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Regulation of (Na+, K+) adenosinetriphosphatase of nerve ending membranes

Action of norepinephrine and a soluble factor

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Abstract

Norepinephrine added in vitro to nerve ending membranes from rat cerebral cortex stimulates the activity of (Na+, K+) adenosinetriphosphatase (ATPase) only in the presence of the soluble brain fraction. In its absence norepinephrine inhibits the enzyme. (Mg2+)ATPase also showed stimulation by norepinephrine in the presence of the soluble fraction, but of lesser magnitude. The activation of (Na+, K+)ATPase by norepinephrine is not reproduced by cyclic AMP and is not antagonized by either α- or β-adrenergic blocking agents. These results suggest that the stimulation caused by norepinephrine is a direct effect on the enzyme and is not mediated by cyclic AMP or adrenergic receptors.

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Authors and Affiliations

  1. Instituto de Biologia Celular Facultad de Medicina, Universidad de Buenos Aires, Paraguay 2155, 1121, Buenos Aires, Argentina

    Georgina Rodriguez de Lores Arnaiz & Marta Mistrorigo de Pacheco

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  1. Georgina Rodriguez de Lores Arnaiz
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  2. Marta Mistrorigo de Pacheco
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Rodriguez de Lores Arnaiz, G., Mistrorigo de Pacheco, M. Regulation of (Na+, K+) adenosinetriphosphatase of nerve ending membranes. Neurochem Res 3, 733–744 (1978). https://doi.org/10.1007/BF00965996

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  • DOI: https://doi.org/10.1007/BF00965996

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