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Molecular & Cellular Proteomics 3:1145-1153, 2004.
© 2004 by The American Society for Biochemistry and Molecular Biology, Inc.

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Research

Proteomic Analysis of Arginine Adducts on Glyoxal-modified Ribonuclease^*

William E. Cotham, Thomas O. Metz, P. Lee Ferguson, Jonathan W. C. Brock, Davinia J. S. Hinton, Suzanne R. Thorpe, John W. Baynes and Jennifer M. Ames^,¶

From the Department of Chemistry and Biochemistry, University of South Carolina, Columbia, SC 29208; and Hugh Sinclair Unit of Human Nutrition, School of Food Biosciences, The University of Reading, Whiteknights, Reading RG6 6AP, United Kingdom

Accumulation 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. Arg³⁹ and Arg⁸⁵, 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 Arg¹⁰, while Arg³³ appeared to be unmodified. We conclude that dihydroxyimidazolidine adducts are the primary products of modification of protein by glyoxal, that Arg³⁹ and Arg⁸⁵ 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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