Analysis of protein glycation using fluorescent phenylboronate gel electrophoresis
Scientific Reports2013Vol. 3(1), pp. 1437–1437
Citations Over TimeTop 23% of 2013 papers
Marta P. Pereira Morais, Dominic C. Marshall, Stephen E. Flower, Christopher J. Caunt, Tony D. James, Robert J. Williams, Nicholas R. Waterfield, Jean van den Elsen
Abstract
Glycated proteins are important biomarkers for age-related disorders, however their analysis is challenging because of the complexity of the protein-carbohydrate adducts. Here we report a method that enables the detection and identification of individual glycated proteins in complex samples using fluorescent boronic acids in gel electrophoresis. Using this method we identified glycated proteins in human serum, insect hemolymph and mouse brain homogenates, confirming this technique as a powerful proteomics tool that can be used for the identification of potential disease biomarkers.
Related Papers
- → Simultaneous characterization of SNPs and N-glycans from multiple glycosylation sites of intact β-2-glycoprotein-1 (B2GP1) by ESI-qTOF-MS(2019)7 cited
- → Glycation of human γB-crystallin: A biophysical investigation(2016)8 cited
- → Impaired Immunoglobulin G Fc Fragment Function in Diabetics is Caused by a Mechanism Different from Glycation(1994)8 cited
- → Protein Glycosylation: The Basic Science(2009)3 cited
- → Skin Aging, Glycation and Glycation Inhibitors(2013)2 cited