Alpha 1-6(alpha 1-3)-difucosylation of the asparagine-bound N-acetylglucosamine in honeybee venom phospholipase A2

Chymotryptic glycopeptides were prepared from a honeybee (Apis mellifica) venom phospholipase A2 (E.C. 3.1.1.4) fraction, with high affinity towards lentil (Lens culinaris) lectin. Treatment of the glycopeptide mixture with peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase A, followed by HPL...

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Bibliographic Details
Published in:Glycoconjugate journal 1992-04, Vol.9 (2), p.82-85
Main Authors: Staudacher, E, Altmann, F, März, L, Hård, K, Kamerling, J P, Vliegenthart, J F
Format: Article
Language:English
Subjects:
Acetylglucosamine - chemistry
Asparagine - chemistry
Bee Venoms - enzymology
Carbohydrate Sequence
Fucose - analysis
Fucose - chemistry
Magnetic Resonance Spectroscopy
Molecular Sequence Data
Oligosaccharides - analysis
Oligosaccharides - chemistry
Phospholipases A - chemistry
Phospholipases A2
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Summary:Chymotryptic glycopeptides were prepared from a honeybee (Apis mellifica) venom phospholipase A2 (E.C. 3.1.1.4) fraction, with high affinity towards lentil (Lens culinaris) lectin. Treatment of the glycopeptide mixture with peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase A, followed by HPLC fractionation, yielded two oligosaccharides, which were analysed by 500 MHz 1H-NMR spectroscopy to give the following structures [formula: see text] This is the first report on a naturally occurring glycoprotein N-glycan with two fucose residues linked to the asparagine-bound N-acetylglucosamine.
ISSN:0282-0080
DOI:10.1007/BF00731703