Gehring K, Cheng C H, Nikaido H, Jap B K
Cell and Molecular Biology, Lawrence Berkeley Laboratory, California.
J Bacteriol. 1991 Mar;173(6):1873-8. doi: 10.1128/jb.173.6.1873-1878.1991.
We have directly measured the stoichiometry of maltodextrin-binding sites in LamB. Scatchard plots and computer fitting of flow dialysis (rate-of-dialysis) experiments clearly establish three independent binding sites per LamB trimer, with a dissociation constant of approximately 60 microM for maltoheptaose. The current model for LamB's function as a specific pore is discussed with respect to the symmetry in LamB's kinetic properties and the implications of our results.
我们直接测定了LamB中麦芽糊精结合位点的化学计量。Scatchard图以及流动透析(透析速率)实验的计算机拟合清楚地表明,每个LamB三聚体有三个独立的结合位点,麦芽七糖的解离常数约为60微摩尔。我们根据LamB动力学性质的对称性以及我们结果的含义,讨论了目前关于LamB作为特定孔道功能的模型。