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Proteomic analysis of arginine adducts on glyoxal-modified ribonuclease.

Publication ,  Journal Article
Cotham, WE; Metz, TO; Ferguson, PL; Brock, JWC; Hinton, DJS; Thorpe, SR; Baynes, JW; Ames, JM
Published in: Molecular & cellular proteomics : MCP
December 2004

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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Published In

Molecular & cellular proteomics : MCP

DOI

EISSN

1535-9484

ISSN

1535-9476

Publication Date

December 2004

Volume

3

Issue

12

Start / End Page

1145 / 1153

Related Subject Headings

  • Trypsin
  • Time Factors
  • Spectrometry, Mass, Electrospray Ionization
  • Ribonucleases
  • Peptides
  • Models, Chemical
  • Kinetics
  • Imidazoles
  • Glyoxal
  • Dithiothreitol
 

Citation

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Cotham, W. E., Metz, T. O., Ferguson, P. L., Brock, J. W. C., Hinton, D. J. S., Thorpe, S. R., … Ames, J. M. (2004). Proteomic analysis of arginine adducts on glyoxal-modified ribonuclease. Molecular & Cellular Proteomics : MCP, 3(12), 1145–1153. https://doi.org/10.1074/mcp.m400002-mcp200
Cotham, William E., Thomas O. Metz, P Lee Ferguson, Jonathan W. C. Brock, Davinia J. S. Hinton, Suzanne R. Thorpe, John W. Baynes, and Jennifer M. Ames. “Proteomic analysis of arginine adducts on glyoxal-modified ribonuclease.Molecular & Cellular Proteomics : MCP 3, no. 12 (December 2004): 1145–53. https://doi.org/10.1074/mcp.m400002-mcp200.
Cotham WE, Metz TO, Ferguson PL, Brock JWC, Hinton DJS, Thorpe SR, et al. Proteomic analysis of arginine adducts on glyoxal-modified ribonuclease. Molecular & cellular proteomics : MCP. 2004 Dec;3(12):1145–53.
Cotham, William E., et al. “Proteomic analysis of arginine adducts on glyoxal-modified ribonuclease.Molecular & Cellular Proteomics : MCP, vol. 3, no. 12, Dec. 2004, pp. 1145–53. Epmc, doi:10.1074/mcp.m400002-mcp200.
Cotham WE, Metz TO, Ferguson PL, Brock JWC, Hinton DJS, Thorpe SR, Baynes JW, Ames JM. Proteomic analysis of arginine adducts on glyoxal-modified ribonuclease. Molecular & cellular proteomics : MCP. 2004 Dec;3(12):1145–1153.

Published In

Molecular & cellular proteomics : MCP

DOI

EISSN

1535-9484

ISSN

1535-9476

Publication Date

December 2004

Volume

3

Issue

12

Start / End Page

1145 / 1153

Related Subject Headings

  • Trypsin
  • Time Factors
  • Spectrometry, Mass, Electrospray Ionization
  • Ribonucleases
  • Peptides
  • Models, Chemical
  • Kinetics
  • Imidazoles
  • Glyoxal
  • Dithiothreitol