Glutathione S-transferase in human lymphoid cell lines and fractionated peripheral leucocytes.

Glutathione S-transferase activity was identified in cytosol from human lymphoid-cell lines and peripheral leucocytes (polymorphonuclear-leucocyte/monocyte and small-lymphocyte fractions) and compared with human liver enzyme. The findings of closely similar elution volume in gel filtration, substrate (1-chloro-2,4-dinitrobenzene) and inhibitory (probenecid) kinetics indicate that the liver, leucocyte and lymphoid-cell transferases are closely related. The interaction of reduced glutathione and 1-chloro-2,4-dinitrobenzene was shown to occur in intact-lymphoid-cell culture, to be linear with time and quantity of cells and to have kinetics similar to those of the enzyme reaction catalysed by cytosol.