Conjugation of polychlorinated agrochemical sulphoxides and sulphones by glutathione
1992
Dulik, D.M. | Huwe, J.K. | Bakke, J.E. | Connors, M.S. | Fenselau, C.
Pentachlorophenyl methyl sulphoxide and pentachlorophenyl methyl sulphone were found to be substrates for microsomal and cytosolic glutathione-S-transferase of rabbit, monkey, chicken and human liver, covalently immobilized on beaded sepharose. Protein was immobilized with >95% transferase activity, measured by dinitrochlorobenzene. Immobilized rabbit liver microsomal transferase activity was more stable than immobilized cytosolic activity. The sulphoxide moiety was displayed by glutathione in the presence of chicken liver microsomal protein. The sulphone moiety was displayed by glutathione in the formation of a diglutathione under catalysis by rhesus monkey liver cytosolic and microsomal protein. Chlorine was displaced by transferases from all species to form regioisomeric monoglutathiones. Qualitative and quantitative differences were observed in product distributions between species and between microsomal and cytosolic protein.
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