Abstract
The K99 antigen of Escherichia coli B41 was isolated by isoelectric precipitation from heated bacterial suspensions. Chromatography and immunoabsorption experiments suggested that the mannose-resistant haemagglutinating activity of partially purified preparations of antigen was K99. The antigen was partially susceptible to bacterial proteases and was inactivated by periodate oxidation. Haemagglutination inhibition experiments with sugars and absorption of K99 with antisera to human blood groups A and B substances suggested that K99 contains a terminal alpha-linked N-acetylgalactosamine moiety, which is involved in the haemagglutination reaction, and an adjacent terminal alpha-linked galactose moiety, which plays no part in the reaction.
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