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Implication of Protein Oxidation in Protein Turnover, Aging, and Oxygen Toxicity

  • E. R. Stadtman
  • C. N. Oliver
  • R. L. Levine
  • L. Fucci
  • A. J. Rivett
Part of the Basic Life Sciences book series (BLSC, volume 49)

Abstract

A number of enzymatic and nonenzymatic mixed-function oxidation (MFO) systems catalyze the oxidation of enzymes.1–6 With oxidation, the enzymes are converted to catalytically inactive or less active forms that are more sensitive to heat denaturat ion7 and to proteolytic degradation.8–11 Enzyme oxidation is likely the basis of some normal biological functions, e.g., in the killing of bacteria by neutrophils, in limitation of the inflammatory response, in controlling the switch from anaerobic to aerobic metabolism, and in the regulation of the turnover of some enzymes. Enzyme oxidation also might be implicated in a variety of pathological disorders, including arthritis, aging, carcinogenesis, broncho-pulmonary dysplasia and adult respiratory distress syndrome, retinopathy of prematurity, and reperfusion-mediated ischemic damage.

Keywords

Glutamine Synthetase Protein Oxidation Histidine Residue Adult Respiratory Distress Syndrome Metal Binding Site 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1988

Authors and Affiliations

  • E. R. Stadtman
    • 1
  • C. N. Oliver
    • 1
  • R. L. Levine
    • 1
  • L. Fucci
    • 1
  • A. J. Rivett
    • 1
  1. 1.Laboratory of Biochemistry, National Heart, Lung, and Blood InstituteNational Institutes of HealthBethesdaUSA

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