Glutathione adducts of helenalin and 11 alpha,13-dihydrohelenalin acetate inhibit glutathione S-transferase from horse liver.

摘要: The 2-mono- and 2,13-bis-glutathionyl adducts of helenalin the 2-monoglutathionyl adduct 11 alpha,13-dihydrohelenalin acetate were previously shown to be formed by spontaneous Michael addition at physiological pH. In living cells, glutathione (GSH) conjugation many types electrophilic agents is catalysed a family GSH S-transferase enzymes (GST). capability from horse liver catalyze reaction other helenanolides with was investigated. enzyme did not accelerate helenalin, alpha,13-dihydrohelenalin, or 2-deacetyl-6-deoxychamissonolide. GSH-adducts, reaction, found inhibitors this enzyme. Free potent inhibitor containing free sulfhydryl groups, show any inhibitory activity on GST. It thus demonstrated that GSH-adducts sesquiterpene lactones possess their own specific biological activity. Two further using as substrate, reductase glyoxalase I, influenced its GSH-adducts.