One‐Step Purification of a Model Periplasmic Protein from Inclusion Bodies by Its Fusion to an Effective Metal‐Binding Peptide

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Abstract
It has been demonstrated that the addition of a metal‐binding amino acid sequence to an exposed terminus of a protein can be useful for purification using immobilized metal affinity chromatography (IMAC). Polyhistidine extensions, wherein sequential histidyl residues are placed at the end of a protein, have been utilized for protein purification through IMAC. Natural metal‐binding peptides may also serve as starting points for the design of an affinity tail. As a model system, an octapeptide derived from angiotensin I was fused to TEM‐β‐lactamase. When the modified protein was expressed in Escherichia coli, a one‐step purification of this recombinant protein was accomplished from resolubilized inclusion body material.