Carbohydrate Specificity of Lectins from Boletopsis leucomelas and Aralia cordate

Yu KOYAMA; Takuji SUZUKI; Shoji ODANI; Sachiko NAKAMURA; Junko KOMINAMI; Jun HIRABAYASHI; Mamoru ISEMURA

doi:10.1271/bbb.70.542

Biochemistry & Molecular Biology Notes

Carbohydrate Specificity of Lectins from Boletopsis leucomelas and Aralia cordate

Yu KOYAMA, Takuji SUZUKI, Shoji ODANI, Sachiko NAKAMURA, Junko KOMINAMI, Jun HIRABAYASHI, Mamoru ISEMURA

Author information

Yu KOYAMA
Laboratory of Cellular Biochemistry, Graduate School of Nutritional and Environmental Sciences, University of Shizuoka
Takuji SUZUKI
Laboratory of Cellular Biochemistry, Graduate School of Nutritional and Environmental Sciences, University of Shizuoka
Shoji ODANI
Department of Biology, Niigata University School of Science
Sachiko NAKAMURA
Glycostructure Analysis Team, Research Center for Glycoscience, National Institute of Advanced Industrial Science and Technology
Junko KOMINAMI
Glycostructure Analysis Team, Research Center for Glycoscience, National Institute of Advanced Industrial Science and Technology
Fine Chemical & Foods Laboratories, J-Oil Mills, Inc.
Jun HIRABAYASHI
Glycostructure Analysis Team, Research Center for Glycoscience, National Institute of Advanced Industrial Science and Technology
Mamoru ISEMURA
Laboratory of Cellular Biochemistry, Graduate School of Nutritional and Environmental Sciences, University of Shizuoka

Keywords: lectin, Aralia cordate, Boletopsis leucomelas, Wasabia japonica, frontal affinity chromatography

JOURNAL FREE ACCESS

2006 Volume 70 Issue 2 Pages 542-545

DOI https://doi.org/10.1271/bbb.70.542

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Abstract

The carbohydrate specificity of three novel lectins, Boletopsis leucomelas lectin (BLL), Aralia cordate lectin (ACL), and Wasabia japonica lectin (WJL), was examined by frontal affinity chromatography using a panel of fluorescently labeled 47 oligosaccharides. The results indicate that BLL recognizes an agalacto structure of the biantennary chain and its bisecting structure. ACL showed strong affinity for triantennary oligosaccharides, but no affinity for tetraantennary structure. WJL showed no appreciable affinity for any of the 47 glycans examined. These lectins with a unique affinity specificity might be useful for examining alterations in the glycan structures of the glycoconjugates in association with development and various diseases.

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