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- W2040760824 abstract "Abstract We had shown previously that the lactose permease of Escherichia coli ML 308225 becomes irreversibly inactivated during lactose transport when the cells are energized by addition of an external energy source; this inactivation is concomitant with an irreversible decrease of the electrochemical potential gradient of protons (Ghazi, A., Therisod, H. and Shechter, E. (1983) J. Bacteriol. 154, 92–103). Addition to energized cells of 2-heptyl-4-hydroxyquinoline- N -oxide (HQNO), an inhibitor of the respiratory chain, suppresses these phenomena. Also, the inactivation of the lactose permease does not take place in energized E. coli K 207 cells, a mutant devoid of a functional respiratory chain. The inactivation of the lactose permease may take place in nonenergized cells and in the absence of lactose, but at a much slower rate. Addition of lactose or methyl-1-thio-β- d -galactoside (TMG), a competitive analogue of lactose, enhances the inactivation. On the other hand, addition of β- d -galactosyl-1-thio-β- d -galactoside (TDG), or p- nitrophenyl -α- d -galactoside (α-NPG), or o- nitrophenyl -β- d -galactoside (ONPG), other competitive analogues of lactose, strongly inhibits the inactivation. From these data, it is concluded that the respiratory activity of the cell in itself leads to an inactivation of the lactose permease. The presence of one class of galactosides enhances the susceptibility of the permease towards inactivation, probably by immobilizing the protein in a conformation more susceptible to the inactivating agent. In contrast, the presence of another class of galactosides can protect the protein against inactivation." @default.
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- W2040760824 date "1985-03-01" @default.
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- W2040760824 title "Inactivation of the lactose permease of Escherichia coli by the respiratory activity" @default.
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- W2040760824 doi "https://doi.org/10.1016/0005-2736(85)90420-1" @default.
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