Mass spectrometry to detect the site specificity of advanced glycation/lipoxidation end-product formation on protein: some challenges and solutions

Ames, Jenny (2008) Mass spectrometry to detect the site specificity of advanced glycation/lipoxidation end-product formation on protein: some challenges and solutions. Biochemical Society Transactions, 36. pp. 1051-1054. ISSN 0300-5127

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Official URL: http://dx.doi.org/10.1042/BST0361051

Abstract

Formation of AGEs (advanced glycation end-products) and ALEs (advanced lipoxidation end-products) on proteins is associated with aging and various diseases of oxidative stress, notably diabetes and its complications. Modification of protein to AGE/ALEs is known to be site-directed and this has potential implications for protein functionality and design of AGE/ALE inhibitors. Determination of the site-specificity of modification is achieved most efficiently by MS. The present paper summarizes some of the challenges that need to be addressed when determining the site-specificity of AGE/ALE formation on protein by MS, using the protein RNase as an example. The following topics are discussed: formation and significance of AGE/ALEs, location of glycated peptides, enzymic digestion of glycated peptides and selection of mass spectrometric settings of analysis for glycated peptides.

Item Type: Article
Subjects: C700 Molecular Biology, Biophysics and Biochemistry
Department: Faculties > Health and Life Sciences > School of Life Sciences > Applied Sciences
Depositing User: EPrints Services
Date Deposited: 11 Feb 2010 13:59
Last Modified: 10 Aug 2015 11:46
URI: http://nrl.northumbria.ac.uk/id/eprint/526

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