Proton NMR study of triantennary complex type N-linked glycan chains: Assignment of proton chemical shifts of the β-Man residue in a basic unit of the triantennary glycan chain having a GlcNAcβ1→6Manα1→6Manβ→ sequence

Tomohiko Taguchi, Yutaka Muto, Ken Kitajima, Shigeyuki Yokoyama, Sadako Inoue, Yasuo Inoue

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

The chemical shifts of ring protons of the P-Man residue in a triantennary complex type N-linked glycan chain having a GlcNAcβ1→6(GlcNAcβ1→2)Manα1→6Manβ sequence were unambiguously determined by two-dimensional proton nuclear magnetic resonance (1H-NMR) spectroscopic methods. The chemical shift of H4 (3.84 ppm) of the β-Man residue was for the first time revealed to be different from those (~ 3.77 ppm) of biantennary and alternative type of triantennary glycans having a GlcNAcβ1→2Manα1→ 6Manβ sequence, but quite close to that (3.86 ppm) of a pentaantennary glycan containing a GlcNAcβ1→6 residue on the Manα1→6Manβ sequence. Thus, the addition of GlcNAcβ1→6 residue on the Man-4' residue, whose formation is catalyzed by GlcNAc transferase V, is considered to cause a down-field shift of β-Man H4 in the complex-type N-glycan chains. One possible explanation of this phenomenon is that the conformation of Manaα1→6 arm is folded back toward the proximal core region, as is the case with the complex-type N-glycan chains with the bisecting GlcNAc residue.

Original languageEnglish
Pages (from-to)31-36
Number of pages6
JournalGlycobiology
Volume7
Issue number1
DOIs
Publication statusPublished - 1997 Feb 1
Externally publishedYes

Keywords

  • 2D H-NMR
  • Conformation of N-Iinked glycan
  • GlcNAc transferase V
  • Triantennary N-linked glycan

ASJC Scopus subject areas

  • Biochemistry

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