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

doi:10.1007/978-1-4939-8793-1_16

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 proceeding › Chapter or section

1 Citation (SciVal)

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.

Original language	English
Title of host publication	Electrophoretic Separation of Proteins
Subtitle of host publication	Methods and Protocols
Editors	Biji T. Kurien, R Hal Scofield
Place of Publication	New York, U. S. A.
Publisher	Humana Press
Chapter	16
Pages	161-175
ISBN (Electronic)	9781493987931
ISBN (Print)	9781493987924
DOIs	https://doi.org/10.1007/978-1-4939-8793-1_16
Publication status	E-pub ahead of print - 14 Nov 2018

Publication series

Name	Methods in Molecular Biology
Volume	1855

Keywords

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

ASJC Scopus subject areas

Molecular Biology
Genetics

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Access to Document

10.1007/978-1-4939-8793-1_16

Cite this

Pereira Morais, M., Munir, O. K., Flower, S., Williams, R. J., James, T., & Van Den Elsen, J. (2018). Analysis of Protein Glycation Using Phenylboronate Acrylamide Gel Electrophoresis. In B. T. Kurien, & R. Hal Scofield (Eds.), Electrophoretic Separation of Proteins: Methods and Protocols (pp. 161-175). (Methods in Molecular Biology; Vol. 1855). Humana Press. Advance online publication. https://doi.org/10.1007/978-1-4939-8793-1_16

Analysis of Protein Glycation Using Phenylboronate Acrylamide Gel Electrophoresis. / Pereira Morais, Marta; Munir, Omar Kassaar; Flower, Stephen et al.
Electrophoretic Separation of Proteins: Methods and Protocols. ed. / Biji T. Kurien; R Hal Scofield. New York, U. S. A.: Humana Press, 2018. p. 161-175 (Methods in Molecular Biology; Vol. 1855).

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

Pereira Morais, M, Munir, OK, Flower, S , Williams, RJ , James, T & Van Den Elsen, J 2018, Analysis of Protein Glycation Using Phenylboronate Acrylamide Gel Electrophoresis. in B T. Kurien & R Hal Scofield (eds), Electrophoretic Separation of Proteins: Methods and Protocols. Methods in Molecular Biology, vol. 1855, Humana Press, New York, U. S. A., pp. 161-175. https://doi.org/10.1007/978-1-4939-8793-1_16

Pereira Morais M, Munir OK, Flower S , Williams RJ , James T , Van Den Elsen J. Analysis of Protein Glycation Using Phenylboronate Acrylamide Gel Electrophoresis. In T. Kurien B, Hal Scofield R, editors, Electrophoretic Separation of Proteins: Methods and Protocols. New York, U. S. A.: Humana Press. 2018. p. 161-175. (Methods in Molecular Biology). Epub 2018 Nov 14. doi: 10.1007/978-1-4939-8793-1_16

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AB - 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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Analysis of Protein Glycation Using Phenylboronate Acrylamide Gel Electrophoresis

Abstract

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Keywords

ASJC Scopus subject areas

UN SDGs

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Protein Glycation Biomarkers for Alzheimers Disease

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Analysis of Protein Glycation Using Phenylboronate Acrylamide Gel Electrophoresis

Abstract

Publication series

Keywords

ASJC Scopus subject areas

UN SDGs

Access to Document

Other files and links

Fingerprint

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Protein Glycation Biomarkers for Alzheimers Disease

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