Cross specificity in some vertebrate and insect glutathione transferases with methyl parathion (dimethyl p nitrophenyl phosphorothionate), 1 chloro 2,4 dinitrobenzene and S crotonyl N acetylcysteamine as substrates

Abstract

Enzymes catalysing the reaction between GSH and methylparathion (dimethyl p nitrophenyl phosphorothionate), 1 chloro 2,4 dinitrobenzene and S crotonyl N acetylcysteamine were separated by (NH4)2SO4 precipitation from homogenates of sheep, rat and mouse livers and from homogenates of cockroaches, houseflies and grass grubs. Electrofocusing of the preparations from each of these species separated a number of zones, each of which catalysed the reaction of GSH with all three substrates. Ion exchange chromatography on CM cellulose also separated a number of fractions in which activity towards the three substrates coincided. In both separation methods patterns of the activities were consistent with the presence in all species of several GSH transferases each having a degree of cross specificity towards the three substrates.