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Mutant and wild-type LamB proteins (phage λ receptor proteins) were purified by affinity chromatography with immobilized maltose-binding protein, and their transport functions were tested in reconstituted liposomes. Two mutant proteins exhibited a marked decrease in affinity for immobilized maltose-binding protein, as well as altered transport rates.

Bacteriophage Lambda Receptor Protein in Escherichia coli K-12: Lowered Affinity of Some Mutant Proteins for Maltose-Binding Protein In Vitro