Abstract
The glutathione transferase (GST) activity in the cytosol of the water flea Daphnia magna Straus was partially purified by glutathione affinity chromatography. Chromatofocusing on the Polybuffer exchangers 94 and 118 separated the GST isoenzymes in one neutral and four cationic forms, and some minor fractions one of which was an anionic form. The major GST isoenzymes were partially characterized by different biochemical parameters. The water pollutants 2,4-dichlorophenoxyacetic acid and 1,4-benzoquinone inhibited the water flea GST isoenzymes, following the same kinetic inhibition patterns as for rat liver GST. It is concluded that water flea GST can play an important role in the detoxification of aquatic pollutants.
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