The positions of the disulfide bonds and the glycosylation site in a lectin of the acorn barnacle Megabalanus rosa

Koji Muramoto, Hisao Kamiya

    Research output: Contribution to journalArticle

    20 Citations (Scopus)

    Abstract

    The positions of the interchain and intrachain disulfide bonds and the glycosylation site in a lectin of the acorn barnacle Megabalanus rosa were determined. The lectin (Mr 140000) is composed of the same subunit (Mr 22000) which is cross-linked by disulfide bonds to form a dimer. Intact lectin yielded two fragments, CB1 and CB2, by cleavage with cyanogen bromide. One intrachain and two interchain disulfide bonds were identified as Cys-53-Cys-61, Cys-14-Cys-50′ and Cys-50-Cys-14′, respectively, by enzymatic digestion and Edman degradation of CB1. Two interchain disulfide bonds were determined as Cys-78-Cys-168 and Cys-144-Cys-160 by enzymatic digestion of CB2. The two interchain disulfide bonds are well conserved through all invertebrate lectins and calcium-dependent animal lectins. S-Carboxaminodomethylated lectin was digested with Staphylococcus aureus V8 proteinase and separated by reversed-phase HPLC. Glycopeptides were detected by the 4-N,N-dimethylamino-4′-azobenzene sulfonyl hyrazide method. Sequence analyses of the glycopeptides showed that a carbohydrate chain attached to Asn-39.

    Original languageEnglish
    Pages (from-to)52-60
    Number of pages9
    JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
    Volume1039
    Issue number1
    DOIs
    Publication statusPublished - 1990 May 31

    Keywords

    • (Acorn barnacle)
    • Agglutinin
    • Disulfide bond
    • Glycoprotein
    • Invertebrate lectin
    • Lectin

    ASJC Scopus subject areas

    • Biophysics
    • Structural Biology
    • Biochemistry
    • Molecular Biology

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