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

Authors

  • Koji Muramoto,

    Corresponding author
    1. Department of Biological Resource Sciences, Graduate School of Agricultural Science, Tohoku University, Sendai, Miyagi 981-8555 and
      *Corresponding author: Tel/Fax: 81-22-717-8807. Email: muramoto@biochem.tohoku.ac.jp
    Search for more papers by this author
  • Dong-Hao Jin,

    1. Department of Biological Resource Sciences, Graduate School of Agricultural Science, Tohoku University, Sendai, Miyagi 981-8555 and
    Search for more papers by this author
  • Yoko Niino,

    1. Department of Biological Resource Sciences, Graduate School of Agricultural Science, Tohoku University, Sendai, Miyagi 981-8555 and
    Search for more papers by this author
  • Kazue Fujiwara,

    1. Department of Biological Resource Sciences, Graduate School of Agricultural Science, Tohoku University, Sendai, Miyagi 981-8555 and
    Search for more papers by this author
  • Shizuya Kabuto,

    1. Department of Biological Resource Sciences, Graduate School of Agricultural Science, Tohoku University, Sendai, Miyagi 981-8555 and
    Search for more papers by this author
  • Tomohisa Ogawa,

    1. Department of Biological Resource Sciences, Graduate School of Agricultural Science, Tohoku University, Sendai, Miyagi 981-8555 and
    Search for more papers by this author
  • Michitoshi Toda,

    1. Department of Marine Biochemistry, School of Fisheries Sciences, Kitasato University, Sanriku, Iwate 022-0101, Japan
    Search for more papers by this author
  • Hisao Kamiya

    1. Department of Marine Biochemistry, School of Fisheries Sciences, Kitasato University, Sanriku, Iwate 022-0101, Japan
    Search for more papers by this author

*Corresponding author: Tel/Fax: 81-22-717-8807. Email: muramoto@biochem.tohoku.ac.jp

Abstract

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.

Ancillary