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Properties of Sodium and Potassium Activated Adenosine Triphosphatases of Rat Brain: Effect of Cyclopropane and Other Agents Modifying Enzyme Activity

机译:大鼠脑钠和钾激活腺苷三磷酸酶的特性:环丙烷和其他药剂对酶活性的影响

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Two ATP-hydrolyzing enzyme systems (ATPases), possibly lipoprotein in nature, have been isolated from particulate fractions of rat cerebral cortex homogenates. They consist of at least two components, one Mg(2+) dependent and the other Mg(2+), Na(+) and K(+) dependent. ATP hydrolysis is measured both by orthophosphate and hydrogen ion liberation. A lack of stoichiometry exists (H(+) ion release 2X orthophosphate formation) over the first 90 seconds of the reaction. H(+) ion and phosphate release are sensitive to strophanthin, but only in the presence of Na(+) and K(+). Sulfyhdryl inhibitors including p-hydroxymercuribenzoate (POMB) and iodoacetate (IAA) inhibit both basic and Na(+)-K(+) activated ATP hydrolysis, but the enzyme system is more resistant to N-ethylamaleimide (NEM), especially the initial 'spurt' of H(+) ion release. Certain gases have an action on enzyme activity, both to decrease (cyclopropane) or increase it (air, nitrogen) at pressures above 1 atmosphere. The significance of the lack of stoichiometry between H(+) ion and orthophosphate release and the action of inhibitory agents is discussed. (Author)

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