Enzymatic Conjugation of Epoxides with Glutathione

Abstract

Glutathione epoxide transferase has been isolated in homogeneous form from the livers of male Sprague-Dawley rats. The enzyme is active in the conjugation of glutathione with a large number of compounds bearing an ethylene oxide ring in the terminal portion of an alkyl chain. The enzyme has a molecular weight of 40,000 and is composed of 2 subunits. Several proteins which catalyze the same reaction are demonstrated. Some of these forms, present in the purified enzyme, are interconvertible by freezing and by treatment with ethylenediaminetetraacetate.