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- W1828771857 abstract "This chapter describes the binding properties of monovalent cations to the Na, K-ATPase. A simplified reaction scheme of Na, K-ATPase is expressed in the chapter where 3 Na+ and 2 K+ are actively transported through the plasma membrane, coupled to the hydrolysis of 1 ATP molecule that is catalyzed by Na, K-ATPase. The first measurement of the binding of monovalent cations to the Na, K-ATPase was made by Kaniike et al., using the ultracentrifugal separation method. They showed that 3 moles of Na+ bind to 1 mole of ouabain-binding site. In precipitates obtained by ultracentrifugation, active sites do not distribute randomly, as a layer structure of membrane is formed. Therefore, a new membrane filtration method is developed that does not disturb equilibrium and help measure the cation binding during the ATPase reaction. The amounts of Na+, K+, Rb+, and ATP bound to the enzyme were measured by a modified membrane filtration method. The reaction mixture contained the enzyme, radioactive monovalent cations or ATP, and [3H] glucose." @default.
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- W1828771857 date "1983-01-01" @default.
- W1828771857 modified "2023-10-12" @default.
- W1828771857 title "Binding of Monovalent Cations to the Na,K-ATPase" @default.
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- W1828771857 doi "https://doi.org/10.1016/s0070-2161(08)60569-9" @default.
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