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© 1984 Oxford University Press

other

Induction of hepatic glutathione S-transferase activity by butylated hydroxyanisole and conjugation of benzo[a]pyrene diol-epoxide

Lennart Dock, Margareta Martinez and Bengt Jernström

Department of Forensic Medicine, Karolinska Institutet S-104 01 Stockholm, Sweden

Dietary administration of 2(3)-tert-butyl-4-hydroxyanisole (BHA) to mice caused an increase in the hepatic soluble glutathione S-transferase activity towards (±)-7ß, 8{alpha}-dihydroxy-9{alpha}, 10{alpha}-oxy-7,8,9,10-tetrahydrobenzo[a]pyrene (BPDE) of ~5-fold whereas that towards 1-chloro-2,4-dinitrobenzene (CDNB) was increased by ~14-fold. Whereas with either substrate the catalytic capacity of the enzyme was elevated by BHA treatment, there was little effect on the Km for CDNB but an increase in the Km for BPDE as substrates. The results thus suggest that BHA-induced GSH S-transferase activity may be of limited importance for protection from certain reactive intermediates of polycyclic aromatic hydrocarbons.


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