| Abstract: | The detoxication of the enantiomers of glycidyl 4-nitrophenyl ether (GNPE), (?)-(R)- and (+)-(S)-GNPE, and glycidyl 1-naphthyl ether (GNE), (?)-(R)- and (+)-(S)-GNE, by rat liver glutathione transferase and epoxide hydrolase was studied. Enantioselectivity was observed with both enzymes favoring the (R)-isomers as determined by the formation of conjugate, diol, and remaining substrate measured by HPLC. Enantiomers of GNE were detoxified by cytosolic epoxide hydrolase but those of GNPE were not. Substantial nonenzymatically formed conjugates of enantiomers of GNPE were detected showing (S)-GNPE the more reactive of the pair. © 1993 Wiley-Liss, Inc. |
