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Glutathione S-transferases Y<sub>c</sub>Y<sub>fetus</sub> and Y<sub>c</sub>Y<sub>c</sub> - kinetic and inhibitor studies relating to their glutathione peroxidase activities
Abstract
The kinetic properties of the glutathione (GSH) peroxidase activities of GSH S-transferases YcYfetus and YcYc were compared. The catalytic efficiency of the fetal iso-enzyme with cumene hydroperoxide as substrate was approximately four times higher than the other. The effects of the non-substrate ligand rose-Bengal as well as the substrate ligands sulphobromophthalein and acrolein on the GSH peroxidase activity of these two iso-enzymes were also investigated. Depending on the ligand, the inhibition profiles of these two iso-enzymes when measured with either the peroxidase substrate, cumene hydroperoxide or the standard GSH S-transferase substrate 1:chloro-2,4-dinitrobenzene were found to be either very similar (sulphobromophthalein) or markedly different (rose Bengal and acrolein). Significantly, the GSH peroxidase activity of the fetal iso-enzyme was far less susceptible to inhibition by the teratogen, acrolein, than that of the YcYc isoenzyme. It is therefore attractive to suggest that should a similar situation arise in vivo, this resistance to peroxidase inhibition may play a role in preventing the fetotoxic effects of acrolein.
