Expression, purification and characterization of yeast protein disulfide isomerase produced by a recombinant baculovirus-mediated silkworm, Bombyx mori, pupae expression system

被引:0
作者
Liyun Wang
Yuri Shimizu
Takemitsu Mizunaga
Shogo Matsumoto
Yuzuru Otsuka
机构
[1] Ochanomizu University,Institute of Environmental Science for Human Life, Department of Food and Nutritional Sciences
[2] Discovery Research Institute,Molecular Entomology Laboratory
来源
Biotechnology Letters | 2008年 / 30卷
关键词
Baculovirus; Glycosylation; Protein disulfide isomerase; Protein expression; Silkworm pupae;
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学科分类号
摘要
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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页码:625 / 630
页数:5
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