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• W1978549408 abstract "Abstract The Ca2+- and Mg2+-activated ATPases of Escherichia coli NRC 482 and Salmonella typhimurium LT2 were purified to homogeneity. Both enzymes consisted of five polypeptides (α-ϵ). The molecular weights of the α, β, and ϵ polypeptides were 56,800, 51,800 and 13,200 for both enzymes. The molecular weights of the γ and δ polypeptides of the E. coli and S. typhimurium ATPases were 32,000 and 20,700, and 30,900 and 21,500, respectively. In both ATPases the stoichiometry of the subunits was α3β3γδϵ as determined with the 14C-labeled enzymes. The ATPases of either organism reacted with equal effectiveness with ATPase-deficient particles of the other organism to reconstitute energy-dependent transhydrogenase activity. Treatment of the homogeneous ATPases of both organisms with TPCK-trypsin stimulated ATPase activity but resulted in destruction of coupling factor activity. Trypsin treatment completely digested the δ and ϵ polypeptides, and removed up to 70% of the γ polypeptide. In the presence of the bifunctional cross-linking reagent dithiobis(succinimidyl propionate) ATPase activity was lost and cross-linking of α to β polypeptides occurred. Crosslinking of α to α or β to β polypeptides was not detected. The function of the individual polypeptides of the ATPase is discussed and a model for their spatial arrangement in the enzyme is presented." @default.
• W1978549408 created "2016-06-24" @default.
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• W1978549408 date "1975-03-01" @default.
• W1978549408 modified "2023-10-15" @default.
• W1978549408 title "Subunit composition, function, and spatial arrangement in the Ca2+- and Mg2+-activated adenosine triphosphatases of Escherichia coli and Salmonella typhimurium" @default.
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• W1978549408 doi "https://doi.org/10.1016/0003-9861(75)90467-1" @default.
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