The possible role of glutathione S‐transferases (GST) in detoxification of fatty acid epoxides generated during lipid peroxidation has been evaluated. Present studies showed that cytosolic human glutathione S‐transferases belonging to α, H, and μ classes isolated from human liver and lung catalyzed the conjugation of glutathione and 9,10‐epoxystearic acid. The product of enzymatic reaction, i.e., conjugate of GSH and epoxystearic acid, was isolated and characterized. The Michaelis constant (Km) values of the α, μ, and π classes of GSTs for 9,10‐epoxystearic acid were found to be 0.47, 0.32 and 0.80 mM, respectively, whereas the maximal velocity (V max) values for the α, μ, and π classes of GSTs were found to be 142, 256, and 52 mol/min/mol, respectively. These results indicate that even though 9,10‐epoxystearic acid is a substrate for all the three classes of GSTs, the μ class isozymes have maximum activity toward this substrate and may preferentially metabolize fatty acid epoxides more effectively as compared to the other classes of GSTs.
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