THE EFFECT OF FENTON'S REAGENT ON TRYPSIN AND RIBONUCLEASE.

Abstract

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.

Document Details

Document Type
Technical Report
Publication Date
Jun 01, 1966
Accession Number
AD0635207

Entities

People

  • J. C. Perrone

Tags

DTIC Thesaurus Topics

  • Biomolecules
  • Chemical Compounds
  • Distillation
  • Enzymes
  • Enzymes And Coenzymes
  • Fractionation
  • Hydrolases
  • Molecules
  • Ribonuclease

Readers

  • Military Logistics and Supply Chain Management
  • Molecular and Cellular Biochemistry
  • Organic Chemistry