| Résumé: | Glutathione transferases (GSTs) obtained from University of Waterloo, Canada, were purified from Pseudomonas sp. UW4, by glutathione-affinity chromatography, identified through bioinformatic analysis and their substrate specificities were investigated. SDS-polyacrylamide gel electrophoresis revealed that the GST purified using Sulfobromophthalein-glutahione (BSP) affinity column resolved into a single band with low molecular weight (MW) of 17 kDa. Isoselectrofocusing showed it exists in single band with pI value of 6.1. Purified GST was reactive towards ethacrynic acid, 1-chloro-2,4-dinitrobenzene, cumene hydroxide and hydrogen peroxide, but no detectable activity with trans-2-octenal, hepta-2,4-dienal and trans-4-phenyl-3-butene-2-one. This demonstrated that putative GST possessed peroxidase activity but is not involved in lipid peroxidation. The purified GST suggested to be similar to PputUW4_00801 (putative glutathione S-transferase) of Pseudomonas sp. UW4.
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