Purification, Characterization, and cDNA Cloning of a Lectin from the Mushroom Pleurocybella porrigens
スポンサーリンク
概要
- 論文の詳細を見る
A lectin, PPL, was purified from the mushroom Pleurocybella porrigens. The results of SDS–PAGE, gel filtration, and MALDI-TOF-mass of PPL indicated that its molecular mass was 56 kDa, and it was composed of four 14 kDa subunits with no disulfide bonds. In hemagglutination inhibition assay, PPL exhibited the strongest binding specificity toward GalNAc among the mono- and oligo-saccharides tested. Among the glycoproteins, asialo-bovine submaxillary mucin (asialo-BSM) showed the strongest inhibitory effect. In surface plasmon resonance analysis, asialo-BSM, porcine stomach mucin (PSM), and BSM exhibited potent binding affinity. The complete amino acid sequence was determined by amino acid sequencing of intact and of enzyme-digested PPL. The cDNA of PPL was cloned from RNA extracted from the mushroom. The open reading frame of the cDNA of the protein consisted of 411 bp, encoding 137 amino acids. This is the first report of isolation of a lectin of the genus Pleurocybella.
論文 | ランダム
- B-3-29 衛星回線へのTCP/IP適用時の伝送誤りに伴うスループットの低下要因について
- SST2000-11 / SAT2000-21 TCP/IPの衛星通信回線への適用について
- SST2000-11 / SAT2000-21 TCP/IPの衛星通信回線への適用について
- 衛星通信回線におけるTCPの性能評価に関する実験的検討
- 衛星通信回線におけるTCPの性能評価に関する実験的検討