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Bioscience, Biotechnology, and Biochemistry Volume 76, 2012 - Issue 2
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Original Articles

Characterization of a New α-Galactosyl-Binding Lectin from the Mushroom Clavaria purpurea

Beatrice LYIMODepartment of Applied Biological Chemistry, United Graduate School of Agricultural Sciences, Kagoshima University
,
Natsumi FUNAKUMADepartment of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University
,
Yuji MINAMIDepartment of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University
&
Fumio YAGIDepartment of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University
Pages 336-342 | Received 29 Sep 2011, Accepted 14 Nov 2011, Published online: 22 May 2014
 
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Abstract

A galactose specific lectin (CpL) was purified from the Clavaria purpurea mushroom by affinity chromatography. CpL agglutinated only trypsin-treated rabbit erythrocytes. On enzyme linked lectin sorbent assay (ELLSA), the lectin bound with thyroglobulin and asialo bovine submaxillary mucin (BSM). The fine sugar binding specificity of CpL was elucidated using inhibition of hemagglutination and sugar immobilized gold nano-particles (SGNP). The results indicated a preference of CpL towards α-galactosyl sugar chains. Among several monosaccharides and disaccharides assayed for dissociation effect on the SGNP-CpL complex, Galα1-3Gal and raffinose were the best inhibitors. The partial amino acid sequence showed two QXW motifs in CpL and similarity towards members of the ricin B superfamily.

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