Abstract

It has been suggested that human erythrocyte anionic glutathione S-transferase rho (GST-p) may be used as a marker of chemical exposure. In the present study, the activity of GST-p in human erythrocyte was measured after incubation of the erythrocytes with some common xenobiotics, and since it has also been suggested that human erythrocyte GST-p and human placental GST-π are identical, the effect of nicotine on purified human placental GST was also determined. Nicotine and cotinine caused an inhibition of the erythrocyte enzyme. There were no effects of malathion, monocrotophos or endosulfan on the erythrocyte enzyme activity. Acrolein, N-ethylmaleimide and styrene oxide, were confirmed as inhibitors of the enzyme.

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