Affinity Electrophoresis for Analysis of Catalytic Module-Carbohydrate Interactions

Darrell W. Cockburn*, Casper Wilkens, Birte Svensson

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingBook chapterEducationpeer-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 publicationCarbohydrate-Protein Interactions : Methods and Protocols
EditorsD. Wade Abbott, Wesley F. Zandberg
Number of pages11
Volume2657
PublisherSpringer
Publication date2023
Edition2
Pages91-101
Chapter6
ISBN (Print)978-1-0716-3150-8, 978-1-0716-3153-9
ISBN (Electronic)978-1-0716-3151-5
DOIs
Publication statusPublished - 2023
SeriesMethods in Molecular Biology
ISSN1064-3745

Keywords

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

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