ISOLATION AND CHARACTERIZATION OF NEW GALNAC GAL-SPECIFIC LECTIN FROMTHE 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 l ectin obtained was determined by SDS-PAGE to be 18,000, independent of the presence or absence of beta-mercaptoethanol. CGL was found to agg lutinate all types of the human erythrocytes together with mouse and r abbit. 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 nonredu cing terminal D-galactose, melibiose, and raffinose were found to be s trong inhibitors. On the other hand, among the glycoproteins, asialo-B SM was the best inhibitor. The hemagglutinating activity of CGL was in dependent of the divalent cations Ca2+ and Mg2+. Significant CGL activ ity was observed between pH 8-10. (C) 1998 Elsevier Science Inc.