Analysis of protein glycation using phenylboronate acrylamide gel electrophoresis

Marta P Pereira Morais; John S Fossey; Tony D James; Jean M H van den Elsen

doi:10.1007/978-1-61779-821-4_9

Analysis of protein glycation using phenylboronate acrylamide gel electrophoresis

Marta P Pereira Morais, John S Fossey, Tony D James, Jean M H van den Elsen

Chemistry

Research output: Contribution to journal › Article › peer-review

6 Citations (Scopus)

Abstract

Carbohydrate modification of proteins adds complexity and diversity to the proteome. However, undesired carbohydrate modifications also occur in the form of glycation, resulting 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 specialised equipment and complex data analysis. In this chapter, we describe a simple electrophoresis-based method that enables users to detect, identify, and analyze these post-translational 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 and glycosylation disorders.

Original language	English
Pages (from-to)	93-109
Number of pages	17
Journal	Methods in molecular biology
Volume	869
DOIs	https://doi.org/10.1007/978-1-61779-821-4_9
Publication status	Published - 2012

UN SDGs

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

Access to Document

10.1007/978-1-61779-821-4_9

Cite this

@article{c2acd77d6d7d422a85a8b3205f1db3f7,

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, resulting 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 specialised equipment and complex data analysis. In this chapter, we describe a simple electrophoresis-based method that enables users to detect, identify, and analyze these post-translational 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 and glycosylation disorders.",

author = "Morais, {Marta P Pereira} and Fossey, {John S} and James, {Tony D} and {van den Elsen}, {Jean M H}",

year = "2012",

doi = "10.1007/978-1-61779-821-4_9",

language = "English",

volume = "869",

pages = "93--109",

journal = "Methods in molecular biology",

issn = "1940-6029",

publisher = "Springer",

}

TY - JOUR

T1 - Analysis of protein glycation using phenylboronate acrylamide gel electrophoresis

AU - Morais, Marta P Pereira

AU - Fossey, John S

AU - James, Tony D

AU - van den Elsen, Jean M H

PY - 2012

Y1 - 2012

N2 - Carbohydrate modification of proteins adds complexity and diversity to the proteome. However, undesired carbohydrate modifications also occur in the form of glycation, resulting 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 specialised equipment and complex data analysis. In this chapter, we describe a simple electrophoresis-based method that enables users to detect, identify, and analyze these post-translational 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 and glycosylation disorders.

AB - Carbohydrate modification of proteins adds complexity and diversity to the proteome. However, undesired carbohydrate modifications also occur in the form of glycation, resulting 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 specialised equipment and complex data analysis. In this chapter, we describe a simple electrophoresis-based method that enables users to detect, identify, and analyze these post-translational 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 and glycosylation disorders.

U2 - 10.1007/978-1-61779-821-4_9

DO - 10.1007/978-1-61779-821-4_9

M3 - Article

C2 - 22585480

SN - 1940-6029

VL - 869

SP - 93

EP - 109

JO - Methods in molecular biology

JF - Methods in molecular biology

ER -

Analysis of protein glycation using phenylboronate acrylamide gel electrophoresis

Abstract

UN SDGs

Access to Document

Fingerprint

Cite this