Gene. 1992 Feb 1;111(1):99-104.

Single-step purification of bacterially expressed polypeptides containing an oligo-histidine domain.

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Department of Tumor Biology, University of Texas M.D. Anderson Cancer Center, Houston 77030.

Abstract

Plasmid expression vectors have been constructed that direct the synthesis in Escherichia coli of fusion proteins containing a stretch of six histidine residues at either the N or C terminus. This oligo-histidine domain allows the single-step purification of the fusion proteins, under nondenaturing conditions, by immobilized metal affinity chromatography on Ni2+ bound to iminodiacetic acid-agarose. Several eukaryotic transcription factors (e.g., the upstream stimulatory factor for the adenovirus major late promoter) have been successfully purified, in an active state, by this method.

PMID:: 1547959; [PubMed - indexed for MEDLINE]

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