The amino-acid sequence of a lectin of the acorn barnacle Megabalanus rosa

Koji Muramoto, Hisao Kamiya

    Research output: Contribution to journalArticlepeer-review

    59 Citations (Scopus)


    The complete amino-acid sequence of a lectin isolated from the coelomic fluid of the acorn barnacle Megabalanus rosa has been determined. The lectin (Mr 64 000) is composed of four identical subunits of 138 amino acids. The amino-acid sequence and the location of two interchain and three intrachain disulfide bridges of the subunit were determined by the manual sequencing of peptides derived from the protein by digestion with trypsin, chymotrypsin and Staphylococcus aureus V8 proteinase, as well as fragments produced by cleavage with cyanogen bromide. The Cys-Pro-Pro-Cys sequence at the interchain disulfide bridges was the same as that of the hinge region of human immunoglobulin IgG1. The amino acid sequence of M. rosa lectin includes some regions homologous to those in Sarcophaga (flesh fly) lectin.

    Original languageEnglish
    Pages (from-to)285-295
    Number of pages11
    JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
    Issue number3
    Publication statusPublished - 1986 Dec 12


    • (Acorn barnacle)
    • Agglutinin
    • Amino-acid sequence
    • Invertebrate lectin
    • Lectin
    • Primary structure

    ASJC Scopus subject areas

    • Biophysics
    • Structural Biology
    • Biochemistry
    • Molecular Biology


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