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- W2026148824 abstract "During centrifugation of Dictyostelium membranes on sucrose and metrizamide gradients, an ATPase activity resistant to azide and molybdate but sensitive to diethylstilbestrol was found to copurify with the plasma membrane markers alkaline phosphatase and 125I in cells surface-labelled by lactoperoxidase catalyzed iodination. This ATPase was enriched 50-fold in purified plasma membranes and could be separated from the mitochondrial ATPase on metrizamide gradients. The plasma membrane ATPase is very specific for ATP as substrate and Mg2+ as essential cofactor. Its pH optimum is 6.5 and it is inhibited by dicyclohexylcarbodiimide, diethylstilbestrol, vanadate, mercurials and Cu2+, but not by ouabain, molybdate, azide or oligomycin. It was not specifically affected by either monovalent cations or anions. These results suggest that the plasma membranes of Dictyostelium contain an ATPase similar to the proton-pumping ATPases recently identified in fungal and plant plasma membranes (Serrano, R. (1984) Curr. Top. Cell. Regul. 23, 87–126)." @default.
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- W2026148824 date "1985-01-01" @default.
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- W2026148824 title "The plasma membrane ATPase of Dictyostelium discoideum" @default.
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- W2026148824 doi "https://doi.org/10.1016/0005-2736(85)90330-x" @default.
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