A sialic acid-binding lectin from the legume Maackia fauriei:: comparison with lectins from M-amurensis

A lectin that exhibits hemagglutination activity and cytotoxicity against human cancer cell lines has been purified from the legume Maackia fauriei. This lectin, designated M.fauriei agglutinin (MFA), is a tetramer of 115.6 kDa consisting of 30 kDa subunits with a pl of 4.9. The hemagglutination activity of MFA was inhibited by N-acetylneuraminic acid, Neu5Acalpha2-3Galbeta1-4GlcNAc, and sialoglycoproteins. MFA was stable at pH values from 4.0 to 8.5, and at temperatures below 50degreesC, and its activity was affected by demetalization with EDTA. MFA has a high homology with lectins from M. amurensis-which is the only legume source of lectins that bind to specific carbohydrate chains containing sialic acid-in its N-terminal 20 amino acid sequence. (C) 2004 Elsevier Ireland Ltd. All rights reserved.