protein carbonyl
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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
- ↑ 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: https://www.ncbi.nlm.nih.gov/pubmed/8352601
- ↑ 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: https://www.ncbi.nlm.nih.gov/pubmed/2870062 Free full text
- ↑ 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: https://www.ncbi.nlm.nih.gov/pubmed/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: https://www.ncbi.nlm.nih.gov/pubmed/6137484 Free Article - ↑ Oliver CN, Ahn BW, Moerman EJ, Goldstein S, Stadtman ER. Age-related changes in oxidized proteins. J Biol Chem 262:5488, 1987 PMID: https://www.ncbi.nlm.nih.gov/pubmed/3571220 Free full text
- ↑ 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: https://www.ncbi.nlm.nih.gov/pubmed/1683703 Free PMC Article
- ↑ Starke-Reed PE, Oliver CN. Protein oxidation and proteolysis during aging and oxidative stress. Arch Biochem Biophys 275:559, 1989 PMID: https://www.ncbi.nlm.nih.gov/pubmed/2574564