International Journal of Industrial Entomology and Biomaterials

Korean Society of Sericultural Science (한국잠사학회)
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Molecular Cloning and Characterization of a Muscle-Specific Lipase from the Bumblebee Bombus ignitus

  • Hu, Zhigang (College of Natural Resources and Life Science, Dong-A University) ;
  • Wang, Dong (College of Natural Resources and Life Science, Dong-A University) ;
  • Lu, Wei (College of Natural Resources and Life Science, Dong-A University) ;
  • Cui, Zheng (Joint Laboratory between Dong-A University and Shenyang Pharmaceutical University, Shenyang Pharmaceutical University) ;
  • Jia, Jing-Ming (Joint Laboratory between Dong-A University and Shenyang Pharmaceutical University, Shenyang Pharmaceutical University) ;
  • Yoon, Hyung-Joo (Department of Agricultural Biology, National Institute of Agricultural Science and Technology) ;
  • Sohn, Hung-Dae (College of Natural Resources and Life Science, Dong-A University) ;
  • Kim, Doh-Hoon (College of Natural Resources and Life Science, Dong-A University) ;
  • Jin, Byung-Rae (College of Natural Resources and Life Science, Dong-A University)
  • Published : 2008.09.30
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Abstract

A muscle-specific lipase gene of the bumblebee Bombus ignitus was cloned and characterized. This gene, which we named Bi-Lipase, consists of seven exons encoding 317 amino acid residues. Bi-Lipase possesses all the features of lipases, including GXSXG consensus motif and Ser-Asp-His catalytic triad. Expressed as a 37-kDa polypeptide in baculovirus-infected insect Sf9 cells, recombinant Bi-Lipase showed an optimal pH of 9.0 and exhibited its highest catalytic activity at $40^{\circ}C$. Furthermore, through the addition of tunicamycin to the recombinant virus-infected Sf9 cells, recombinant Bi-Lipase was found to be N-glycosylated. Northern and western blot analyses indicated that Bi-Lipase was expressed in the wing, thorax, and leg muscles. These results show that Bi-Lipase is a muscle-specific lipase, suggesting a possible role of Bi-Lipase in the utilization of lipids for muscular activity in B. ignitus.

Keywords

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