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Assay of methylglyoxal-derived protein and nucleotide AGEs
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Rabbani, Naila, Shaheen, Fozia, Anwar, Attia, Masania, Jinit and Thornalley, Paul J. (2014) Assay of methylglyoxal-derived protein and nucleotide AGEs. Biochemical Society Transactions, 42 (2). pp. 511-517. doi:10.1042/BST20140019
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Official URL: http://dx.doi.org/10.1042/BST20140019
Abstract
Glyoxalase- and methylglyoxal-related research has required the development of quantitative and reliable techniques for the measurement of methylglyoxal-derived glycation adducts of protein and DNA. There are also other glycation adducts, oxidation adducts and nitration adducts of proteins and oxidation adducts of DNA. Proteolysis of protein releases glycation, oxidation and nitration free adducts (glycated, oxidized and nitrated amino acids) in plasma and nuclease digestion of DNA releases glycated and oxidized nucleosides into plasma and other body fluids for excretion in urine. The gold standard method for quantifying these adducts is stable isotopic dilution analysis LC–MS/MS. Protein and DNA adduct residues are determined by assay of enzymatic hydrolysates of protein and DNA extracts prepared using cocktails of proteases and nucleases respectively. Free adducts are determined by analysis of ultrafiltrates of plasma, urine and other physiological fluids. Protein damage markers (13 glycation adducts, five oxidation adducts and 3-nitrotyrosine) and DNA damage markers (three glycation adducts and one oxidation adduct) are quantified using 25 μg of protein, 10 μg of DNA or 5 μl of physiological fluid. Protein and nucleotide AGE (advanced glycation end-product) assay protocols resistant to interferences is described.
| Item Type: | Journal Article | ||||
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| Subjects: | Q Science > QD Chemistry Q Science > QH Natural history > QH426 Genetics |
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| Divisions: | Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School > Biomedical Sciences > Translational & Experimental Medicine > Metabolic and Vascular Health (- until July 2016) Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School |
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| Library of Congress Subject Headings (LCSH): | Glycosylation, Oxidation , Nitration, DNA adducts | ||||
| Journal or Publication Title: | Biochemical Society Transactions | ||||
| Publisher: | Portland Press Ltd | ||||
| ISSN: | 1470-8752 | ||||
| Official Date: | 14 January 2014 | ||||
| Dates: |
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| Volume: | 42 | ||||
| Number: | 2 | ||||
| Page Range: | pp. 511-517 | ||||
| DOI: | 10.1042/BST20140019 | ||||
| Status: | Peer Reviewed | ||||
| Publication Status: | Published | ||||
| Access rights to Published version: | Restricted or Subscription Access |
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