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- W2070056757 abstract "1.1. Activation of Mg2+-ATPase of rabbit and guinea-pig erythrocyte membrane by bicarbonate or chloride could be completely abolished by ethylene-glycol-bis-(β-aminoethylether)-N,N'-tetraacetic acid. The anion stimulation was actually an activation of contaminating Ca2+ -stimulated Mg2+-ATPase by monovalent cations associated with the anions.2.2. Guinea-pig red cell Ca2+-Mg2+-ATPase could be activated by both sodium and potassium while the rabbit enzyme was sensitive only to sodium. The concentrations of monovalent cations for half-maximal stimulation of Ca2+-Mg2+-ATPase are: kna+ = 40.8 mM, kk+ = 12.2 mM (guinea-pig); KNa+ = 13.3mM (rabbit).3.3. Potassium enhanced activation of rabbit erythrocyte membrane Ca2+-Mg2+-ATPase by red cell Ca2+-Mg2+-ATPase activator protein. With the guinea pig enzyme, neither sodium nor potassium enhanced activator stimulation of Ca2+-Mg2+-ATPase.4.4. Ca2+-Mg2+-ATPase of aged rabbit erythrocyte membrane responded to sodium but not to activator protein.5.5. Triton X-100 solubilized rabbit erythrocyte membrane Ca2+-Mg2+-ATPase has an apparent molecular weight of 371,000. It did not respond to the activator.6.6. One major and three minor proteins, visualized by SDS-polyacrylamide gel electrophoresis, were extracted from rabbit erythrocyte membrane by 50 μM chlorpromazine." @default.
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- W2070056757 date "1980-01-01" @default.
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- W2070056757 title "Erythrocyte membrane anion-sensitive Mg2+-ATPase—Identity with monovalent cation sensitive Ca2+-Mg2+-ATPase" @default.
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- W2070056757 doi "https://doi.org/10.1016/0020-711x(80)90010-5" @default.
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