Stoichiometry of maltodextrin-binding sites in LamB, an outer membrane protein from Escherichia coli
- 1 March 1991
- journal article
- research article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 173 (6) , 1873-1878
- https://doi.org/10.1128/jb.173.6.1873-1878.1991
Abstract
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.Keywords
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