Proteomic analysis of arginine adducts on glyoxal-modified ribonuclease.

Published

Journal Article

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.

Full Text

Duke Authors

Cited Authors

  • Cotham, WE; Metz, TO; Ferguson, PL; Brock, JWC; Hinton, DJS; Thorpe, SR; Baynes, JW; Ames, JM

Published Date

  • December 2004

Published In

Volume / Issue

  • 3 / 12

Start / End Page

  • 1145 - 1153

PubMed ID

  • 15377717

Pubmed Central ID

  • 15377717

Electronic International Standard Serial Number (EISSN)

  • 1535-9484

International Standard Serial Number (ISSN)

  • 1535-9476

Digital Object Identifier (DOI)

  • 10.1074/mcp.m400002-mcp200

Language

  • eng