Histidine-ligand chromatography of proteins Multiple modes of binding mechanism

Hu S. and Do D.D. (1993) Histidine-ligand chromatography of proteins Multiple modes of binding mechanism. Journal of Chromatography A, 646 1: 31-35. doi:10.1016/S0021-9673(99)87004-6


Author Hu S.
Do D.D.
Title Histidine-ligand chromatography of proteins Multiple modes of binding mechanism
Journal name Journal of Chromatography A   Check publisher's open access policy
ISSN 0021-9673
Publication date 1993-08-27
Sub-type Article (original research)
DOI 10.1016/S0021-9673(99)87004-6
Volume 646
Issue 1
Start page 31
End page 35
Total pages 5
Subject 1602 Criminology
1308 Clinical Biochemistry
1313 Molecular Medicine
Abstract The objective of this work is to exploit the versatile applications of matrix-linked histidine in protein chromatography. The negatively charged histidine at alkaline pH acts as a cation exchanger for proteins with high isoelectric points. Because of the hydrophobicity of the imidazole ring in histidine, enzymes, such as yeast alcohol dehydrogenase, are strongly retained by this histidine-ligand column in presence of 1.2 M ammonium sulfate. Due to the high formation constants of complexes between immobilised-histidine and metal ions, this column could be applied to serve as a ligand-exchange chromatography. In this instance, the interaction between proteins and the ligand takes place via the coordination sphere of the complex-forming metal ions. All these binding modes have been elucidated by the investigations of the effects of pH, metal ions, salt type and concentrations on (1) the purification of trypsin and (2) the binding of model proteins. It should be noted that this work differs from the reported applications [M.A. Vijalakshmi, Trends Biotechnol. 7 (1989) 71] where the protein binding occurs at low ionic strength and at pH values near or around their isoelectric points.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Scopus Import
 
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