The asparagine-linked carbohydrate of honeybee venom hyaluronidase |
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Authors: | Viktoria Kubelka Friedrich Altmann and Leopold M?rz |
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Institution: | (1) Institut für Chemie der Universität für Bodenkultur Wien, Gregor Mendelstrae 33, A-1180 Vienna, Austria |
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Abstract: | Hyaluronidase from the venom of the honeybee (Apis mellifera) has been purified by gelpermeation and cation exchange chromatography. Its asparagine-linked carbohydrate chains were released from tryptic glycopeptides with N-glycosidase A and reductively aminated with 2-aminopyridine. Separation of the fluorescent derivatives by size-fractionation and reversed-phase HPLC afforded eighteen fractions which were analysed by two-dimensional HPLC mapping combined with exoglycosidase digestions. The bulk of the N-linked glycans of hyaluronidase consisted of small oligosaccharides (Man1–3GlcNAc2), most of which were either 1,3-monofucosylated or 1,3-(1,6-)difucosylated at the innermost GlcNAc residue. High-mannose type structures constituted the minor fractions, together making up about 5% of the oligosaccharide pool from hyaluronidase. Four fractions, making up 8% of the N-linked glycans, contained the terminal trisaccharide GalNAc1-4Fuc1-3]GlcNAc1- in 1,2-linkage to the core 1,3-mannosyl residue. No evidence for the presence of O-glycans or sialic acids could be found.Abbreviations GalNAc
N-acetylgalactosamine
- GlcNAc
N-acetylglucosamine
- PA
pyridylamino
- PLA
phospholipase A2
- 2D-HPLC
two-dimensional HPLC |
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Keywords: | hyaluronidase Apis mellifera bee venom N-linked carbohydrate chains 1" target="_blank">gif" alt="agr" align="BASELINE" BORDER="0">1 3-fucosylation |
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