The mechanism by which 2(3)-tert-butyl-4-hydroxyanisole exerts anticarcinogenic and toxic effect in animals including human is believed to be the induction of detoxifying enzymes in the liver and other tissues. This study was designed to determine specific isozymes of glutathione S-transferase induced in rat liver by BHA. Administration of 0.75% BHA in diet for three days increased the concentration of glutathione and the activities of GSH S-transferase and of glutathione reductase in liver cytosol, while the activity of glutathione peroxidase was decreased by BHA treatment. Basic isozymes of GSH S-transferase $L_2$ and $A_2$ were induced significantly 1.35 and 1.50 fold, respectively by BHA administration. $B_2$, AC and $C_2$ isozymes were induced slightly more (8-12%)compared to the control group. But neutral/acidic isozymes of GSH S-transferase were reduced significantly 0.37 fold and BL isozyme was reduced slightly 0.90 fold by BHA administration. The activities of selenium-dependent glutathione peroxidase of $L_2$, BL, $B_2$ and $C_2$ was increased 1.46, 1.53, 1.19 and 1.61 fold, respectively. Selenium-independent peroxidase showed similar patterns of Se-dependent peroxidase except $L_2$ isozyme, that showed no difference between treated vs nontreated. Isozymes $L_2$, BL and $B_2$ showed 2-3 times-higher activities of Se-dependent peroxidase than those of Se-independent peroxidase but $A_2$, AC and $C_2$ isozyme revealed several folds more activities of Se-independent peroxidase than those of Se-dependent peroxidase.