African Journal of

  • Abbreviation: Afr. J. Biotechnol.
  • Language: English
  • ISSN: 1684-5315
  • DOI: 10.5897/AJB
  • Start Year: 2002
  • Published Articles: 12227

Full Length Research Paper

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

  Cheng Xiang Hou1,2, Zhi Qiang Fu3, Byung Rae Jin4 and Zhong Zheng Gui1,2*        
  1Jiangsu University of Science and Technology, Zhenjiang 212018, China. 2Sericultural Research Institute, Chinese Academy of Agricultural Sciences, Zhenjiang 212018, China. 3Shanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Shanghai 200232, China. 4College of Natural Resources and Life Science, Dong-A University, Pusan 604714, Korea.
Email: [email protected]

  •  Accepted: 10 January 2008
  •  Published: 05 February 2008



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 Mof 28 kDa. Steady state kinetic assays of the enzyme were conducted with 1-chloro-2,4-dinitrobenzene as a substrate. The KmVmaxKcat and Kcat/Kfor the purifiedBmGST 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.


Key words: Purification, characterization, glutathione S-transferase, Bombyx mori.