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  • Title: One-step purification of a model periplasmic protein from inclusion bodies by its fusion to an effective metal-binding peptide.
    Author: Beitle RR, Ataai MM.
    Journal: Biotechnol Prog; 1993; 9(1):64-9. PubMed ID: 7763412.
    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-beta-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.
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