the functional analysis low-abundance proteins and enabled biotechnologists develop economically viable large-scale processes for production many with wide variety applications medicine industry. Whilst authentic eukaryotic requires that they be chemically modified following translation vivo (usually by phosphorylation, glycosylation or site-specific proteolysis), continued widespread use Escherichia coli as organism, which is unable introduce such modifications, owes much its special place development molecular cloning technology. In this chapter, we shall discuss genetic manipulation both bacterial mammalian genes order not only facilitate their E. coli, but also simplify purification protein product using affinity chromatography. These approaches are restricted application versatile vectors other been slower, so concentrate primarily on recombinant from bacterium.

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