We have tested the ability of a representative range of dietary glucosinolates and their breakdown products, found in high concentrations in cruciferous vegetables, to act as blocking agents against carcinogenesis by inducing the activity of the anticarcinogenic phase II marker enzyme quinone reductase in murine hepa1c1c7 cells. Breakdown of glucosinolates was catalysed by the endogenous plant enzyme thioglucoside glucohydrolase at neutral and acid pH. Only two unmodified glucosinolates, p-hydroxybenzyl and 2-hydroxybut-3-enyl, significantly induced quinone reductase activity. However, after enzymic hydrolysis at near-neutral pH, some of the glucosinolates yielded breakdown products that significantly induced quinone reductase in the order: 3-methylsulphinylpropyl→prop-2-enyl→pent-4enyl ∼ 2-phenylethyl ∼ benzyl → all others tested. Incubation with myrosinase at acidic pH resulted in induction of quinone reductase activity by the hydrolysis products of only three of the tested glucosinolates: 3-methylsulphinylpropyl∼ 2-phenylethyl → benzyl → all others, activity due to the two alkenyl compounds being lost. The results show that the potential cancer-blocking action of both intact and thioglucoside glucohydrolase-treated glucosinolates, as assessed by induction of phase II enzyme activity, is dependent on the nature of the side chain of the parent glucosinolate.