Affordable Access

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
Type
Published Article
Journal
European journal of biochemistry / FEBS
Publication Date
Volume
115
Issue
3
Pages
559–563
Identifiers
PMID: 7238520
Source
Medline

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).

There are no comments yet on this publication. Be the first to share your thoughts.

Statistics

Seen <100 times
0 Comments