Purification and structural characterization of lectins from the cnidarian Bunodeopsis antilliensis [corrected].

Purification and characterization of two different lectins from the Mexican anemone Bunodeopsis antilliensis are reported. These two lectins named Bunodeopsis antilliensis agglutinin-A (BAA-A) and -B (BAA-B) presented the following characteristics: BAA-A was resolved as a component, with haemagglutinating activity for human blood type A (N-acetylgalactosamine-galactose-fucose), with a molecular weight of 28,900 obtained by means of mass spectrometry, showed an isoelectric point of 5.04 with a higher carbohydrate specificity for N-acetylgalactosamine (GalNAc). The analysis of the N-terminal revealed it is related to phosphoesterase and GTP binding protein. BAA-B mainly active with human blood type B (galactose-galactose-fucose) was resolved into three fractions (BAA-B1-3). Their molecular weight were: BAA-B(1) 39,350, BAA-B(2) 28,300 and BAA-B(3) 17,550. The estimated isoelectric points were 8.05, 4.66 and 6.60, respectively. Only fraction 3 exhibited haemagglutinating activity with a higher carbohydrate specificity for galactose and mannose. The analysis of the N-terminal pointed out it is related with phospholipase A(2). We suggest these lectins could be related to a feeding strategy[corrected].