Carbohydrate Specificity of Lectins from Boletopsis leucomelas and Aralia cordate

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

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  • Carbohydrate Specificity of Lectins from<i>Boletopsis leucomelas</i>and<i>Aralia cordate</i>

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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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