Comparison of the amino acid sequences of acorn barnacle lectins showing different inhibitory activities toward the crystal growth of calcium carbonate

Koji Muramoto, Dong Hao Jin, Yoko Niino, Kazue Fujiwara, Shizuya Kabuto, Tomohisa Ogawa, Michitoshi Todaand, Hisao Kamiya

    Research output: Contribution to journalArticlepeer-review

    6 Citations (Scopus)

    Abstract

    The amino acid sequence of a D-galactose-binding lectin isolated from the hemolymph of the acorn barnacle Balanus rostratus was determined. The lectin (BRL) (Mr 120K) is a multimeric protein whose subunit consists of 182 amino acids. The amino acid sequence was compared with those of multiple lectins (BRA-2, BRA-3) from Megabalanus rosa to explore the relationship between the structures and the inhibitory activity toward the crystal growth of calcium carbonate. Although BRL was 46% identical to BRA-2 and 15% identical to BRA-3, the lectin had no inhibitory activity, unlike BRA-2 and BRA-3. Both the number and the localization of acidic amino acid residues and their amide forms were different among them. Observations by scanning electron microscopy revealed modifications in the size and morphology of the calcium carbonate crystals grown in the presence of the lectins.

    Original languageEnglish
    Pages (from-to)703-709
    Number of pages7
    JournalFisheries Science
    Volume67
    Issue number4
    DOIs
    Publication statusPublished - 2001 Sep 21

    Keywords

    • Acorn barnacle
    • Agglutinin
    • Amino acid sequence
    • Balanus rostratus
    • Hemagglutinin
    • Hemolymph
    • Lectin

    ASJC Scopus subject areas

    • Aquatic Science

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