用于分析催化模块与碳水化合物相互作用的亲和电泳

Affinity Electrophoresis for Analysis of Catalytic Module-Carbohydrate Interactions.

作者信息

Cockburn Darrell, Wilkens Casper, Svensson Birte

机构信息

Department of Microbiology and Immunology, University of Michigan, 1150 W Medical Center Drive, Ann Arbor, MI, 48109, USA.

Department of Chemical and Biochemical Engineering, Technical University of Denmark, Kongens Lyngby, Denmark.

出版信息

Methods Mol Biol. 2017;1588:119-127. doi: 10.1007/978-1-4939-6899-2_9.

DOI:10.1007/978-1-4939-6899-2_9

PMID:28417364

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.

摘要

亲和电泳长期以来一直用于研究蛋白质与大的可溶性配体之间的相互作用。人们发现该技术在检测蛋白质（尤其是碳水化合物结合模块，即CBMs）与多糖的结合方面具有很大的实用性。近年来，蛋白质（大多是酶）的碳水化合物表面结合位点也通过这种方法进行了研究。在此，我们描述了一种用于鉴定酶催化模块与多种碳水化合物配体之间结合相互作用的方案。