Affiliation:
1. Cell and Molecular Biology, Lawrence Berkeley Laboratory, California.
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.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
14 articles.
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