Free radical reactions with proteins and enzymes: the inactivation of pepsin.
The reactions of free radicals produced by ionizing radiation with pepsin have been studied by steady-state inactivation measurements and by pulse radiolysis. In de-aerated solutions thehydroxyl radical has been found to be the most efficient of the primary free radicals generated from water in causing inactivation. The reactions of the more selective oxidizing inorganic radical anions Br2-. and (SCN)2-., with pepsin have also beenexamined. In the case of the thiocyanate radical anion (SCN)2-., the inactivation efficiency is found to depend on SCN- concentration, an effect shown to arise from a reversible redox reaction involving the tryptophan and (SCN)2-. radicals. The results demonstrate that tryptophan residue plays an essential role in the enzyme activity of pepsin.
D001128:Argon; D001966:Bromine; D003037:Cobalt Radioisotopes; D004307:Dose-Response Relationship, Radiation; D005609:Free Radicals; D005720:Gamma Rays; D009609:Nitrous Oxide; D010100:Oxygen; D010434:Pepsin A / Q000528:radiation effects*; D011675:Pulse Radiolysis; D012996:Solutions; D013861:Thiocyanates; D014867:Water
D003037:Cobalt Radioisotopes; D005609:Free Radicals; D012996:Solutions; D013861:Thiocyanates; D014867:Water; D001128:Argon; D010434:Pepsin A; D009609:Nitrous Oxide; D010100:Oxygen; D001966:Bromine