1. Isolation and Characterization of New GalNAc/Gal-Specific Lectin from the Sea Mussel Crenomytilus Grayanus
- Author
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Vera E Glazkova, V. I. Molchanova, Andrey S Skobun, Alexander V Kurika, and Nataliya I. Belogortseva
- Subjects
Cations, Divalent ,Immunology ,Carbohydrates ,Chromatography, Affinity ,Divalent ,Sepharose ,Mice ,chemistry.chemical_compound ,Affinity chromatography ,Lectins ,Animals ,Humans ,Monosaccharide ,Amino Acids ,Raffinose ,Melibiose ,Pharmacology ,chemistry.chemical_classification ,biology ,Hemagglutination ,Temperature ,Lectin ,Hydrogen-Ion Concentration ,Chromatography, Ion Exchange ,Molecular biology ,Bivalvia ,Molecular Weight ,chemistry ,Biochemistry ,Chromatography, Gel ,biology.protein ,Electrophoresis, Polyacrylamide Gel ,Rabbits ,Glycoprotein - 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. more...
- Published
- 1998
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