Dependence on pH of substrate binding to lactose carrier in Escherichia coli cytoplasmic membranes
- 10 January 1983
- journal article
- Published by Wiley in FEBS Letters
- Vol. 151 (1), 102-104
- https://doi.org/10.1016/0014-5793(83)80352-4
Abstract
Lactose permease in Escherichia mediates proton-substrate cotransport. The molecular mechanism of this process is not understood. We examined the effect of proton concentration on the binding of a substance analogue to the carrier. The dissociation constant of p-nitrophenyl-α-galactoside from the carrier was dependent on pH, with an apparent pKa of 9.7Keywords
This publication has 14 references indexed in Scilit:
- Lactose carrier protein of Escherichia coli: interaction with galactosides and protonsBiochemistry, 1981
- Dependence on pH of Parameters of Lactose Transport in Escherichia coliEuropean Journal of Biochemistry, 1981
- The kinetics of the β-galactoside-proton symport of Escherichia coliBiochemical Journal, 1981
- Amplification and characterization of the proline transport carrier of Escherichia coli K-12 by using proT+ hybrid plasmids.Proceedings of the National Academy of Sciences, 1979
- Proton‐dependent binding of proline to carrier in Escherichia coli membraneFEBS Letters, 1977
- Stoicheiometry of lactose–proton symport across the plasma membrane of Escherichia coliBiochemical Journal, 1973
- Proton-coupled ?-galactoside translocation in non-metabolizingEscherichia coliJournal of Bioenergetics and Biomembranes, 1972
- A mutant of escherichia coli K12 energy-uncoupled for lactose transportBiochimica et Biophysica Acta (BBA) - Biomembranes, 1972
- Specific labeling and partial purification of the M protein, a component of the beta-galactoside transport system of Escherichia coli.Proceedings of the National Academy of Sciences, 1965