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Boronic acid–lectin affinity chromatography. 1. Simultaneous glycoprotein binding with selective or combined elution

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Abstract

We introduce a novel combination of boronic acid affinity chromatography with lectin affinity chromatography, dubbed as boronic acid–lectin affinity chromatography (BLAC). Concanavalin A and wheat germ agglutinin lectins were mixed with the pesudo-lectin boronic acid to form the BLAC affinity column and their performance was evaluated with standard glycoproteins. Optimization of the binding and elution buffers for the BLAC system is described. The BLAC columns were employed to isolate glycoproteins of interest using both selective and/or combined elution.

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Acknowledgements

This work was supported by the Marie Curie Chair (006733) of the European Commission and the GenAu program (GZ 200.065/2-VI/2/2002) of the Austrian Ministry of Arts, Science and Education.

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  1. Horváth Laboratory of Bioseparation Sciences, Institute of Analytical Chemistry and Radiochemistry, University of Innsbruck, Innrain 66, 6020, Innsbruck, Austria

    Alex Monzo, Guenther K. Bonn & András Guttman

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  1. Alex Monzo
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  2. Guenther K. Bonn
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  3. András Guttman
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Correspondence to András Guttman.

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Monzo, A., Bonn, G.K. & Guttman, A. Boronic acid–lectin affinity chromatography. 1. Simultaneous glycoprotein binding with selective or combined elution. Anal Bioanal Chem 389, 2097–2102 (2007). https://doi.org/10.1007/s00216-007-1627-y

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  • DOI: https://doi.org/10.1007/s00216-007-1627-y

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