Effects of potassium, temperature and time on ouabain interaction with the cardiac Na+, K+-ATPase: further evidence supporting an allosteric site |
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| Authors: | J C Allen A Schwartz |
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| Affiliation: | 1. Université Montpellier, Adaptation Ecophysiologique et Ontogenèse, UMR9190 MARBEC, cc 092, Place E. Bataillon, 34095 Montpellier cedex 05, France;2. Ifremer, LEAD, BP2059, 98846 Nouméa Cedex, New Caledonia;3. Alfred-Wegener-Institut für Polar- und Meeresforschung, Biologische Anstalt Helgoland, 27498 Helgoland, Germany |
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| Abstract: | Na+, K+-ATPase was isolated from calf heart. The specific activity was measured by a spectrophotometric method which allowed continual monitoring of the reaction. Ouabain-induced inhibition of the enzyme system was shown to be both temperature and time-dependent. [3H]Ouabain binding in the presence of ATP, Mg2+, Na+ and K+ was shown to be time-dependent. A direct temporal correlation between ouabain binding and inhibition of specific activity of the enzyme system was demonstrated. The effects of K+ and ouabain reinforce the allosteric nature of the Na+, K+-ATPase. |
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