1977 Volume 25 Issue 12 Pages 3410-3414
Interaction of the 12, 13-epoxytrichothecenes and related mycotoxins with epoxide hydrolase and glutathione-S-transferase (GSH-S-transferase) from rat liver was examined in vitro. Neither hydrolysis of safrole oxide by the microsomal epoxide hydrolase nor conjugation of 2, 3-epoxy-(p-nitrophenoxy) propane with GSH by the soluble GSH-S-transferase was interfered with the trichothecenes such as T-2 toxin and fusarenon-X. Gas-liquid chromatography (GLC) analysis and colorimetric determination of the residual GSH revealed that the trichothecenes were inert to the partially purified GSH-S-transferase. In contrast to the trichothecenes, PR-toxin, an epoxide mycotoxin from Penicillium roqueforti, and lactones such as patulin and penicillic acid from Penicillium and Aspergillus spp., were found to react non-enzymatically with GSH in molar ratio of 1 : 1.