Abstract
The recpetor for the phage lambda, a protein component of the outer membrane, is present at decreased levels in strains of Escherichia coli that are deficient in lipopolysaccharide. Loss of the protein was quantitated both by an assay of the phage receptor function and by an assay of antiserum-blocking ability to detect inactive protein. The loss of protein was correlated with the loss of sugar residues and phosphage from the core region of the lipopolysaccharide. Implications for the importance of ionic interactions in the stabilization of the outer membrane are discussed.
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