Structural Features of N-Glycans Linked to Royal Jelly Glycoproteins: Structures of high-mannose type, hygrid type, and biantennary type glycans

• KIMURA Yoshinobu

  Department of Bioresources Chemistry, Faculty of Agriculture, Okayama University

• MIYAGI Chiyoko

  Department of Bioresources Chemistry, Faculty of Agriculture, Okayama University

• KIMURA Mariko

  Department of Bioresources Chemistry, Faculty of Agriculture, Okayama University

• NITODA Teruhiko

  Department of Bioresources Chemistry, Faculty of Agriculture, Okayama University

• KAWAI Nobuyuki

  Yamada Bee Farm

• SUGIMOTO Hiroyuki

  Yamada Bee Farm

書誌事項

タイトル別名

• Structural Features of N-Glycans Linked to Royal Jelly Glycoproteins: Structures of high-mannose type, hybrid type, and biantennary type glycans.
• Structural Features of<i>N</i>-Glycans Linked to Royal Jelly Glycoproteins: Structures of high-mannose type, hybrid type, and biantennary type glycans

抄録

  The structures of N-glycans of total glycoproteins in royal jelly have been explored to clarify whether antigenic N-glycans occur in the famous health food. The structural feature of N-glycans linked to glycoproteins in royal jelly was first characterized by immunoblotting with an antiserum against plant complex type N-glycan and lectin-blotting with Con A and WGA. For the detail structural analysis of such N-glycans, the pyridylaminated (PA-) N-glycans were prepared from hydrazinolysates of total glycoproteins in royal jelly and each PA-sugar chain was purified by reverse-phase HPLC and size-fractionation HPLC. Each structure of the PA-sugar chains purified was identified by the combination of two-dimensional PA-sugar chain mapping, ESI-MS and MS/MS analyses, sequential exoglycosidase digestions, and 500 MHz ¹H-NMR spectrometry.<br>   The immunoblotting and lectinblotting analyses preliminarily suggested the absence of antigenic N-glycan bearing β1-2 xylosyl and/or α1-3 fucosyl residue(s) and occurrence of β1-4GlcNAc residue in the insect glycoproteins.<br>   The detailed structural analysis of N-glycans of total royal jelly glycoproteins revealed that the antigenic N-glycans do not occur but the typical high mannose-type structure (Man_9~4GlcNAc₂) occupies 71.6% of total N-glycan, biantennary-type structures (GlcNAc₂Man₃GlcNAc₂) 8.4%, and hybrid type structure (GlcNAc₁Man₄GlcNAc₂) 3.0%. Although the complete structures of the remaining 17% N-glycans; C4, (HexNAc₃Hex₃HexNAc₂: 3.0%), D2 (HexNAc₂Hex₅HexNAc₂: 4.5%), and D3 (HexNAc₃Hex₄HexNAc₂: 9.5%) are still obscure so far, ESI-MS analysis, exoglycosidase digestions by two kinds of β-N-acetylglucosaminidase, and WGA blotting suggested that these N-glycans might bear a β1-4 linkage N-acetylglucosaminyl residue.<br>

収録刊行物

• Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ

  Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ 64 (10), 2109-2120, 2000

  公益社団法人 日本農芸化学会

キーワード

• royal jelly
• insect glycoprotein
• <i>N</i>-glycan glycoform
• antigenic <i>N</i>-glycan

詳細情報

• CRID: 1390001206472885632
• NII論文ID: 110002679784
• NII書誌ID: AA10824164
• DOI: 10.1271/bbb.64.2109
• COI: 1:CAS:528:DC%2BD3cXnvVOht7k%3D
• ISSN: 13476947
• ISSN: 09168451
• ISSN: http://id.crossref.org/issn/09168451
• NDL書誌ID: 5557752
• PubMed: 11129583
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I5557752
• Web Site: http://www.tandfonline.com/doi/pdf/10.1271/bbb.64.2109
• 本文言語コード: en
• データソース種別:
  • JaLC
  • NDL
  • Crossref
  • PubMed
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可