The authors demonstrated an incomplete indentity of Cl. botulinum hemagglutinins of types A and B in the double diffusion reaction in agar gel, and their difference by electrophoretic mobility. Some differences in the interaction of hemagglutinins A and B with human erythrocytes were found by the hemagglutination inhibition method; apparently, of the principal significance in the relization of the reaction of human erythrocyte hemagglutination with hemagglutinins of Cl. botulinum, types A and B, was the OH-group position in the C4 galactose of the mucopolysaccharides of the erythrocyte cell wall. Apart from C4, apparently, for hemagglutinin of types A of significance was the reactive capacity of C1 and C2 galactose atoms, whereas for hemagglutinin of type B--free OH-group in C2 galactose atom.
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