Copper salt-dependent hydroxyl radical formation. Damage to proteins acting as antioxidants

Biochim Biophys Acta. 1983 Aug 23;759(1-2):38-41. doi: 10.1016/0304-4165(83)90186-1.

Abstract

Cupric ions (Cu2+) and ferric ions (Fe3+) added to hydrogen peroxide generate hydroxyl radicals (OH) capable of degrading deoxyribose with the formation of thiobarbituric acid-reactive products. This damage can be inhibited by catalase, OH radical scavengers and specific metal ion chelators. All proteins tested nonspecifically inhibited copper-dependent damage but have little effect on the iron-dependent reaction. Copper ions appear to bind to the proteins which prevents formation of OH radicals in free solution. However, OH radicals are still generated at a site-specific location on the protein molecule. Protein damage is detected as fluorescent changes in amino acid residues.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Albumins / metabolism
  • Animals
  • Antioxidants / metabolism*
  • Cattle
  • Copper / metabolism*
  • Deoxyribose / metabolism
  • Ferric Compounds / metabolism
  • Humans
  • Hydrogen Peroxide / metabolism
  • Papain / metabolism
  • Proteins / metabolism*
  • Rabbits
  • gamma-Globulins / metabolism

Substances

  • Albumins
  • Antioxidants
  • Ferric Compounds
  • Proteins
  • gamma-Globulins
  • Deoxyribose
  • Copper
  • Hydrogen Peroxide
  • Papain