Purification and properties of reconstitutively active and inactive adenosinetriphosphatase from Escherichia coli

M. Futai, P. C. Sternweis, L. A. Heppel

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Abstract

The Mg2+ and Ca2+ stimulated adenosine triphosphatase (ATPase) (EC 3.6.1.3; ATP phosphohydrolase) (bacterial coupling factor) was purified from two strains of E. coli by two different procedures: the method of Neslon, Kanner, and Gutnick, and by a modified procedure described in this paper. The ATPase purified from E. coli K12 (λ) by the first procedure had 4 subunits (α, β, γ, and ε). It did not bind to a deficient membrane, nor did it reconstitute ATP driven transhydrogenase activity. The modified procedure yielded 5 subunits (α, β, γ, δ, and ε). This ATPase could bind to a deficient membrane and reconstitute ATP driven transhydrogenase. This finding suggests that the δ subunit is required for the reaction with the membrane. The molecular weight of the 4 subunit ATPase was significantly lower than that of the 5 subunit ATPase, as judged by equilibrium centrifugation. The specific ATPase activities of both preparations were about the same. These two procedures were also applied to E. coli ML308 to 225.

Original languageEnglish (US)
Pages (from-to)2725-2729
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume71
Issue number7
DOIs
StatePublished - 1974

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