Metal-affinity separations: a new dimension in protein processing.
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.
Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125.
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Arnold
D000818:Animals; D002614:Chelating Agents; D002846:Chromatography, Affinity / Q000379:methods*; D003574:Cytochrome c Group / Q000302:isolation & purification; D007098:Imino Acids; D008024:Ligands; D008670:Metals; D011506:Proteins / Q000302:isolation & purification*
D002614:Chelating Agents; D003574:Cytochrome c Group; D007098:Imino Acids; D008024:Ligands; D008670:Metals; D011506:Proteins; C008109:iminodiacetic acid