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Metal-affinity separations: a new dimension in protein processing.

F H Arnold
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Abstract

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 biospecific 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 recombinant 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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AnimalsChelating AgentsChromatography, AffinityCytochrome c GroupImino AcidsLigandsMetalsProteinsJournal ArticleResearch Support, Non-U.S. Gov'tResearch Support, U.S. Gov't, Non-P.H.S.Review

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F H Arnold. 1991. Metal-affinity separations: a new dimension in protein processing.. https://doi.org/10.1038/nbt0291-151

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