Glutathione S-transferase (transferase π) from human placenta is identical or closely related to glutathione S-transferase (transferase ϱ) from erythrocytes

Abstract

Glutathione S-transferase (RX: glutathione R-transferase, EC 2.5.1.18) from human placenta has been purified to homogeneity. This enzyme, transferase π, is an acidic protein (isoelectric point at pH 4.8) composed of two subunits. The molecular weights for the dimer and monomer were determined by independent methods as 47 000 and 23 400, respectively. These properties are not significantly different from those of glutathione S-transferase ϱ from human erythrocytes. Antibodies to transferase π reacted with the enzyme from erythrocytes but not with the basic transferases α-ϵ and the neutral transferase μ isolated from human liver. Antibodies to the latter enzymes did not react with the transferase from placenta. Further similarities between transferases π and ϱ appear in amino acid compositions, kinetic constants and substrate specificities. Both the placental and the erythrocyte enzyme have considerably higher activity with ethacrynic acid than any other of the human glutathione S-transferases. The glutathione S-transferase could be distinguished from two additional acidic glutathione-dependent enzymes, glyoxalase I and selenium-dependent glutathione peroxidase. It is concluded that transferase π from placenta is identical with or very closely related to transferase ϱ from erythrocytes.