2011年1月
Primary Structure and Specificity of a New Member of Galectin Family from the Amethyst Deceiver Mushroom Laccaria amethystina
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
- ,
- ,
- 巻
- 75
- 号
- 1
- 開始ページ
- 62
- 終了ページ
- 69
- 記述言語
- 英語
- 掲載種別
- DOI
- 10.1271/bbb.100542
- 出版者・発行元
- TAYLOR & FRANCIS LTD
A new galectin was characterized in the Amethyst deceiver mushroom Laccaria amethystina. The complete amino acid (AA) sequence of the lectin, which exhibited beta-galactoside specificity, was deduced from its peptide sequences. The AA sequence of L. amethystina galectin (LAG) showed high homology with those of the same genus, at 75.6% identity to Laccaria bicolor, and 35.5-65.0% to galectins of Agrocybe spp. and Coprinopsis cinerea. The AA sequence of LAG contained all but one conserved residue known to be involved in beta-galactoside binding, with His at the position 57 residue replaced by Thr in LAG. Analysis of binding specificity by hemagglutination inhibition assay and enzyme-linked lectin-sorbent assay revealed high specificity of LAG towards O-glycoproteins.
- リンク情報
- ID情報
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- DOI : 10.1271/bbb.100542
- ISSN : 0916-8451
- eISSN : 1347-6947
- CiNii Articles ID : 10027896663
- Web of Science ID : WOS:000287384100010