Detoxification of Styrene Oxide by Human Liver Glutathione Transferase

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Abstract
Cytosolic glutathione transferase (GST) was investigated in four human livers. The profile of GST activity was determined by isoelectric focusing using 1-chloro-2,4-dinitrobenzene as the electrophilic substrate. Three livers contained at least one basic and a near-neutral isoenzyme (GST μ). GSTμ was not detectable in the fourth liver. The kinetics of GST with styrene oxide as the electrophilic substrate were studied in the cytosolic fraction, with the pooled fractions from isoelectric focusing containing high activity of GSTμ transferase, and with GSTμ purified to homogeneity. The cytosol obeyed Michaelis-Menten kinetics when styrene oxide was used as the variable substrate. The average (± s.e.m.) of the Vmax and Kmwere 21.9 ± 7.9 nmol min-1mg-1and 4.9 ± 0.4 mM, respectively. At varying concentrations of glutathione, the enzyme did not obey Michaelis-Menten kinetics. Such kinetics were also observed with the fractions from isoelectric focusing and with the homogeneous GSTμ fraction. The Eadie-Hofstee plot showed two phases: one with a low and another with a high Kmvalue.The apparent Kmvalues for the cytosol were 0.035 ± 0.022 and 0.88 ± 0.36 mM. The kinetic pattern of purified GSTμ is consistent with that found in the cytosol.

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