Structure of the major oligosaccharide of cobra venom factor

D. Channe Gowda, Michael Schultz, Reinhard Bredehorst, Carl Wilhelm Vogel

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28 Scopus citations


Cobra venom factor (CVF), the complement-activating glycoprotein in cobra venom, contains three or possibly four N-linked oligosaccharide chains per molecule and is devoid of O-linked saccharides. Analysis by lectin-affinity staining revealed the presence of complex-type oligosaccharides containing non-reducing terminal α-galactosyl residues and fucose residues linked to the proximal N-acetylglucosamine. Sialic acid residues could not be detected. For their structural analysis, the oligosaccharides were released by hydrazinolysis and fractionated on Bio-Gel P-4. Approximately 80% of the eluted oligosaccharides have a size equivalent of 17 ± 2 glucose units. The major oligosaccharide representing about 45% of the total carbohydrate present in CVF was purified to homogeneity by MicroPak AX-5 HPLC and its structure was analyzed by sequential exoglycosidase digestion. The positions of the glycosidic linkages of the sugar residues were established by methylation analysis of CVF-derived glycopeptides. The data of these analyses indicated that the major oligosaccharide has a symmetrical fucosylated biantennary complex-type structure terminating with unusual α-galactosyl residues.

Original languageEnglish (US)
Pages (from-to)335-342
Number of pages8
JournalMolecular Immunology
Issue number3
StatePublished - Mar 1992

All Science Journal Classification (ASJC) codes

  • Immunology
  • Molecular Biology


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