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Novel Metal-Affinity Protein Separations

Suh, S.-S. and Van Dam, M. E. and Wuenschell, G. E. and Plunkett, S. and Arnold, F. H. (1990) Novel Metal-Affinity Protein Separations. In: Protein Purification. ACS Symposium Series. No.427. American Chemical Society , Washington, DC, pp. 139-149.

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The affinity exhibited by proteins for chelated metals has been exploited in two new protein purification techniques: metal affinity aqueous two-phase extraction and metal affinity precipitation. Metal-chelating derivatives of polyethylene glycol have been used to selectively enhance the partition coefficients of proteins in aqueous two-phase separations. When the metal chelate is attached to both ends of the water-soluble polymer, the resulting bis-chelate is an effective precipitating agent for proteins that contain multiple surface-accessible histidines. Parameters important in the design and application of these affinity separations include pH, the number of accessible histidines on the proteins, and the design of the metal affinity ligand. These techniques offer the potential for large-scale application and integration of an affinity separation early in the purification process.

Item Type:Book Section
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Arnold, F. H.0000-0002-4027-364X
Additional Information:© 1990 American Chemical Society. Received January 18, 1990. Published in print 12 June 1990. This research has been supported by the National Science Foundation Grant No. EET-8807351. F. H. A. is the recipient of an NSF Presidential Young Investigator Award.
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Series Name:ACS Symposium Series
Issue or Number:427
Record Number:CaltechAUTHORS:20180405-104511502
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Official Citation:Novel Metal-Affinity Protein Separations S.-S. Suh, M. E. Van Dam, G. E. Wuenschell, S. Plunkett, and F. H. Arnold Protein Purification. June 12, 1990 , 139-149 DOI:10.1021/bk-1990-0427.ch010
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:85634
Deposited By: Ruth Sustaita
Deposited On:05 Apr 2018 20:55
Last Modified:15 Nov 2021 20:30

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