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. 1990 Jul;69(1):99-102.

In vitro interaction of mercury, copper (II) and cadmium with human glutathione transferase pi

M M Almar  1 , P J Dierickx
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  • PMID: 2218073

In vitro interaction of mercury, copper (II) and cadmium with human glutathione transferase pi

M M Almar et al. Res Commun Chem Pathol Pharmacol. 1990 Jul.

Abstract

The in vitro interaction of mercury, copper (II) and cadmium with human glutathione transferase (GST) pi was studied using reduced glutathione (GSH) and 1-chloro-2,4-dinitrobenzene as substrate. Tumor specific human GST pi was isolated from the human hepatoma derived PLC/PRF/5 cell line. The inhibition of the GST pi activity was dose dependent. Kinetic studies never revealed competitive inhibition. A parabolic inhibition was found with GSH as the variable substrate. The heavy metals are spontaneously conjugated with GSH and cysteine, but interact with GST pi by direct binding to this protein. This binding could have a protective function against heavy metals.

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