1H-NMR spectroscopic characterization of dansyl glyco-asparagines derived from hen egg white clycoproteins

doi:10.1007/BF01049271

Paper

1H-NMR spectroscopic characterization of dansyl glyco-asparagines derived from hen egg white clycoproteins

Published Sep 1, 1985 · H. Halbeek, J. Vliegenthart, H. Iwase

Glycoconjugate Journal

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4

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Abstract

Dansyl glyco-asparagines were prepared from a partially fractionated mixture of hen egg white glycoproteins. Reverse-phase high performance liquid chromatography (HPLC) on a silica-based octadecyl column yielded ten such derivatives in a virtually pure state. The detailed structures of the glyco-asparagines were identified by 500-MHz1H nuclear magnetic resonance (NMR) spectroscopy. Two of them were found to be of the oligomannosideN-type, four were of the intersected-hybridN-type and another four were of the intersected multi-antennaryN-type. In monogalactosylated, intersected structures the galactose residue was proved by1H-NMR to be attached in β(1–4)-linkage to the GlcNAcβ1-4Manα1–3 branch.Dansyl glyco-asparagines turned out to be suitable derivatives for1H-NMR spectroscopic analysis. The combination of HPLC and high-resolution NMR spectroscopy of such derivatives proved to be a powerful technique in studying the (micro-)heterogeneity of sugar chains in glycoproteins.

Study Snapshot

Dansyl glyco-asparagines derived from hen egg white glycoproteins are suitable for 1H-NMR spectroscopic analysis, revealing the micro-heterogeneity of sugar chains in glycoproteins.

PopulationOlder adults (50-71 years)

Sample size24

MethodsObservational

OutcomesBody Mass Index projections

ResultsSocial networks mitigate obesity in older groups.

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Paper

1H-NMR spectroscopic characterization of dansyl glyco-asparagines derived from hen egg white clycoproteins

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References

Determination of the structure of ovalbumin glycopeptide AC-B by 1H nuclear magnetic resonance spectroscopy at 500 MHz.

The study confirms the structure of two unique ovalbumin glycopeptides and identifies a Man 8 GlcNAc 2 Asn glycopeptide as a processing intermediate in ovalbumin.

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This study successfully separated intact ovalbumin glycopeptides AC-C into four distinct glycopeptides using high-pressure liquid chromatography, confirming their structures and establishing a previously unreported one.

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This study identifies a novel glycoasparagine structure in ovalbumin glycopeptide fraction (GP-IV) using anion-exchange borate chromatography, demonstrating its potential for separating and preparing oligosaccharides with similar molecular size but different vicinal c

Purification and characterization of a beta-N-acetylglucosaminidase from Octopus vulgaris. Determination of specificity by using 360-MHz 1H-NMR spectroscopy.

Beta I, a beta-N-acetylglucosaminidase from Octopus vulgaris, exhibits both linkage and site specificity, hydrolyzing beta 1,4 linkage of N-acetylglucosamine at specific sites on glycopeptides isolated from ovalbumin.

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The sugar chains in hen ovomucoid are mainly formed by an alternate biosynthetic pathway, not the ordinary processing pathway of asparagine-linked sugar chains.

Citations

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