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  • Title: Isolation and characterization of new GalNAc/Gal-specific lectin from the sea mussel Crenomytilus grayanus.
    Author: Belogortseva NI, Molchanova VI, Kurika AV, Skobun AS, Glazkova VE.
    Journal: Comp Biochem Physiol C Pharmacol Toxicol Endocrinol; 1998 Jan; 119(1):45-50. PubMed ID: 9568372.
    Abstract:
    A lectin, Crenomytilus grayanus (CGL), was purified from sea mussel C. grayanus by affinity chromatography on acid-treated Sepharose 6B and following gel filtration on Sephacryl S-200. Molecular weight of the lectin obtained was determined by SDS-PAGE to be 18,000, independent of the presence or absence of beta-mercaptoethanol. CGL was found to agglutinate all types of the human erythrocytes together with mouse and rabbit. In hemagglutination inhibition assays, N-acetyl-D-galactosamine, D-galactose, and D-talose were the most potent inhibitors among the monosaccharides tested. Out of the oligosaccharides containing nonreducing terminal D-galactose, melibiose, and raffinose were found to be strong inhibitors. On the other hand, among the glycoproteins, asialo-BSM was the best inhibitor. The hemagglutinating activity of CGL was independent of the divalent cations Ca2+ and Mg2+. Significant CGL activity was observed between pH 8-10.
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