Structural characterization of a rhamnose-binding glycoprotein (lectin) from Spanish mackerel (Scomberomorous niphonius) eggs

Takatomo Terada, Yasuharu Watanabe, Hiroaki Tateno, Takako Naganuma, Tomohisa Ogawa, Koji Muramoto, Hisao Kamiya

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    58 Citations (Scopus)


    A rhamnose-binding glycoprotein (lectin), named SML, was isolated from the eggs of Spanish mackerel (Scomberomorous niphonius) by affinity and ion-exchange chromatographies. SML was composed of a non-covalently linked homodimer. The SML subunit was composed of 201 amino acid residues with two tandemly repeated domains, and contained 8 half-Cys residues in each domain, which is highly homologous to the N-terminal lectin domain of calcium-independent α-latrotoxin receptor in mammalian brains. Each domain has the same disulfide bonding pattern; Cys10-Cys40, Cys20-Cys99, Cys54-Cys86 and Cys67-Cys73 were located in the N-terminal domain, and Cys108-Cys138, Cys117-Cys195, Cys152-Cys182 and Cys163-Cys169 were in the C-terminal domain. SML was N-glycosylated at Asn168 in the C-terminal domain. The structure of the sugar chain was determined to be NeuAc-Galβ1-4GlcNAcβ1-2Manα1-6-(NeuAc-Galβ1-4GlcNAcβ1-2Manα1-3)Manβ1-4GlcNAcβ1-4GlcNAc-Asn.

    Original languageEnglish
    Pages (from-to)617-629
    Number of pages13
    JournalBiochimica et Biophysica Acta - General Subjects
    Issue number4
    Publication statusPublished - 2007 Apr


    • Animal lectin
    • Disulfide bonds
    • Glycoprotein
    • N-linked sugar chains
    • Rhamnose-binding lectin
    • Spanish mackerel

    ASJC Scopus subject areas

    • Biophysics
    • Biochemistry
    • Molecular Biology


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