Genetic Approach to Facilitate Purification of Recombinant Proteins with a Novel Metal Chelate Adsorbent View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1988-11-01

AUTHORS

E. Hochuli, W. Bannwarth, H. Döbeli, R. Gentz, D. Stüber

ABSTRACT

We describe a general purification method for recombinant proteins based upon the selective interaction between a poly-histidine peptide, which is fused to the protein of interest, and a novel metal chelate adsorbent. The principle of the technique is illustrated with mouse dihydrofolate reductase. DNA elements coding for adjacent histidines were fused to the mouse dihydrofolate reductase gene. Subsequent expression in E. coli resulted in the production of hybrid proteins that could be purified by immobilized metal ion affinity chromatography, followed by removal of the histidine affinity peptide with carboxypeptidase A. More... »

PAGES

1321-1325

Journal

TITLE

Nature Biotechnology

ISSUE

11

VOLUME

6

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/nbt1188-1321

    DOI

    http://dx.doi.org/10.1038/nbt1188-1321

    DIMENSIONS

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    152 rdf:type schema:Organization
     




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