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

  • MURAMOTO KOJI
    Department of Biological Resource Sciences, Graduate School of Agricultural Science, Tohoku University
  • JIN DONG-HAO
    Department of Biological Resource Sciences, Graduate School of Agricultural Science, Tohoku University
  • NIINO YOKO
    Department of Biological Resource Sciences, Graduate School of Agricultural Science, Tohoku University
  • FUJIWARA KAZUE
    Department of Biological Resource Sciences, Graduate School of Agricultural Science, Tohoku University
  • KABUTO SHIZUYA
    Department of Biological Resource Sciences, Graduate School of Agricultural Science, Tohoku University
  • OGAWA TOMOHISA
    Department of Biological Resource Sciences, Graduate School of Agricultural Science, Tohoku University
  • TODA MICHITOSHI
    Department of Marine Biochemistry, School of Fisheries Sciences, Kitasato University
  • KAMIYA HISAO
    Department of Marine Biochemistry, School of Fisheries Sciences, Kitasato University

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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.

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