International Journal of Industrial Entomology and Biomaterials

Korean Society of Sericultural Science (한국잠사학회)
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Baculovirus Expression and Biochemical Characterization of the Bombyx mori Protein Disulfide Isomerase (bPDI)

  • Goo, Tae-Won (Department of Sericulture and Entomology, The National Institute of Agriculture Science and Technology, R. D. A.) ;
  • Yun, Eun-Young (Department of Sericulture and Entomology, The National Institute of Agriculture Science and Technology, R. D. A.) ;
  • Kim, Sung-Wan (Department of Sericulture and Entomology, The National Institute of Agriculture Science and Technology, R. D. A.) ;
  • Park, Kwang-Ho (Department of Sericulture and Entomology, The National Institute of Agriculture Science and Technology, R. D. A.) ;
  • Hwang, Jae-Sam (Department of Sericulture and Entomology, The National Institute of Agriculture Science and Technology, R. D. A.) ;
  • Kwon, O-Yu (Department of Anatomy, College of Medicine, Chungnam National University) ;
  • Kang, Seok-Woo (Department of Sericulture and Entomology, The National Institute of Agriculture Science and Technology, R. D. A.)
  • Published : 2003.12.01
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Abstract

Protein disulfide isomerase (PDI) found in the endoplasmic reticulum (ER) catalyzes disulfide bond exchange and assists in protein folding of newly synthesized proteins. PDI also functions as a molecular chaperone and has been found to be associated with proteins in the ER. In addition, PDI functions as a subunit of two more complex enzyme systems: the prolyl-4-hydroxylase and the triacylglycerol transfer proteins. A cDNA that encodes protein disulfide isomerase was previously isolated from Bombyx mori (bPDI), in which open reading frame of 494 amino acids contained two PDI-typical thioredoxin active site of WCGHCK and an ER retention signal of the KDEL motif at its C-terminal, and we report its functional characterization here. This putative bPDI cDNA is expressed in insect Sf9 cells as a recombinant proteins using baculovirus expression vector system. The bPDI recombinant proteins are successfully recognized by antirat PDI antibody, and shown to be biologically active in vitro by mediating the oxidative refolding of reduced and scrambled RNase. This suggests that bPDI may play an important role in protein folding mechanism of insects.

Keywords

References

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