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- W2238897211 abstract "Five uncoupled mutant strains of Escherichia coli carrying mutations in the uncD gene have been studied. In each of these mutant strains the beta-subunit of the F1 portion of the membrane-bound adenosine triphosphatase is abnormal. In one of the mutant strains (carrying the uncD12 allele) in F1-ATPase aggregate was formed which was purified and found to have low ATPase activity. ATPase activity was absent in the other four strains and the abnormal beta-subunits were tightly bound to the membranes. However, membranes from these strains exhibited various proton permeabilities as indicated by NADH-dependent atebrin-fluorescence quenching and bound different amounts of normal F1-ATPase. The amounts of reconstitution of energy-linked reactions after the addition of normal F1-ATPase also varied depending on the mutant allele. It is apparent that considerable phenotypic variations can occur between strains carrying mutations in the same unc gene." @default.
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- W2238897211 date "1979-04-15" @default.
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- W2238897211 title "Properties of membranes from mutant strains of <i>Escherichia coli</i> in which the β-subunit of the adenosine triphosphatase is abnormal" @default.
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- W2238897211 doi "https://doi.org/10.1042/bj1800111" @default.
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