[The carbohydrate specificity of the extracellular lectins in bacteria of the genus Bacillus].

The paper presents the study of interaction of extracellular sialo-specific lectins of Bacillus genus bacteria with different types of erythrocytes and affinity of these biologically active substances to derivatives of N-acetylneuramine acid and natural sialo and asialo conjugates. It is established that lectins under study possess a very narrow carbohydrate specificity and distinguish strictly definite carbohydrate structures. The identification processes first of all require the availability of N-glycolylneuraminic acid in the structure of receptors, and to the less extent of alpha-isomer of N-acetylneuraminic acid in O-acetylated form added to terminal galactose alpha 2-6-or alpha 2-3-bonds.