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- W1555058476 abstract "An ATP-hydrolyzing enzyme system (ATPase) has been found in the ‘microsomal’ fraction of heart muscle homogenates, which appears to consist of at least two components, one, Mg2+-dependent and the other, Mg2+ + Na+ + K+-dependent. Various inhibitory agents were employed in order to differentiate these two components or sites of activity. Amytal and ethyl alcohol are representative of compounds that inhibit the Mg2+ + Na+ + K+-dependent activity to a greater extent than the Mg2+-dependent activity. Ouabain and p-hydroxymercuribenzoate. (POMB) specifically inhibit the Mg2+ + Na+ + K+-ATPase activity while having little or no effect on the basic Mg2+-activity. The POMB-sensitive portion of the enzyme system appears to be sensitive to ouabain. Sodium azide, guanidine, and trinitrobenzenesulfonic acid represent compounds which preferentially inhibit the basic Mg2+ activity of the heart muscle, while being almost unreactive on a similar enzyme system from brain. These substances markedly increase the sensitivity of the enzyme system to both ouabain and to sulfhydryl group inhibitors. The possibility that certain charged groups are involved in the effect of ouabain on the membrane ATPase system from heart muscle is discussed." @default.
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- W1555058476 date "1964-03-01" @default.
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- W1555058476 title "A sodium-and potassium-stimulated adenosine triphosphatase from cardiac tissues—II" @default.
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- W1555058476 doi "https://doi.org/10.1016/0006-2952(64)90149-2" @default.
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