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Structure determination by 360-MHz 1H-NMR spectroscopy and methylation analysis of a biantennary glycan of the N-acetyllactosaminic type isolated from rat-liver plasma membrane.

Authors
  • Debray, H
  • Fournet, B
  • Montreuil, J
  • Dorland, L
  • Vliegenthart, F C
Type
Published Article
Journal
European journal of biochemistry / FEBS
Publication Date
Apr 01, 1981
Volume
115
Issue
3
Pages
559–563
Identifiers
PMID: 7238520
Source
Medline
License
Unknown

Abstract

Glycopeptides obtained by exhaustive pronase digestion of delipidated rat liver plasmic membranes were purified by gel filtration on Sephadex G-25. These glycopeptides were further fractionated by affinity chromatography on a concanavalin-A--Sepharose 4B column into the following fractions: (a) glycopeptides which did not bind to the column (fraction 1); (b) glycopeptides with weak affinity for concanavalin-A--Sepharose, which could be eluted with buffer only (fraction 2); (c) glycopeptides retained on the column and which could be eluted specifically with buffer containing 0.2 M methyl alpha-glucoside (fraction 3). On the basis of the carbohydrate composition, methylation analysis and 360-MHz 1H-NMR spectroscopy, the following primary structure of a glycan in fraction 2 is proposed: (see formula in text).

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