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Glycobiology vol 7 no 1 pp. 31-36, 1997
© 1997

research-article

Proton NMR study of triantennary complex type N-linked glycan chains: assignment of proton chemical shifts of the ß-Man residue in a basic unit of the triantennary glycan chain having a GlcNAcß1->6Man{alpha}1->6Manß->sequence

Tomohiko Taguchi, Yutaka Muto, Ken Kitajima, Shigeyuki Yokoyama, Sadako Inoue1 and Yasuo Inoue1,2

Department of Biophysics and Biochemisny, Graduate School of Science, University of Tokyo Tokyo-113, Japan
1Institute of Biological Chemistiy, Academia Sinica Taipei, Taiwan

2To whom correspondence should be addressed

Received on March 29, 1996; revised on July 22, 1996; accepted on August 11, 1996

The chemical shifts of ring protons of the ß-Man residue in a triantennary complex type N-linked glycan chain having a GlcNAcß1->6(GlcNAcß1->2)Man{alpha}1ß6Manß 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 ß-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 GlcNAcß1->2Man{alpha}1->6Manß sequence, but quite close to that (3.86 ppm) of a pentaantennary glycan containing a GlcNAcß1->6 residue on the Man{alpha}1->6Manß sequence. Thus, the addition of GlcNAcß1->6 residue on the Man-4' residue, whose formation is catalyzed by GlcNAc transferase V, is considered to cause a down-field shift of ß-Man H4 in the complex-type N-glycan chains. One possible explanation of this phenomenon is that the conformation of Man{alpha}1->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.

triantennary N-linked glycan 2D 1H-NMR GlcNAc transferase V conformation of N-linked glycan


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