Analysis of Protein Glycation Using Phenylboronate Acrylamide Gel Electrophoresis

Marta Pereira Morais, Omar Kassaar Munir, Stephen Flower, Robert J Williams, Tony James, Johannes Van Den Elsen

Research output: Chapter or section in a book/report/conference proceedingChapter or section

1 Citation (SciVal)


Carbohydrate modification of proteins adds complexity and diversity to the proteome. However, undesired carbohydrate modifications also occur in the form of glycation, which have been implicated 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 specialized equipment and complex data analysis. In this chapter, we describe two easy-to-use electrophoresis-based methods that will enable researchers to detect, identify, and analyze these posttranslational 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.

Original languageEnglish
Title of host publicationElectrophoretic Separation of Proteins
Subtitle of host publicationMethods and Protocols
EditorsBiji T. Kurien, R Hal Scofield
Place of PublicationNew York, U. S. A.
PublisherHumana Press
ISBN (Electronic)9781493987931
ISBN (Print)9781493987924
Publication statusE-pub ahead of print - 14 Nov 2018

Publication series

NameMethods in Molecular Biology


  • Boronic acid
  • Flu-PAGE
  • Gel electrophoresis
  • Protein glycation
  • mP-AGE

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics


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