Purification and characterization of a glutathione S-transferase from the fungus Cunninghamella elegans.

@article{Cha2001PurificationAC,
  title={Purification and characterization of a glutathione S-transferase from the fungus Cunninghamella elegans.},
  author={C. J. Cha and Brian F. Coles and Carl Cerniglia},
  journal={FEMS microbiology letters},
  year={2001},
  volume={203 2},
  pages={257-61}
}
Cunninghamella elegans grown on Sabouraud dextrose broth had glutathione S-transferase (GST) activity. The enzyme was purified 172-fold from the cytosolic fraction (120000 x g) of the extract from a culture of C. elegans, using Q-Sepharose ion exchange chromatography and glutathione affinity chromatography. The GST showed activity against 1-chloro-2,4-dinitrobenzene, 1,2-dichloro-4-nitrobenzene, 4-nitrobenzyl chloride, and ethacrynic acid. Sodium dodecyl sulfate-polyacrylamide gel… CONTINUE READING