TY - JOUR
T1 - Affinity Electrophoresis for Analysis of Catalytic Module-Carbohydrate Interactions
AU - Cockburn, Darrell W.
AU - Wilkens, Casper
AU - Svensson, Birte
N1 - Publisher Copyright:
© 2023. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.
PY - 2023
Y1 - 2023
N2 - 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.
AB - 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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U2 - 10.1007/978-1-0716-3151-5_6
DO - 10.1007/978-1-0716-3151-5_6
M3 - Article
C2 - 37149524
AN - SCOPUS:85158032319
SN - 1064-3745
VL - 2657
SP - 91
EP - 101
JO - Methods in molecular biology (Clifton, N.J.)
JF - Methods in molecular biology (Clifton, N.J.)
ER -