Abstract
Ribonuclease A (ribonucleate pyrimidine-nucleotido-2′-transferase (cyclizing), EC 2.7.7.16) was treated with Fe 2+ and H 2O 2 (Fenton's Reagent), a chemical source of hydroxyl radicals (OH·). H 2O 2 alone had little or no effect on ribonuclease A activity at low H 2O 2/ribonuclease A molar excesses. As the molar ratio increased (H 2O 2/ribonuclease A > 100) ribonuclease A was inactivated by H 2O 2; the magnitude of this effect increased with increased in H 2O 2 concentration and was enhanced with time. Fe 2+ and Fe 3+ alone had no effect on ribonuclease A activity. In an attempt to isolate the OH· effect, ribonuclease A was inactivated by Fe 2+ and H 2O 2 using a minimum excess of H 2O 2 and very short reaction time. Inactivation was a function of Fe 2+ concentration and was attributed to hydroxyl radicals. There was a nonlinear but reproducible relationship between molar ratio Fe 2+/ribonuclease A and degree of enzymic inactivation.
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