Isolation and Biochemical Characterization of Apios tuber lectin

Eri Kenmochi, Syed Rashel Kabir, Tomohisa Ogawa, Ryno Naude, Hiroaki Tateno, Jun Hirabayashi, Koji Muramoto

    Research output: Contribution to journalArticlepeer-review

    21 Citations (Scopus)


    Apios tuber lectin, named ATL, was isolated from Apios americana Medikus by two chromatography steps, hydrophobic chromatography and anion-exchange chromatography. The minimum concentration required for the hemagglutination activity toward rabbit erythrocytes of ATL was 4 μg/mL. ATL was composed of a homodimer of 28.4 kDa subunits. The amino acid sequence of ATL was similar to those of other legume lectins. The lectin showed moderate stability toward heating and acidic pH, and the binding affinity against several monosaccharides, such as D-glucosamine and D-galactosamine. ATL also bound to desialylated or agalactosylated glycoproteins such as asialo and agalacto transferrin. ATL decreased the transepithelial electrical resistance across human intestinal Caco-2 cell monolayers, suggesting the effect on the tight junction-mediated paracellular transport.

    Original languageEnglish
    Pages (from-to)987-1002
    Number of pages16
    Issue number1
    Publication statusPublished - 2015 Jan 1


    • American groundnut
    • Apios americana
    • Lectin
    • Legume lectin

    ASJC Scopus subject areas

    • Analytical Chemistry
    • Chemistry (miscellaneous)
    • Molecular Medicine
    • Pharmaceutical Science
    • Drug Discovery
    • Physical and Theoretical Chemistry
    • Organic Chemistry


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