350-kDa royal jelly glycoprotein (Apisin), which stimulates proliferation of human monocytes, bears the β1-3galactosylated N-glycan: Analysis of the N-glycosylation site

Mariko Kimura, Yoshinobu Kimura, Kazunori Tsumura, Kiyoshi Okihara, Hiroyuki Sugimoto, Hideo Yamada, Masami Yonekura

Research output: Contribution to journalArticle

49 Citations (Scopus)


While doing a structural analysis of minor component N-glycans linked to 350-kDa royal jelly glycoprotein (RJGP), which stimulates the proliferation of human monocytes, we found that a Galβ1-3GlcNAcβ1-4Man unit occurs on the insect glycoprotein. The structure of the fluorescence-labeled N-glycan was analyzed by sugar component analysis, IS-MS, and 1H-NMR. The structural analysis showed that the 350-kDa RJGP bears Galβ1- 3GlcNAcβ1-4(GlcNAcβ1-2)Manα1-3 (Manα1-3Manα1-6) Manβ1-4GlcNAcβ1-4GlcNAc, suggesting this insect glycoprotein is one of the substrates for both β1-3 galactosyl and β1-4 N-acetyl- glucosamininyl transferases. To our knowledge, this is the first report that succeeded in identifing an insect glycoprotein bearing the β1-3 galactosylated N-glycan.

Original languageEnglish
Pages (from-to)2055-2058
Number of pages4
JournalBioscience, Biotechnology and Biochemistry
Issue number9
Publication statusPublished - Sep 1 2003



  • Apis mellifera
  • Insect glycoprotein
  • N-glycosylation
  • Royal jelly
  • Site analysis

ASJC Scopus subject areas

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

Cite this