The Effect of Fenton's Reagent on Trypsin and Ribonuclease

摘要

The inactivation of trypsin by Fenton's reagent is very fast during the first few minutes of reaction: in the first three minutes of reaction about 50% of the activity is lost. However, the inactivation after this initial reaction period is much slower. Fractionation of the reaction mixture shows the presence of two main components: a fast fraction with little activity and a slower and more active fraction. Several authors have published experiments showing that partially damaged molecules are formed during the irradiation of proteins. It was possible to demonstrate that this is also true for trypsin treated with Fenton's reagent. Furthermore, trypsin after suffering this double treatment showed marked changes in its enzymatic characteristics. Cu(++) was found to have a marked influence on the inactivation of ribonuclease by Fenton's reagent.