Isolation, properties and tissue distribution of rat glutathione transferase E.

A simple small-scale purification procedure is described for GSH transferase E. This enzyme is shown to be a dimer of subunits of apparent Mr 28 500, to have an isoelectric point of pH 7.0, GSH transferase activity towards certain alkyl epoxides and alkyl halides, and to be the most active Se-independent GSH peroxidase so far described. It is present in a number of tissues, although at a low concentration. It is relatively abundant in the epididymis and the adrenal gland, but undetectable in lactating mammary gland and skeletal muscle. Its previously observed lability is confirmed.