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Review
Bio/Technology  9, 151 - 156 (1991)
doi:10.1038/nbt0291-151

Metal-Affinity Separations: A New Dimension in Protein Processing

Frances H. Arnold1

1Division of Chemistry and Chemical Engineering 210-41, California Institute of Technology, Pasadena, California 91125.

Rapid growth in the preparative and high-resolution analytical applications of metal-affinity chromatography demonstrate the appeal of metal recognition as a basis for protein separations. Stable, inexpensive chelated metals effectively mimic bio-specific interactions, providing selective ligands for protein binding. This article reviews recent progress in understanding the mechanisms of metal-protein recognition that underlie metal-affinity separations. Also discussed are schemes for integrating metal-affinity purifications into the expression and bioprocessing of re-combinant proteins. Promising future developments include new metal-affinity processes for analytical and preparative-scale separations and a range of techniques for enhancing the selectivity of metal-affinity separations.

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