Properties of a Lectin in Chum Salmon Ova

Hisao Kamiya, Koji Muramoto, Rina Goto, Masahiro Sakai, Hitoshi Ida

    Research output: Contribution to journalArticlepeer-review

    18 Citations (Scopus)


    A saline extract of chum salmon Oncorhynchus keta ova agglutinated rabbit erythrocytes but not human type B cells or sheep erythrocytes, and the hemagglutinating activity was independent of divalent cations. L-Rhamnose was the most effective inhibitor of a chum salmon ova lectin. Melibiose, L-arabinose, and D-galactose also inhibited the agglutination to some extent. The lectin was purified by affinity chromatography on L-rhamnose-Sepharose 6B and fast protein liquid chromatography on a Superose 12 column. The purified elctin showed a single band with a molecular weight of 22,000 in SDS-polyacrylamide gel electrophoresis with and without 2-mercaptoethanol. The agglutinin activity varied with the stages of development. The activity reduced markedly after the eyed stage and disappeared just before hatching. The purified lectin did agglutinate a fish pathogenic bacterium Vibrio anguillarum, but did not show the growth inhibition of bacterium.

    Original languageEnglish
    Pages (from-to)1139-1144
    Number of pages6
    Issue number7
    Publication statusPublished - 1990 Jan 1

    ASJC Scopus subject areas

    • Aquatic Science


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