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 in Book/Report/Conference proceedingChapter

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.

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
Chapter16
Pages161-175
ISBN (Electronic)9781493987931
ISBN (Print)9781493987924
DOIs
StatusE-pub ahead of print - 14 Nov 2018

Publication series

NameMethods in Molecular Biology
Volume1855

Keywords

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

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

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). New York, U. S. A.: Humana Press. 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; Williams, Robert J; James, Tony; Van Den Elsen, Johannes.

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 in Book/Report/Conference proceedingChapter

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). https://doi.org/10.1007/978-1-4939-8793-1_16
Pereira Morais, Marta ; Munir, Omar Kassaar ; Flower, Stephen ; Williams, Robert J ; James, Tony ; Van Den Elsen, Johannes. / Analysis of Protein Glycation Using Phenylboronate Acrylamide Gel Electrophoresis. Electrophoretic Separation of Proteins: Methods and Protocols. editor / Biji T. Kurien ; R Hal Scofield. New York, U. S. A. : Humana Press, 2018. pp. 161-175 (Methods in Molecular Biology).
@inbook{dd381b8773eb4588bf76a7506563dc78,
title = "Analysis of Protein Glycation Using Phenylboronate Acrylamide Gel Electrophoresis",
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.",
keywords = "Boronic acid, Flu-PAGE, Gel electrophoresis, Protein glycation, mP-AGE",
author = "{Pereira Morais}, Marta and Munir, {Omar Kassaar} and Stephen Flower and Williams, {Robert J} and Tony James and {Van Den Elsen}, Johannes",
year = "2018",
month = "11",
day = "14",
doi = "10.1007/978-1-4939-8793-1_16",
language = "English",
isbn = "9781493987924",
series = "Methods in Molecular Biology",
publisher = "Humana Press",
pages = "161--175",
editor = "{T. Kurien}, Biji and {Hal Scofield}, R",
booktitle = "Electrophoretic Separation of Proteins",
address = "USA United States",

}

TY - CHAP

T1 - Analysis of Protein Glycation Using Phenylboronate Acrylamide Gel Electrophoresis

AU - Pereira Morais, Marta

AU - Munir, Omar Kassaar

AU - Flower, Stephen

AU - Williams, Robert J

AU - James, Tony

AU - Van Den Elsen, Johannes

PY - 2018/11/14

Y1 - 2018/11/14

N2 - 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.

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.

KW - Boronic acid

KW - Flu-PAGE

KW - Gel electrophoresis

KW - Protein glycation

KW - mP-AGE

UR - http://www.scopus.com/inward/record.url?scp=85056501064&partnerID=8YFLogxK

U2 - 10.1007/978-1-4939-8793-1_16

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

M3 - Chapter

SN - 9781493987924

T3 - Methods in Molecular Biology

SP - 161

EP - 175

BT - Electrophoretic Separation of Proteins

A2 - T. Kurien, Biji

A2 - Hal Scofield, R

PB - Humana Press

CY - New York, U. S. A.

ER -