Erifili Mosialou

TL;DR: It is shown that the protective effect of glutathione could be partly reversed by an inhibitor (100μM bromosulphophophtalein) of the enzyme, and apparently, rat liver musomal glutATHione transferase has the capacity to inhibit lipid peroxidation in a reconstituted system.

TL;DR: Molecular cloning and heterologous expression of rat GSTA5-5 has led to the demonstration that it exhibits substantially greater activity for AFB1-8,9-epoxide than other rat transferases, and a novel aflatoxin-aldehyde reductase (AFAR) that is similarly induced by ethoxyquin is identified.

TL;DR: Findings show that the enzyme can remove harmful products of lipid peroxidation and thereby possibly protect intracellular membranes against oxidative stress and could prove valuable in studying the factor responsible for glutathione-dependent protection against lipidperoxidation.

TL;DR: Microsomal glutathione transferase can detoxify a number of lipid peroxidation products as well as a fatty acid ozonide and imply a protective role for the enzyme under conditions of oxidative stress.

TL;DR: The glutathione peroxidase activity of the microsoma1 glutathion transferase may protect the organism from reactive hydroperoxides formed during oxidative stress and the significance of the extrahepatic enzyme needs to be studied.