Abstract
A new galectin was characterized in the Amethyst deceiver mushroom Laccaria amethystina. The complete amino acid (AA) sequence of the lectin, which exhibited β-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 β-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.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
