Purification and characterization of Microcystis aeruginosa (freshwater cyanobacterium) lectin

Masato Yamaguchi, Mituru Jimbo, Ryuichi Sakai, Koji Muramoto, Hisao Kamiya

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    Microcystis aeruginosa, strain M228, a laboratory culture of freshwater cyanobacterium, showed hemagglutinating activity against rabbit, horse and human ABO erthrocytes. Crossed absorption tests revealed the presence of a single type of lectin in the extract of M228 strain cells. The lectin, termed MAL, was purified in combination with the affinity chromatography on acid-treated agarose gel and the gel permeation chromatography in an electrophoretically pure form. MAL was a glycoprotein containing 7.8% neutral sugars and was composed of a single polypeptide having a molecular weight of 57 kDa. Isoelectric point was estimated to be pH 6.4. Hemagglutinating activity of the lectin was inhibited effectively by N-acetyl-d-galactosamine and by glycoproteins. d-galactose and lactose also showed moderate inhibitory activity. The destruction of the hemagglutinating activity by a 2-mercaptoethanol treatment suggests the presence of intra-chain disulfide bond(s) essential for the activity in the molecule. The sequence of the amino-terminal region of MAL was determined as Val-Lys-Ala-Ser-Lys-Val-Ser-Thr-Ser-Gln-Ala-Gly-Ser-Lys-Glu-Lys-Lys-Ala. Copyright (C) 1998 Elsevier Science Inc.

    Original languageEnglish
    Pages (from-to)593-597
    Number of pages5
    JournalComparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
    Issue number3
    Publication statusPublished - 1998 Jan 1


    • Agglutinin
    • Blue-green algae
    • Cyanobacteria
    • Hemagglutinin
    • Lectin
    • Microcystis aeruginosa

    ASJC Scopus subject areas

    • Biochemistry
    • Physiology
    • Molecular Biology


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