Glycoconjugate Journal

, Volume 10, Issue 3, pp 240–246 | Cite as

Glycosylation of the thrombin-like serine protease ancrod fromAgkistrodon rhodostoma venom. Oligosaccharide substitution pattern at eachN-glycosylation site

  • Günter Pfeiffer
  • Dietmar Linder
  • Karlhermann Strube
  • Rudolf Geyer


In a previous study, we determined the structures of the glycans present in ancrod, a thrombin-like serine protease from the venom of the Malayan pit viperAgkistrodon rhodostoma (Pfeifferet al. (1992)Eur J Biochem205:961–78). In order to allocate the various carbohydrate chains to distinctN-glycosylation sites of the molecule, we have now isolated individual glycopeptides. Peptide moieties were identified after deglycosylation with peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase F by amino acid analysis and sequencing. Liberated oligosaccharides were assigned to the previously deduced carbohydrate structures by high performance liquid chromatography. Although only quantitative differences were observed, the results indicate that each glycosylation site of ancrod carries its characteristic oligosaccharide pattern. Furthermore, all potential sites were shown to be substituted by carbohydrates.


glycoprotein glycopeptides N-linked oligosaccharides snake venom 



high pH anion exchange HPLC


reversed phase HPLC


peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase F


pulsed amperometric detection.


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Copyright information

© Chapman & Hall 1993

Authors and Affiliations

  • Günter Pfeiffer
    • 1
  • Dietmar Linder
    • 1
  • Karlhermann Strube
    • 2
  • Rudolf Geyer
    • 1
  1. 1.Biochemisches Institut am Klinikum der UniversitätGiessenGermany
  2. 2.BASF AG, HauptlaborLudwigshafenGermany

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