Abstract
Rat liver soluble fraction catalyzes the formation of a conjugate of glutathione and [ 3H]benzo(a)-4,5-oxide. The conjugate was isolated by thin-layer chromatography and identified by its radioactivity and its ninhydrin reactivity. When both [ 3H]benzo(a)-pyrene-4,5-oxide and [ 14C]glutathione were used, the radioactivity from each precursor was in the conjugate. The reaction was linear with protein concentration from 10 to 500 μg protein. Transferase activity was pH dependent, and sensitive to heat and pronase digestion. The amount of nonenzymatic conjugation was negligible under all the conditions described. This procedure measures a key enzyme in polycylic hydrocarbon metabolism and its activity may relate to the efficiency of detoxification of active carcinogenic intermediates.
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