Structure of the mannose-rich oligosaccharide chains of concanavalin A-binding glycopeptides derived from beef brain glycoproteins.

Abstract:

:A neutral, mannose-rich, concanavalin A (Con A)-binding glycopeptide fraction was obtained by proteolytic digestion of defatted beef brain tissue. Hydrazinolysis followed by gel filtration of the reaction products provided three oligosaccharides. A portion of each oligosaccharide was treated by exhaustive digestion with alpha-mannosidase. Another portion was subjected to selective acetolysis of Man alpha 1 leads to 6Man linkages, providing two fragments that were recovered by gel filtration. The structure of the intact oligosaccharides, as well as the fragments obtained by selective acetolysis and enzymatic treatment, were resolved by gas-liquid chromatographic-mass spectrometric analysis. The structures of the three oligosaccharides were: (a) Man alpha 1 leads to 2Man alpha 1 leads to 6(Man alpha 1 leads to 3)Man alpha 1 leads to 6(Man alpha 1 leads to 2Man alpha 1 leads to 2Man alpha 1 leads to 3)Man beta 1 leads to 4-N-acetylglucosamine (GlcNAc)beta 1 leads to 4N-acetylglucosaminitol (GlcOLNAc); (b) Man alpha 1 leads to 2Man alpha 1 leads to 6(Man alpha 1 leads to 3)Man alpha 1 leads to 6(Man alpha 1 leads to 2Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcOLNAc; and (c) Man alpha 1 leads to 6(Man alpha 1 leads to 3) Man alpha 1 leads to 6(Man alpha 1 leads to 3)Man beta 1 leads to 4GlcNAc-beta 1 leads to 4GlcOLNAc. These structures account for 15-20% of the glycoprotein-carbohydrate of whole beef brain and most of the oligosaccharides that demonstrate a high affinity for Con A. In view of the large number of Con A-binding glycoproteins in brain tissue, it appears that many of these different glycoproteins must contain structurally identical oligosaccharides.

journal_name

J Neurochem

authors

Somawardhana CW,Brunngraber EG

doi

10.1111/j.1471-4159.1983.tb04746.x

subject

Has Abstract

pub_date

1983-08-01 00:00:00

pages

321-30

issue

2

eissn

0022-3042

issn

1471-4159

journal_volume

41

pub_type

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