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
- 3 March 2005
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 115 (3) , 559-563
- https://doi.org/10.1111/j.1432-1033.1981.tb06239.x
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 [Con] A-Sepharose 4B column into the following fractions: glycopeptides which did not bind to the column (fraction 1); glycopeptides with weak affinity for Con A-Sepharose, which could be eluted with buffer only (fraction 2); and 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 primary structure of a glycan in fraction 2 is proposed.This publication has 34 references indexed in Scilit:
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