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In vitro effect of arsenical compounds on glutathione-related enzymes

journal contribution
posted on 2001-01-01, 00:00 authored by S Chouchane, E Snow
The mechanism of arsenic toxicity is believed to be due to the ability of arsenite (AsIII) to bind protein thiols. Glutathione (GSH) is the most abundant cellular thiol, and both GSH and GSH-related enzymes are important antioxidants that play an important role in the detoxification of arsenic and other carcinogens. The effect of arsenic on the activity of a variety of enzymes that use GSH has been determined using purified preparations of glutathione reductase (GR) from yeast and bovine glutathione peroxidase (GPx) and equine glutathione S-transferase (GST). The effect on enzyme activity of increasing concentrations (from 1 μM to 100 mM) of commercial sodium arsenite (AsIII) and sodium arsenate (AsV) and a prepared arsenic(III)−glutathione complex [AsIII(GS)3] and methylarsenous diiodide (CH3AsIII) has been examined.

History

Journal

Chemical research in toxicology

Volume

14

Issue

5

Pagination

517 - 522

Publisher

American Chemical Society

Location

Washington, D.C.

ISSN

0893-228X

Language

eng

Publication classification

C1 Refereed article in a scholarly journal

Copyright notice

2001, American Chemical Society

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