Anionic glutathione S-transferases were purified from human lung and placenta. Chemical and immunochemical characterization, including polyacrylamide-gel electrophoresis, gave strong evidence that the anionic lung and placental enzymes are chemically similar, if not identical, proteins. The electrophoretic mobilities of both proteins were identical in conventional alkaline gels as well as in ge...

l,3-Bis(2-chloroethyl)-l-nitrosourea (BCNU) is known to be detoxi fied by a denitrosation reaction catalyzed by glutathione-dependent en zymes in rat liver cytosol (R. E. Talcott and V. A. Levin, Drug Metab. Dispos., //: 175-176, 1983). Using a modification of their procedure, we have measured the ability of different purified rat glutathione transferase isoenzymes to denitrosate BCNU. The cata...

Three major forms of cytosolic glutathione S-transferase (designated F1, F2, and F3 transferases according to increasing isoelectric points) were purified to homogeneity from liver of DBA/2J mice, primarily by CM-cellulose and hydroxylapatite chromatography. The purified enzymes were shown to have specific activities of 104, 281, and 143 units/mg, respectively, when assayed with 1 m~ each of l-...