Molecular weights and subunit structure of LamB proteins.
Phage lambda-receptor proteins of Escherichia coli, LamB proteins, form oligomeric aggregates to build transmembrane diffusion pores selective for maltose and maltodextrins. The molecular weights (MW) of functional oligomers as well as dissociated monomers were determined by sedimentation equilibrium analysis in homogeneous non-ionic surfactant and deuterium oxide and in 6 M guanidine-HCl, respectively. The MW of oligomers and monomers appeared as 135 600 and 45 900, respectively. Thus, functional Lamb proteins consisted of three identical subunits.
D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins / Q000032:analysis*; D010582:Bacteriophage lambda / Q000032:analysis*; D002851:Chromatography, High Pressure Liquid; D004926:Escherichia coli / Q000032:analysis*; D008970:Molecular Weight; D018272:Porins; D011991:Receptors, Virus / Q000032:analysis*; D014461:Ultracentrifugation
D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D018272:Porins; D011991:Receptors, Virus; C016532:maltoporins