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A Polypeptide Fusion Designed for the Purification of Recombinant Proteins

Bio/Technology volume 2, pages 76–81 (1984)Cite this article

An Erratum to this article was published on 01 March 1984

Abstract

Recombinant DNA technology was used to produce human urogastrone with a C-terminal polyarginine fusion. This peptide fusion formed the basis of a two-step ion exchange purification that gave 64mg of urogastrone at >95% purity with 44% yield. In the first step, a substantial purification was obtained due to the unusual basicity of the polyarginine-fused protein. Further purification was achieved after removing polyarginine using carboxypep-tidase B. As expected, rechromatography demonstrated a large change in the elution profile of the recombinant protein, but not the contaminants. This purification method is simple, effective, and highly suitable to scale-up. In principle, it may be applied to any recombinant protein.

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  1. Searle Research and Development, Lane End Road, High Wycombe, Bucks, HP12 4HL, U.K.

    Helmut M. Sassenfeld & Stephen J. Brewer

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  1. Helmut M. Sassenfeld
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  2. Stephen J. Brewer
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Sassenfeld, H., Brewer, S. A Polypeptide Fusion Designed for the Purification of Recombinant Proteins. Nat Biotechnol 2, 76–81 (1984). https://doi.org/10.1038/nbt0184-76

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