Affinity-chromatographic studies based on the binding-specificity of the lambda receptor of Escherichia coli.

The lambda receptor in the outer-membrane of Escherichia coli is capable of binding macromolecular polysaccharides. Bio-specific binding of bacteria to covalently immobilized ligands of the lambda receptor can also be demonstrated. This finding can be exploited for the affinity-chromatographic separation of E. coli populations differing in surface-receptor characteristics. The technique is applicable to the affinity-chromatographic enrichments of mutants with changes in the lambda receptor-binding site or in the regulation of its synthesis.