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Dependence on pH of substrate binding to lactose carrier in Escherichia coli cytoplasmic membranes
Author(s) -
Yamato I.,
Rosenbusch J.P.
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80352-4
Subject(s) - lactose permease , dissociation constant , escherichia coli , chemistry , cotransporter , membrane , substrate (aquarium) , lactose , dissociation (chemistry) , permease , binding site , membrane transport protein , biochemistry , biophysics , membrane protein , biology , organic chemistry , sodium , ecology , receptor , gene
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 p K a of 9.7.