Affordable Access

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

Authors
  • Cha, C J
  • Coles, B F
  • Cerniglia, C E
Type
Published Article
Journal
FEMS microbiology letters
Publication Date
Sep 25, 2001
Volume
203
Issue
2
Pages
257–261
Identifiers
PMID: 11583857
Source
Medline
License
Unknown

Abstract

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 electrophoresis gel filtration chromatography revealed that the native enzyme was homodimeric with a subunit of M(r) 27000. Comparison by Western blot analysis implied that this fungal GST had no relationship with mammalian alpha-, mu-, and pi-class GSTs, although it showed a small degree of cross-reactivity with a theta-class GST. The N-terminal amino acid sequence of the purified enzyme showed no significant homology with other known GSTs.

Report this publication

Statistics

Seen <100 times