Purification, Characterization, and cDNA Cloning of a Lectin from the Mushroom Pleurocybella porrigens

被引：32
|
作者：
Suzuki, Tomohiro [1 ]
Amano, Yuko [2 ]
Fujita, Motohiro [2 ]
Kobayashi, Yuka [2 ]
Dohra, Hideo [3 ]
Hirai, Hirofumi [2 ]
Murata, Takeomi [2 ]
Usui, Taichi [2 ]
Morita, Tatsuya [2 ]
Kawagishi, Hirokazu [1 ,2 ]
机构：
[1] Shizuoka Univ, Grad Sch Sci & Technol, Dept Biosci, Suruga Ku, Shizuoka 4228529, Japan
[2] Shizuoka Univ, Fac Agr, Dept Appl Biol Chem, Suruga Ku, Shizuoka 4228529, Japan
[3] Shizuoka Univ, Inst Genet Res & Biotechnol, Suruga Ku, Shizuoka 4228529, Japan
来源：
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 2009年 / 73卷 / 03期
关键词：
mushroom; Pleurocybella porrigens; lectin; purification; cloning; HIGH-AFFINITY LECTIN; RICIN B-CHAIN; FRUITING BODIES; POLYPORUS-SQUAMOSUS; N-ACETYLLACTOSAMINE; CHROMATOGRAPHY; EXPRESSION;
D O I：
10.1271/bbb.80774
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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.
引用
收藏
页码：702 / 709
页数：8
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