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Study of an unusual advanced glycation end-product (AGE) derived from glyoxal using mass spectrometry
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Lopez-Clavijo, Andrea, Duque-Daza, Carlos A., Romero-Canelón, Isolda, Barrow, Mark P., Kilgour, David P. A., Rabbani, Naila, Thornalley, Paul J. and O’Connor, Peter B. (2014) Study of an unusual advanced glycation end-product (AGE) derived from glyoxal using mass spectrometry. Journal of The American Society for Mass Spectrometry, Volume 25 (Number 4). pp. 673-683. doi:10.1007/s13361-013-0799-2 ISSN 1044-0305.
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Official URL: http://dx.doi.org/10.1007/s13361-013-0799-2
Abstract
Glycation is a post-translational modification (PTM) that affects the physiological properties of peptides and proteins. In particular, during hyperglycaemia, glycation by α-dicarbonyl compounds generate α-dicarbonyl-derived glycation products also called α-dicarbonyl-derived advanced glycation end products. Glycation by the α-dicarbonyl compound known as glyoxal was studied in model peptides by MS/MS using a Fourier transform ion cyclotron resonance mass spectrometer. An unusual type of glyoxal-derived AGE with a mass addition of 21.98436 Da is reported in peptides containing combinations of two arginine-two lysine, and one arginine-three lysine amino acid residues. Electron capture dissociation and collisionally activated dissociation results supported that the unusual glyoxal-derived AGE is formed at the guanidino group of arginine, and a possible structure is proposed to illustrate the 21.9843 Da mass addition.
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