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Purification and biochemical characterization of a novel glutathione S-transferase of the silkworm, <i>Bombyx mori</i>
Abstract
A novel glutathione S-transferase has been purified from Bombyx mori larvae using affinity chromatography on a glutathione agarose column. The purified enzyme appeared as a single band on SDS-PAGE and had a Mr of 28 kDa. Steady state kinetic assays of the enzyme were conducted with 1-
chloro-2,4-dinitrobenzene as a substrate. The Km, Vmax, Kcat and Kcat/Km for the purified BmGST were 0.494 mM, 72.07 mmol/min/mg, 65.43 s-1 and 132.45 mM-1·s-1, respectively. The enzyme had a maximum activity at approximately pH 7.1 and 25ºC. BmGST indicated lower inhibitory rate by some inhibitors (albendazol, praziquantel, bile acid and NaCl), suggesting that this novel BmGST could differ structurally or functionally from other animal GSTs.
chloro-2,4-dinitrobenzene as a substrate. The Km, Vmax, Kcat and Kcat/Km for the purified BmGST were 0.494 mM, 72.07 mmol/min/mg, 65.43 s-1 and 132.45 mM-1·s-1, respectively. The enzyme had a maximum activity at approximately pH 7.1 and 25ºC. BmGST indicated lower inhibitory rate by some inhibitors (albendazol, praziquantel, bile acid and NaCl), suggesting that this novel BmGST could differ structurally or functionally from other animal GSTs.
