Structural Analysis ofN-Linked Carbohydrate Chains of Funnel Web Spider (Agelenopsis aperta) Venom Peptide Isomerase | Zendy

Yasushi Shikata | Zendy; Hiroshi Ohe | Zendy; Nariyasu Mano | Zendy; Manabu Kuwada | Zendy; Naoki Asakawa | Zendy

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Structural Analysis ofN-Linked Carbohydrate Chains of Funnel Web Spider (Agelenopsis aperta) Venom Peptide Isomerase

Author(s) -

Yasushi Shikata,

Hiroshi Ohe,

Nariyasu Mano,

Manabu Kuwada,

Naoki Asakawa

Publication year - 1998

Publication title -

bioscience biotechnology and biochemistry

Language(s) - Uncategorized

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.62.1211

Subject(s) - exoglycosidase , peptide , chemistry , biochemistry , carbohydrate , fast atom bombardment , fucose , chromatography , venom , mass spectrometry , glycoprotein , glycan

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 alpha 1-6 linked to the reducing N-acetylglucosamine in approximately 80% of them.

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