Further studies of oligosaccharide recognition by the soluble 13 kDa lectin of bovine heart muscle. Ability to accommodate the blood-group-H and -B-related sequences

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Abstract
Oligosaccharide recognition by the 13 kDa soluble lectin from bovine heart muscle has been investigated by inhibition of binding of the 125I-labelled lectin to trypsin-treated rabbit erythrocytes. The results indicate that the Type 1 (Gal.beta.1-3GlcNAc) and the Type 2 (Gal.beta.1-4GlcNAc) backtone structures are the basic recognition units, and that the blood-group-H structure, the blood-group-B structure, the ''B-like'' structure [afucosyl-(blood group B)] and the .alpha.2-3 sialylated analogues of the backbone structures can also be accommodated and hence are candidate receptor structures for the lectin. A comparison of available inhibition data on six other soluble .beta.-galactoside-binding lectins (three from human lung and three from rat lung) has shown some common features among these and the bovine lectin, e.g. in general a stronger reaction with N-acetyl-lactosamine than with lactose, and a lack of reaction with 3-fucosyl-lactose and 6-sialyl-lactose. However, there are distinctive features among the lectins, e.g. differences in relative reactions with the blood-group-A structure, and no two of the lectins appear to be identical in their fine specificities.