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 chromatog raphv 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 α‐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: (Formula Presented.) Copyright © 1981, Wiley Blackwell. All rights reserved
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CITATION STYLE
DEBRAY, H., FOURNET, B., MONTREUIL, J., DORLAND, L., & VLIEGENTHART, J. F. C. (1981). 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. European Journal of Biochemistry, 115(3), 559–563. https://doi.org/10.1111/j.1432-1033.1981.tb06239.x
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