Sialoglycoconjugate-specific lectin from Maackia fauriei

A lectin has been purified from the bark of the legume Maackia fauriei. This lectin, MFA, was found to agglutinate human ABO erythrocytes at a titer of 256. The results from electrophoretic analyses, gel-filtration chromatography, and enzyme linked lectinsorbent assay indicate that MFA is an acidic glycoprotein, and exists as a tetramer of 30 kDa subunits that are linked by noncovalent bonds. The activity of MFA is critically dependent upon CaC1$_2$. MFA demonstrated high homogeneity with the lectins from M. amurensis, which is the only legume source of lectins that bind to sialoglycoconjugate, in its N-terminal amino acid sequence and amino acid composition, (omitted)