Document Type
Article
Publication Date
1-1-2001
Abstract
We have studied the interaction of the Gal-GalNAc-reactive champedak lectin-C with neuraminidase-treated and untreated IgA1 from IgA nephropathy patients. The binding ability of the lectin to untreated IgA1 from IgA nephropathy patients was significantly lower as compared to the untreated IgA1 from normal controls. This differential lectin-binding capacity was abrogated when the experiment was performed on neuraminidase-treated sera. Treatment of the serum IgA1 with neuraminidase also abrogated the differential charge distribution between the alpha -heavy chains of IgA nephropathy patients and normal controls. Copyright (C) 2001 S. Karger AG, Basel.
Keywords
IgA nephropathy, IgA1, Sialic acid, Lectin-C, α-Heavy chain, Two-dimensional gel electrophoresis
Publication Title
Nephron
Volume
89
Issue
4
Additional Information
Departments of Biochemistry and bMedicine, Faculty of Medicine, University of Malaya, Kuala Lumpur, Malaysia