Proteomic analysis of arginine adducts on glyoxal-modified ribonucleaseCotham, W.E., Metz, T.O., Ferguson, P.L., Brock, J.W.C., Hinton, D.J.S., Thorpe, S.R., Baynes, J.W. and Ames, J.M. (2004) Proteomic analysis of arginine adducts on glyoxal-modified ribonuclease. Molecular & Cellular Proteomics, 3 (12). pp. 1145-1153. ISSN 1535-9476 Full text not archived in this repository. It is advisable to refer to the publisher's version if you intend to cite from this work. See Guidance on citing. To link to this item DOI: 10.1074/mcp.M400002-MCP200 Abstract/SummaryAccumulation of advanced glycation end-products (AGEs) on proteins is associated with the development of diabetic complications. Although the overall extent of modification of protein by AGEs is limited, localization of these modifications at a few critical sites might have a significant effect on protein structure and function. In the present study, we describe the sites of modification of RNase by glyoxal under physiological conditions. Arg(39) and Arg(85), which are closest to the active site of the enzyme, were identified as the primary sites of formation of the glyoxal-derived dihydroxyimidazolidine and hydroimidazolone adducts. Lower amounts of modification were detected at Arg(10), while Arg(33) appeared to be unmodified. We conclude that dihydroxyimidazolidine adducts are the primary products of modification of protein by glyoxal, that Arg(39) and Arg(85) are the primary sites of modification of RNase by glyoxal, and that modification of arginine residues during Maillard reactions of proteins is a highly selective process.
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