Isolation and Characterization of New GalNAc/Gal-Specific Lectin from the Sea Mussel Crenomytilus Grayanus

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 abs...

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Bibliographic Details
Published in:	Comparative biochemistry and physiology. C, Comparative pharmacology and toxicology Vol. 119; no. 1; pp. 45 - 50
Main Authors:	Belogortseva, Nataliya I, Molchanova, Valentina I, Kurika, Alexander V, Skobun, Andrey S, Glazkova, Vera E
Format:	Journal Article
Language:	English
Published:	United States Elsevier Inc 1998
Subjects:	Amino Acids - analysis Animals Bivalvia - chemistry Carbohydrate-binding protein Carbohydrates - analysis Cations, Divalent Chromatography, Affinity Chromatography, Gel Chromatography, Ion Exchange Crenomytilus grayanus Electrophoresis, Polyacrylamide Gel GalNAc/Gal-specific lectin Hemagglutination - drug effects Humans Hydrogen-Ion Concentration invertebrate Lectins - chemistry Lectins - isolation & purification Lectins - pharmacology Marine Mice Molecular Weight Rabbits Temperature TBS, tris-buffered saline EDTA, ethylenediamine tetraacetate GalNAc/Gal-specific lectin BSA, bovine serum albumin SDS-PAGE, sodium dodecyl sulfate-polyacrylamide gel electrophoresis PBS, phosphate-buffered saline Crenomytilus grayanus invertebrate Carbohydrate-binding protein BSM, bovine submaxillary mucin CGL, Crenomytilus grayanus lectin
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Summary:	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 β-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 Ca 2+ and Mg 2+. Significant CGL activity was observed between pH 8–10.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0742-8413 1367-8280
DOI:	10.1016/S0742-8413(97)00180-1