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- Title
Expression, Purification, and Characterization of Endo-β- N-Acetylglucosaminidase H Using Baculovirus-Mediated Silkworm Protein Expression System.
- Authors
Mitsudome, Takumi; Xu, Jian; Nagata, Yudai; Masuda, Atsushi; Iiyama, Kazuhiro; Morokuma, Daisuke; Li, Zhiqing; Mon, Hiroaki; Lee, Jae; Kusakabe, Takahiro
- Abstract
Endo-β- N-acetylglucosaminidase (Endo H) from Streptomyces plicatus hydrolyzes the core di-GlcNAc units of asparagine-linked oligosaccharides and is regarded as an important tool for glycobiology research. In the present study, we established a large-scale system to produce secreted Endo H using a silkworm-baculovirus expression system (silkworm-BES). The recombinant Endo H purified from silkworm hemolymph had activity comparable to that from recombinant Escherichia coli. As well as its well-characterized substrate RNase B, the Endo H from silkworm-BES was able to deglycosylate the high-mannose glycoproteins from silkworm hemolymph. Interestingly, the secretion amount of recombinant Endo H was significantly varied among the different silkworm strains, which could provide valuable information for larger-scale protein productions from silkworm-BES.
- Subjects
N-acetylglucosaminidase; STREPTOMYCES; ASPARAGINE; OLIGOSACCHARIDES; SILKWORMS; HEMOLYMPH
- Publication
Applied Biochemistry & Biotechnology, 2014, Vol 172, Issue 8, p3978
- ISSN
0273-2289
- Publication type
Article
- DOI
10.1007/s12010-014-0814-5