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- W2034632838 abstract "The effects of chemical modifications of the Na+-H+ antiport in Escherichia coli have been analyzed by studying the resulting variations of the energy-dependent, downhill Na+ efflux from membrane vesicles. The histidyl reagent diethylpyrocarbonate (EtO)2C2O3 prevents the activation of the Na+ efflux mechanism by delta microH+ or its components. Inactivation of the antiporter by (EtO)2C2O3 is completely reversed by hydroxylamine. The data suggest that histidine residues are involved in the molecular mechanism of the Na+-H+ antiport. In contrast, no conclusive evidence suggesting participation of carboxylic, tyrosine or sulfhydryl residues in the Na+-H+ exchange reaction has been obtained." @default.
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- W2034632838 date "1985-04-01" @default.
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- W2034632838 title "Chemical modifications of the Na+ - H+ antiport in Escherichia coli membrane vesicles" @default.
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- W2034632838 doi "https://doi.org/10.1111/j.1432-1033.1985.tb08823.x" @default.
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