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. 1991 Mar;173(6):1873–1878. doi: 10.1128/jb.173.6.1873-1878.1991

Stoichiometry of maltodextrin-binding sites in LamB, an outer membrane protein from Escherichia coli.

K Gehring 1, C H Cheng 1, H Nikaido 1, B K Jap 1
PMCID: PMC207716  PMID: 2001992

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.

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Selected References

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