Nakae T, Ishii J N
Ann Microbiol (Paris). 1982 Jan;133A(1):21-5.
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.
大肠杆菌的噬菌体λ受体蛋白，即LamB蛋白，形成寡聚聚集体以构建对麦芽糖和麦芽糊精具有选择性的跨膜扩散孔。分别通过在均相非离子表面活性剂和重水中以及在6 M盐酸胍中的沉降平衡分析来测定功能性寡聚体以及解离单体的分子量（MW）。寡聚体和单体的MW分别显示为135600和45900。因此，功能性Lamb蛋白由三个相同的亚基组成。
