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Analysis of Protein Glycation Using Phenylboronate Acrylamide Gel Electrophoresis by Marta P. Pereira Morais; Julia D. Mackay; Savroop K. Bhamra; J. Grant Buchanan; Tony D. James; John S. Fossey; Jean M. H. van den Elsen is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract The incorporation of the specialized carbohydrate affinity ligand methacrylamido phenylboronic acid in polyacrylamide gels for SDS‐PAGE analysis has been successful for the separation of carbohydrates and has here been adapted for the analysis of post‐translationally modified proteins. While conventional SDS‐PAGE analysis cannot distinguish between glycated and unglycated proteins, methacrylamido phenylboronate acrylamide gel electrophoresis (mP‐AGE) in low loading shows dramatic retention of δ‐gluconolactone modified proteins, while the mobility of the unmodified proteins remains unchanged. With gels containing 1% methacrylamido phenylboronate, mP‐AGE analysis of gluconoylated recombinant protein Sbi results in the retention of the modified protein at a position expected for a protein that has quadrupled its expected molecular size. Subsequently, mP‐AGE was tested on HSA, a protein that is known to undergo glycation under physiological conditions. mP‐AGE could distinguish between various carbohydrate‐protein adducts, using __in vitro__ glycated HSA, and discriminate early from late glycation states of the protein. Enzymatically glycosylated proteins show no altered ret

Who reads Analysis of Protein Glycation Using Phenylboronate Acrylamide Gel Electrophoresis?

Author

Marta P. Pereira Morais; Julia D. Mackay; Savroop K. Bhamra; J. Grant Buchanan; Tony D. James; John S. Fossey; Jean M. H. van den Elsen

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Ltd.; Wiley; Research Square (ISSN 1615-9853)

Published

2009

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)