Affinity Electrophoresis for Analysis of Catalytic Module-Carbohydrate Interactions

Darrell Cockburn, Casper Wilkens, Birte Svensson

Research output: Chapter in Book/Report/Conference proceedingBook chapterResearchpeer-review

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.
Original languageEnglish
Title of host publicationProtein-Carbohydrate Interactions : Methods and Protocols
EditorsD. Wade Abbott, Alicia Lammerts van Bueren
Volume1588
PublisherSpringer
Publication date2017
Pages119-127
Chapter9
ISBN (Print)978-1-4939-6898-5
ISBN (Electronic)978-1-4939-6899-2
DOIs
Publication statusPublished - 2017
SeriesMethods in Molecular Biology
ISSN1064-3745

Keywords

  • Protein Binding
  • Affinity electrophoresis
  • Carbohydrate binding module
  • Dissociation constant
  • Polyacrylamide gel electrophoresis
  • Polysaccharide
  • Surface binding site

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