Structure-function relationship in glycosylated alpha-chymotrypsin as probed by IMAC and IMACE.

作者信息

Jiang K Y, Pitiot O, Anissimova M, Adenier H, Vijayalakshmi M A

机构信息

Laboratoire d'Interactions Moléculaires et de Technologie des Séparations (LIMTech.S), Université de Technologie de Compiègne, CNRS-UPRES A 6022, Centre de Recherche de Royallieu BP 529, 60 205, Compiègne, Cedex, France.

出版信息

Biochim Biophys Acta. 1999 Aug 17;1433(1-2):198-209. doi: 10.1016/s1388-1981(99)00087-6.

DOI:10.1016/s1388-1981(99)00087-6

PMID:10446372

Abstract

Chemical glycosylation of bovine alpha-chymotrypsin, by a glucosamine adduct on the carboxyl group, results in the modification of its catalytic activity. The structural alterations of alpha-chymotrypsin resulting from its glycosylation are studied by immobilized metal-ion affinity chromatography (IMAC) and immobilized metal-ion affinity capillary electrophoresis (IMACE). The chemical glycosylation of alpha-chymotrypsin generates two distinct subpopulations of the protein: one which totally loses the initial affinity for IDA-Cu(II) and another which exhibits an increased affinity for the metal chelate ligand.

摘要