Specificity of the binding site of the sialic acid-binding lectin from ovine placenta, deduced from interactions with synthetic analogues.

摘要: The specificity of the sialic acid-binding lectin from ovine placenta was examined in detail by haemagglutination inhibition assays applying a panel 32 synthetic acid analogues. carboxylic group is prerequisite for interaction with lectin, α-anomer methyl glycoside only little more effective as an inhibitor than β-anomer and most potent 9-deoxy-10-carboxylic Neu5Ac, followed 4-oxo-Neu5Ac. In contrast to majority known lectins, N-acetyl Neu5Ac not indispensable binding, neither hydroxyl at C-9 since substitutions this carbon atom are well tolerated. Furthermore, all sulfur-containing substituents enhanced affinity lectin. This first found strongly bind thio derivatives.