Expression,purification and characterization of yeast protein disulfide isomerase produced by a recombinant baculovirus-mediated silkworm, <Emphasis Type="Italic">Bombyx mori</Emphasis>, pupae expression system |
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| Authors: | Liyun Wang Yuri Shimizu Takemitsu Mizunaga Shogo Matsumoto Yuzuru Otsuka |
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| Institution: | (1) Institute of Environmental Science for Human Life, Department of Food and Nutritional Sciences, Ochanomizu University, 2-1-1 Ohtsuka, Bunkyo-ku, Tokyo 112-8610, Japan;(2) Molecular Entomology Laboratory, Discovery Research Institute, Riken, 2-1, Hirosawa, Wako Saitama, 351-0198, Japan |
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| Abstract: | Protein disulfide isomerase (PDI) is a multifunctional polypeptide presents in the endoplasmic reticulum of the cell. Silkworm
(Bombyx mori) pupae were used as hosts to produce recombinant PDI (rPDI). The concentration-dependent chaperone activity of rPDI was evidenced
by the inhibition of the aggregation of rhodanese. Approximately 297 μg rPDI was purified from a single silkworm pupa. Results
of rPDI treated with endoglycosidase H and N-glycanase, PNGase F, indicate that non-N-glycosylated rPDI (occupying 90%) and N-glycosylated rPDI are expressed in the silkworm expression system. The difference in glycosylation between silkworm pupae
and yeast is discussed. |
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| Keywords: | Baculovirus Glycosylation Protein disulfide isomerase Protein expression Silkworm pupae |
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