PMID: 9164863May 15, 1997Paper

Glutathione S-transferases from the white-rot fungus, Phanerochaete chrysosporium

The Biochemical Journal
C A DowdD Sheehan

Abstract

A glutathione S-transferase (GST) was purified to homogeneity from the white-rot fungus, Phanerochaete chrysosporium, by affinity chromatography on glutathione-agarose followed by Mono-Q ion-exchange FPLC. This protein immunoblotted with antisera to rat Theta class GST 5-5 and also showed N-terminal sequence similarity to the Theta class, including the presence of a conserved serine residue that has been specifically implicated in catalysis in this class [Wilce, Board, Feil and Parker (1995) EMBO J. 14, 2133-2143] and other residues conserved in plant sequences. Catalytic activity was found to be highly labile in the purified protein, although preliminary evidence for activity (approx. 120 m-units/mg) with 1,2-epoxy-3-(p-nitrophenoxy)propane was obtained in some preparations. The enzyme seems to be a dimer with a subunit molecular mass of 25 kDa by SDS/PAGE. The native molecular masses estimated by non-denaturing electrophoresis and by Superose-12 gel filtration were 58 and 45 kDa respectively. A second protein purified in this study also gave low level of activity with 1,2-epoxy-3-(p-nitrophenoxy)propane and had a subunit molecular mass of 28 kDa (native size 62-63 kDa), but did not immunoblot with any GST class and seemed to ...Continue Reading

Citations

Jun 12, 2009·Drug Metabolism Reviews·Viktor CvilinkLenka Skálová
Mar 31, 2017·BMC Genomics·Shirin SeifbarghiDwayne D Hegedus
Jan 7, 2003·Applied and Environmental Microbiology·Kajari DharJohn P N Rosazza
Sep 20, 2017·Ecotoxicology and Environmental Safety·Chaitali P LabadeVaijayanti A Tamhane
Jan 4, 2017·Environmental Science & Technology·Lounès HarouneJean-Philippe Bellenger

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