論文

2019年6月

Expression, purification, and characterization of highly active endo-α-N-acetylgalactosaminidases expressed by silkworm-baculovirus expression system

Journal of Asia-Pacific Entomology
  • Akihiro Morio
  • ,
  • Jian Xu
  • ,
  • Akitsu Masuda
  • ,
  • Yurie Kinoshita
  • ,
  • Masato Hino
  • ,
  • Daisuke Morokuma
  • ,
  • Hatsumi M. Goda
  • ,
  • Nozomu Okino
  • ,
  • Makoto Ito
  • ,
  • Hiroaki Mon
  • ,
  • Ryosuke Fujita
  • ,
  • Takahiro Kusakabe
  • ,
  • Jae Man Lee

22
2
開始ページ
404
終了ページ
408
記述言語
掲載種別
研究論文(学術雑誌)
DOI
10.1016/j.aspen.2019.01.009

© 2019 Korean Society of Applied Entomology The O-glycosidase, endo-α-N-acetylgalactosaminidase from Enterococcus faecalis (endoEF) catalyzes the cleavage of core 1 and core 3 type O-linked disaccharides between GalNAc and serine or threonine residues from glycoproteins. The endoEF has broad substrate specificity and thus is extensively utilized for the structural and functional analysis of the O-linked glycans. In this study, we expressed and purified the recombinant endoEF (rEndoEF) by using the silkworm-baculovirus expression vector system (Silkworm-BEVS) and confirmed the deglycosylation activity of rEndoEF targeting reporter glycoproteins, which was equivalent to the commercial O-glycosidase. Thus, our study provides important clues to produce highly active rEndoEF O-glycosidases employing silkworm-BEVS as an alternative.

リンク情報
DOI
https://doi.org/10.1016/j.aspen.2019.01.009
Scopus
https://www.scopus.com/record/display.uri?eid=2-s2.0-85062386153&origin=inward
Scopus
https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85062386153&origin=inward
Scopus Citedby
https://www.scopus.com/inward/citedby.uri?partnerID=HzOxMe3b&scp=85062386153&origin=inward