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• W2065466246 abstract "The conditions for optimal activity of Na+-K+-dependent ATPase (E.C. 3.6.1.3) in microsomal preparations from the combined Malpighian tubules and hindgut of Homorocoryphus nitidulus vicinus, were determined. Preincubation of the enzyme at 30°C, without ATP, caused a reduction in Na+-K+-dependent ATPase activity of approximately 15% hr−1. The pH optimum lay between 7.25–7.50. The temperatyre optima for Na+-K+ dependent-ATPase and Mg2+ ATPase were 42°C and 45°C respectively. Activation energies of between 17.66 and 24.38 Kcal mole−1 were obtained for Na+-K+ dependent ATPase for the temperature range 15° to 25°C. Incubations at low temperatures caused an increase in the affinity of Na+-K+ dependent ATPase for potassium ions as well as reducing the inhibitory effect of ouabain. Maximal activation of the enzyme was found over a range of Mg2+: ATP of 1:0.5–1. Na+ and K+ concentrations of 100 mM and 20 to 25 mM respectively were required for maximal activation of Na+-K+ dependent ATPase at 30°C. The Km of Na+-K+ dependent ATPase was 0.14 m-mol 1−1 ATP. Vmax was approximately 240 nmole Pi liberated mg protein−1 min−1. Na+-K+ dependent ATPase was inhibited by ouabain, ethacrynic acid and ethanol. Concentrations of between 10−6 and 10−7 M ouabain, 2 and 3 mM ethacrynic acid and concentrations of 2.5% ethanol, reduced Na+-K+ dependent ATPase activity by 50%." @default.
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• W2065466246 date "1976-01-01" @default.
• W2065466246 modified "2023-09-29" @default.
• W2065466246 title "Properties of Na+-K+-dependent ATPase from the malpighian tubules and hindgut of Homorocoryphus nitidulus vicinus" @default.
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• W2065466246 doi "https://doi.org/10.1016/0020-1790(76)90095-0" @default.
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