Abstract
Affinity electrophoresis has long been used to study the interaction between proteins and large soluble ligands. The technique has been found to have great utility for the examination of polysaccharide binding by proteins, particularly carbohydrate binding modules (CBMs). In recent years, carbohydrate surface binding sites of proteins mostly enzymes have also been investigated by this method. Here, we describe a protocol for identifying binding interactions between enzyme catalytic modules and a variety of carbohydrate ligands.
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Acknowledgments
This work was supported by a grant to B.S. from the Danish Council for Independent Research|Natural Sciences.
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Cockburn, D., Wilkens, C., Svensson, B. (2017). Affinity Electrophoresis for Analysis of Catalytic Module-Carbohydrate Interactions. In: Abbott, D., Lammerts van Bueren, A. (eds) Protein-Carbohydrate Interactions. Methods in Molecular Biology, vol 1588. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-6899-2_9
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DOI: https://doi.org/10.1007/978-1-4939-6899-2_9
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