The amino-acid sequence of multiple lectins of the acorn barnacle Megabalanus rosa and its homology with animal lectins

Koji Muramoto, Hisao Kamiya

    研究成果: Article査読

    62 被引用数 (Scopus)

    抄録

    The amino-acid sequence of a lectin isolated from the coelomic fluid of the acorn barnacle Megabalanus rosa has been determined. The lectin (Mr 140 000) is a multimeric protein whose subunit consists of 173 amino acids and one carbohydrate chain attached to Asn-39. The amino-acid sequence was determined by the manual sequencing of peptides derived from the protein by digestion with Staphylococcus aureus V8 proteinase, lysine endopeptidase and chymotrypsin, as well as fragments produced by cleavage with cyanogen bromide. The amino-acid sequence of the lectin was compared with the sequence of one (Mr 64 000) of the multiple lectins of M. rosa. They are distinct molecules in spite of a significant homology in their amino-acid sequences. The amino-acid sequence includes some regions homologous to those in other invertebrate lectins, such as sea urchin and flesh fly lectins, and vertebrate lectins. This is the first report to show the amino-acid sequence of multiple lectins isolated from an invertebrate.

    本文言語English
    ページ(範囲)42-51
    ページ数10
    ジャーナルBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
    1039
    1
    DOI
    出版ステータスPublished - 1990 5 31

    ASJC Scopus subject areas

    • 生物理学
    • 構造生物学
    • 生化学
    • 分子生物学

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