Crossref journal-article
American Society for Microbiology
Journal of Bacteriology (235)
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.

Bibliography

Gehring, K., Cheng, C. H., Nikaido, H., & Jap, B. K. (1991). Stoichiometry of maltodextrin-binding sites in LamB, an outer membrane protein from Escherichia coli. Journal of Bacteriology, 173(6), 1873–1878.

Authors 4
  1. K Gehring (first)
  2. C H Cheng (additional)
  3. H Nikaido (additional)
  4. B K Jap (additional)
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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)
Funders 0

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@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} }