Purification and biochemical characterization of a novel glutathione S-transferase of the silkworm, Bombyx mori

文献类型： 外文期刊

第一作者： Hou, Cheng Xiang

作者： Hou, Cheng Xiang;Gui, Zhong Zheng;Fu, Zhi Qiang;Hou, Cheng Xiang;Gui, Zhong Zheng;Jin, Byung Rae

作者机构：

关键词： purification;characterization;glutathione S-transferase;Bombyx mori

期刊名称：AFRICAN JOURNAL OF BIOTECHNOLOGY （ 影响因子：0.573； 五年影响因子：0.794 ）

ISSN： 1684-5315

年卷期： 2008 年 7 卷 3 期

页码：

收录情况： SCI

摘要： 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 M-r of 28 kDa. Steady state kinetic assays of the enzyme were conducted with 1-chloro- 2,4- dinitrobenzene as a substrate. The K-m, V-max, K-cat and K-cat/ K-m for the purified BmGST were 0.494 mM, 72.07 mu mol/ 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 25 C. 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.

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