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.
D000687:Amylopectin / Q000378:metabolism; D000688:Amylose / Q000378:metabolism; D001425:Bacterial Outer Membrane Proteins; D010582:Bacteriophage lambda; D002846:Chromatography, Affinity; D004926:Escherichia coli / Q000378:metabolism*; D018272:Porins; D011991:Receptors, Virus / Q000378:metabolism*
D001425:Bacterial Outer Membrane Proteins; D018272:Porins; D011991:Receptors, Virus; C016532:maltoporins; D000688:Amylose; D000687:Amylopectin