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- W2065321693 abstract "1 The inactive ATPase of four different mutant strains of Escherichia coli have been purified to homogeneity. 2 Molecular weight, subunit patterns in sodium dodecylsulfate electrophoresis and immunological prperties of mutant and wild-type proteins are identical. The mutant enzymes compete with the wild-type enzyme for the binding sites on themembrane. 3 On freezing and thawing in salt solutions, the ATPase is split into subunits IA (α, γ, ɛ), IB (δα, γ, ɛ), and II (β). By complementation in vitro of the isolated subunits, it is shown that subcomplex IA (α, γ, ɛ) is latered in the mutant strains described here." @default.
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- W2065321693 date "1978-06-01" @default.
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- W2065321693 title "Complementation in vitro of Mutant and Wild-Type ATPase of Escherichia coli Using Isolated Subunits" @default.
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- W2065321693 doi "https://doi.org/10.1111/j.1432-1033.1978.tb12362.x" @default.
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