Metal-Affinity Separations: A New Dimension in Protein Processing
- Creators
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Arnold, Frances H.
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 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.
Additional Information
© 1991 Springer Nature Limited.Additional details
- Eprint ID
- 89057
- Resolver ID
- CaltechAUTHORS:20180822-141010067
- Created
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2018-08-22Created from EPrint's datestamp field
- Updated
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2021-11-16Created from EPrint's last_modified field