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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Dates
Type | When |
---|---|
Created | 8 years, 10 months ago (Nov. 4, 2016, 1:52 p.m.) |
Deposited | 2 years ago (Aug. 20, 2023, 3:25 p.m.) |
Indexed | 1 year, 8 months ago (Dec. 8, 2023, 3:32 a.m.) |
Issued | 34 years, 6 months ago (March 1, 1991) |
Published | 34 years, 6 months ago (March 1, 1991) |
Published Print | 34 years, 6 months ago (March 1, 1991) |
@article{Gehring_1991, title={Stoichiometry of maltodextrin-binding sites in LamB, an outer membrane protein from Escherichia coli}, volume={173}, ISSN={1098-5530}, url={http://dx.doi.org/10.1128/jb.173.6.1873-1878.1991}, DOI={10.1128/jb.173.6.1873-1878.1991}, number={6}, journal={Journal of Bacteriology}, publisher={American Society for Microbiology}, author={Gehring, K and Cheng, C H and Nikaido, H and Jap, B K}, year={1991}, month=mar, pages={1873–1878} }