Lectins from seeds of Crotalaria pallida (smooth rattlebox)

Abstract A lectin from the seeds of Crotalaria pallida (CPL), with an apparent molecular mass of 30 kDa, determined by SDS–polyacrylamide gel electrophoresis, showed human type A and B erythrocytes agglutination activity, which is inhibited by raffinose and galactose. The lectin requirement for divalent cation was demonstrated with EDTA/EGTA blocking hemagglutination activity. Although the N-terminal amino acid sequence of CPL is identical to another lectin from Crotalaria striata , which is taxonomically synonymous to Crotalaria pallida , these lectins differ in amino acid composition and hemagglutination properties.