Structural analysis of n-linked carbohydrate chains of funnel web spider (agelenopsis aperta) venom peptide isomerase

Yasushi Shikata, Hiroshi Ohe, Nariyasu Mano, Manabu Kuwada, Naoki Asakawa

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)


The structure of the N-linked carbohydrate chains of peptide isomerase from the venom of the funnel web spider (Agelenopsis aperta) has been analyzed. Carbohydrates were released from peptide isomerase by hydrazinolysis and reductively aminated with 2-aminopyridine. The fluorescent derivatives were purified by phenol/chloroform extraction, followed by size-exclusion HPLC. The structure of the purified pyridylamino (PA-) carbohydrate chains were analyzed by a combination of two-dimensional HPLC mapping, sugar composition analysis, sequential exoglycosidase digestions, and mass spectrometry. The peptide isomerase contains six kinds of N-linked carbohydrate chains of truncated high-mannose type, with a fucose α1-6 linked to the reducing N-acetylglucosamine in approximately 80% of them.

Original languageEnglish
Pages (from-to)1211-1215
Number of pages5
JournalBioscience, Biotechnology and Biochemistry
Issue number6
Publication statusPublished - 1998 Jan 1
Externally publishedYes


  • N-glycan
  • Peptide isomerase
  • Trimannosyl core structure
  • Two-dimensional HPLC mapping
  • α1,6-fucosylation

ASJC Scopus subject areas

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry


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