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文献和实验Expression of Recombinant Proteins with Uniform N-Termini
to a self-splicing mini-intein. This fusion construct is expressed in an engineered E. coli strain from which the pepP gene coding for aminopeptidase P has been deleted. We describe a protocol using human cationic trypsinogen as an example to demonstrate
Recombinant Single Globin-Chain Expression and Purification
of normal and modified human globin chains in bacteria employing a fusion-protein expression vector (1 ). An expression system was later developed in which α- and β-globin chains were coexpressed, resulting in the formation of soluble tetrameric Hb in yeast
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