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Updated: May 22, 2026

Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases
Published on: December 26, 2011
Analysis of protein glycation using phenylboronate acrylamide gel electrophoresis
Marta P Pereira Morais1, John S Fossey, Tony D James
1Department of Biology and Biochemistry, University of Bath, Bath, UK. M.P.Pereira.Morais@bath.ac.uk
Abstract:
Carbohydrate modification of proteins adds complexity and diversity to the proteome. However, undesired carbohydrate modifications also occur in the form of glycation, resulting in diseases such as diabetes, Alzheimer's disease, autoimmune diseases, and cancer. The analysis of glycated proteins is challenging due to their complexity and variability. Numerous analytical techniques have been developed that require expensive specialised equipment and complex data analysis. In this chapter, we describe a simple electrophoresis-based method that enables users to detect, identify, and analyze these post-translational modifications. This new cost-effective methodology will aid the detection of unwanted glycation products in processed foods and may lead to new diagnostics and therapeutics for age-related chronic diseases and glycosylation disorders.
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