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- W2052439957 abstract "1.1. An attempt was made to correlate the ouabain-sensitive (Na+-K+)-activated ATPase system previously demonstrated in Escherichia coli, strain K-12, with the cation transport system in this organism.2.2. Growth of the bacterial cells in a medium containing ouabain (10−4 M) decreased the potassium content and increased the sodium content by significant and equivalent amounts.3.3. An active, glucose-dependent uptake of 86Rb+ with a half-time of 7 min was demonstrated. K+ ions competed with 86Rb+ ions for uptake by the bacterial cells. Na+ ions stimulated the 86Rb+ uptake in concentrations up to 25 mM.4.4. Ouabain (8 × 10−5 M) at pH 7·0 did not have a significant effect on the 86Rb+ uptake rate. At pH 5·3 ouabain (8 × 10−7–8 × 10−3 M) significantly inhibited the 86Rb+ uptake by maximally 10 per cent.5.5. These results indicate that E. coli possessess a slightly ouabain-sensitive Na+—K+ transport system, which is mediated by the (Na+—K+)-activated ATPase system, but which normally is overshadowed by the ouabain-insensitive H+—K+ transport system." @default.
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- W2052439957 date "1992-09-01" @default.
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- W2052439957 title "Identification of lens protein cleavage sites" @default.
- W2052439957 doi "https://doi.org/10.1016/0014-4835(92)90742-b" @default.
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