Differential N-Glycan modifications of human alpha 1-acid glycoprotein (α1AGP) produced in different silkworm strains using the baculovirus expression system

研究成果: Contribution to journalArticle査読

1 被引用数 (Scopus)

抄録

N-glycosylation plays an important role in various biological activities and in the structural stability of serum glycoproteins. The baculovirus expression system (BES) is widely used to produce recombinant proteins but in some case it is not suitable for medical use because of the differences in N-linked glycans between insects and mammals. We reported that human serum protein alpha 1-acid protein (α1AGP) is effectively used as a model protein for evaluating the validity of engineering the insect-type N-glycosylation pathway. Using this protein, the productivity and N-linked glycan structures were compared among the 37 different silkworm strains. Interestingly, there was no difference in N-linked glycan structure among the silkworm strains, but there was difference in the degree of N-glycosylation.

本文言語英語
ページ(範囲)49-53
ページ数5
ジャーナルJournal of Insect Biotechnology and Sericology
84
2
DOI
出版ステータス出版済み - 11 11 2015

All Science Journal Classification (ASJC) codes

  • バイオテクノロジー
  • 応用微生物学とバイオテクノロジー
  • ビジネス、管理および会計(全般)
  • 農業および生物科学(全般)
  • 昆虫科学
  • 産業および生産工学

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