Abstract
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.
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Acknowledgments
We thank Alzheimer’s Research UK (ARUK-PPG2011B-17) and the Dunhill Medical Trust (DMT research grant R320/1113) for supporting this research.
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Pereira Morais, M.P., Kassaar, O., Flower, S.E., Williams, R.J., James, T.D., van den Elsen, J.M.H. (2019). Analysis of Protein Glycation Using Phenylboronate Acrylamide Gel Electrophoresis. In: Kurien, B., Scofield, R. (eds) Electrophoretic Separation of Proteins. Methods in Molecular Biology, vol 1855. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-8793-1_16
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DOI: https://doi.org/10.1007/978-1-4939-8793-1_16
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