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protein carbonyl

Pathology: - metal catalyzed oxidation of proteins introduces carbonyl groups (aldehydes & ketones) at Lys, Arg, Pro or Thr residues in a site-specific manner - the oxidative modification of proteins can induce structural changes that effect function & turnover - measurement of protein carbonyls (OxyBlot) has provided support for the free radical theory of aging

References

  1. Stadtman ER, Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions. Ann Rev Biochem 62:797, 1993 PMID: 8352601
  2. Farber JM & Levine RL. Sequence of a peptide susceptible to mixed-function oxidation. Probable cation binding site in glutamine synthetase. J Biol Chem 261:4574, 1986 PMID: 2870062 Free full text
  3. Levine RL. Oxidative modification of glutamine synthetase. I. Inactivation is due to loss of one histidine residue. J Biol Chem. 1983 Oct 10;258(19):11823-7. PMID: 6137483 Free Article - Levine RL. Oxidative modification of glutamine synthetase. II. Characterization of the ascorbate model system. J Biol Chem. 1983 Oct 10;258(19):11828-33. PMID: 6137484 Free Article
  4. Oliver CN, Ahn BW, Moerman EJ, Goldstein S, Stadtman ER. Age-related changes in oxidized proteins. J Biol Chem 262:5488, 1987 PMID: 3571220 Free full text
  5. Smith CD, Carney JM, Starke-Reed PE et al Excess brain protein oxidation and enzyme dysfunction in normal aging and in Alzheimer disease. Proc Natl Acad Sci U S A. 1991 Dec 1;88(23):10540-3. PMID: 1683703 Free PMC Article
  6. Starke-Reed PE, Oliver CN. Protein oxidation and proteolysis during aging and oxidative stress. Arch Biochem Biophys 275:559, 1989 PMID: 2574564