Abstract
Lipopolysaccharide isolated from colicin E2-sensitive Escherichia coli and from “receptor-minus” mutants inhibits the activity of colicin E2. Lipid A and the polysaccharide fraction obtained by mild acid hydrolysis of lipopolysaccharide are inactive either alone or when tested in combination. Periodate oxidation of lipopolysaccharide destroys over 85% of its inhibition activity.
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Selected References
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