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- W99496661 abstract "(Na+ + K+)-activated ATPase is the biochemical equivalent of the sodium pump of mammalian cell membranes (1, 2). The enzyme transformes the energy, which is obtained from the hydrolysis of 1 mol ATP to ADP and phosphate, into the vectorial transport of 3 mol Na+ out of the cell and of 2 mol K+ into the cell. This stoichiometry has been obtained with the intact system of the red blood cell (3, 4) and after reconstitution of the sodium pump by incorporating the purified enzyme into liposomes (5). The transport of cations seems to occur via the Na+ - dependent formation of a phosphorylated intermediate, whose hydrolysis is activated by the presence of K+ (2). More recently it has been proposed that the active transport of Na+ and K+ occurs through reciprocating conformational changes of two chemically identical subunits (6, 7) showing half-of-the sites reactivity (7). If this assumption were right, one should find a negative cooperativity of the ATP and ouabain binding sites and of the substrate dependency of (Na+ + K+)-ATPase. This finding is demonstrated in this report." @default.
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- W99496661 date "1977-01-01" @default.
- W99496661 modified "2023-09-27" @default.
- W99496661 title "Biochemical Characteristics of the Sodium Pump: Indications for a Half-of-Sites Reactivity of (Na+ + K+)-ATPase" @default.
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- W99496661 doi "https://doi.org/10.1007/978-3-642-46352-5_13" @default.
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