Journal article · Book chapter
Affinity Electrophoresis for Analysis of Catalytic Module-Carbohydrate Interactions
University of Michigan, Ann Arbor1
Department of Chemical and Biochemical Engineering, Technical University of Denmark2
Center for BioProcess Engineering, Department of Chemical and Biochemical Engineering, Technical University of Denmark3
Department of Biotechnology and Biomedicine, Technical University of Denmark4
Enzyme and Protein Chemistry, Section for Protein Chemistry and Enzyme Technology, Department of Biotechnology and Biomedicine, Technical University of Denmark5
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.
| Language: | English |
|---|---|
| Publisher: | Springer |
| Year: | 2017 |
| Pages: | 119-127 |
| Series: | Methods in Molecular Biology |
| Journal subtitle: | Methods and Protocols |
| ISBN: | 149396898X , 149396898x , 1493968998 , 9781493968985 and 9781493968992 |
| ISSN: | 19406029 and 10643745 |
| Types: | Journal article and Book chapter |
| DOI: | 10.1007/978-1-4939-6899-2_9 |
| ORCIDs: | Wilkens, Casper and Svensson, Birte |
Affinity electrophoresis Carbohydrate binding module Dissociation constant Polyacrylamide gel electrophoresis Polysaccharide Protein Binding Surface binding site
