Bacteriophage lambda receptor protein in Escherichia coli K-12: lowered affinity of some mutant proteins for maltose-binding protein in vitro.

Mutant and wild-type LamB proteins (phage lambda 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.