Glutathione transferase activity in some flagellates and amoebae, and purification of the soluble glutathione transferases from Acanthamoeba.
Glutathione transferase (GST) enzymes are toxicologically important from many points of view. Nine protozoans were investigated here for their GST content. Six aerobic amoebae had very different specific GST activities, but an anaerobic amoeba and two anaerobic flagellates 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 Acanthamoeba culbertsoni and A. polyphaga were purified and partially characterized. The same two cationic and one anionic GST isoenzyme were found in both Acanthamoeba ssp., while A. culbertsoni had one more cationic isoenzyme. It is concluded that GST in aerobic amoebae can play an important role in detoxication.
Dierickx
P J
PJ
Instituut voor Hygiëne en Epidemiologie, Brussel, Belgium.
Almar
M M
MM
De Jonckheere
J F
JF
D000048:Acanthamoeba / Q000201:enzymology*; D000656:Amoeba / Q000201:enzymology*; D000693:Anaerobiosis; D000818:Animals; D004748:Entamoeba histolytica / Q000201:enzymology; D005872:Giardia / Q000201:enzymology*; D005982:Glutathione Transferase / Q000302:isolation & purification / Q000378:metabolism*; D009253:Naegleria / Q000201:enzymology; D012995:Solubility; D014246:Trichomonas vaginalis / Q000201:enzymology*
D005982:Glutathione Transferase