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Retention Behavior of Proteins on Glutamic Acid-Boned Silica Stationary Phase

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Abstract

A glutamic acid-bonded silica (Glu-silica) stationary phase with cation-exchange properties was synthesized using l-glutamic acid as ligand and silica gel as matrix. The effects of solution pH value, salt concentration and metal ion on the retention of proteins were examined. The standard protein mixture was separated with a prepared chromatographic column and an iminodiacetic acid column, and compared. The influence of the binding capacity of an immobilized metal ion on the complexation of metal chelate column was studied. The results indicate that the obtained column displays cation-exchange characteristic and better separation ability for proteins. As fixing metal ion on the Glu-silica column, retention of proteins on the column is a cooperative interaction of metal chelate and cation-exchange. The stationary phase shows the typical metal chelate properties with the increase of the sorption capacity of immobilized metal ion.

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Acknowledgments

This work was supported by grants from Natural Science Foundation of Shaanxi Province (No. 2007B22), NWU Funds (No. U5NW4), and Shaanxi Provincial Key Discipline Program. The authors would like to thank Professor Yinmao Wei for his constructive comments and valuable suggestions in this paper.

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Authors and Affiliations

  1. College of Chemical Engineering, Northwest University, 710069, Xi’an, Shaanxi, People’s Republic of China

    Rong Li, Yan Wang, Guo Liang Chen & Xiao Gang Wang

  2. Institute of Analytical Science, Northwest University, Xi’an, Shaanxi, 710069, People’s Republic of China

    Rong Li & Jian Bin Zheng

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  1. Rong Li
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  2. Yan Wang
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  3. Guo Liang Chen
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Correspondence to Jian Bin Zheng.

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Li, R., Wang, Y., Chen, G.L. et al. Retention Behavior of Proteins on Glutamic Acid-Boned Silica Stationary Phase. Chroma 70, 731–737 (2009). https://doi.org/10.1365/s10337-009-1219-4

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