Purification of acidic glutathione S-transferases from human lung, placenta and erythrocyte and the development of a specific radioimmunoassay for their measurement

Abstract

Human acidic glutathione S-transferases (GST) have been purified from placenta, lung and erythrocytes. The purification protocol resulted in a high yield of pure protein for each tissue, when compared to previous procedures. An apparent subunit Mr of 24,800 was calculated for each of the acidic GST and each enzymes had a pI of 4.75. No immunochemical differences were detected between the acidic GST isolated from the three tissues. A specific and sensitive radioimmunoassay suitable for the measurement of human acidic GST in plasma or tissues is described.