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Glutathione transferase activity in some flagellates and amoebae, and purification of the soluble glutathione transferases from Acanthamoeba

Dierickx, P.J.; Almar, M.M.; De Jonckheere, J.F.

Biochemistry International 22(4): 593-600

1990

ISSN/ISBN: 0158-5231
PMID: 2078188
Document Number: 361371
Nine protozoans were investigated for their glutathione transferase (GST) content. Six aerobic amoebae (5 Acanthamoeba species and Naegleria andersoni jamiesoni) had very different specific GST activities, but an anaerobic amoeba (Entamoeba histolytica) and 2 anaerobic flagellates (Giardia lamblia, Trichomonas vaginalis) did not have any GST activity, suggesting that the peroxidase activity of GST is an evolutionarily important property for aerobic organisms. The soluble GST isoenzymes of A. culbertsoni and A. polyphaga were purified and partially characterized. The same 2 cationic and one anionic GST isoenzyme were found in both Acanthamoeba spp., while A. culbertsoni had one more cationic isoenzyme. It is concluded that GST in aerobic amoebae can play an important role in detoxication.

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