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  • Title: Origins of the different sensitivities of (Na+ + K+)-dependent adenosinetriphosphatase preparations to ouabain.
    Author: Periyasamy SM, Huang WH, Askari A.
    Journal: Comp Biochem Physiol B; 1983; 76(3):449-54. PubMed ID: 6315301.
    Abstract:
    Properties of the Na+, K+-ATPase preparations from rat and dog kidney medullae were compared. The two enzymes, with a 1000-fold difference in ouabain sensitivities, had similar subunit compositions and similar K0.5 values and Hill coefficients for substrates and activators of several catalytic activities; suggesting that the structural differences of the two are limited to the ouabain binding domains. Experiments on the interactions of ouabain, Pi, and Mg2+ with the enzymes showed that the two enzymes differed (a) in their inherent affinities for ouabain; and (b) in that Mg2+ binding increased affinity for ouabain to a greater extent in the dog enzyme than in the rat enzyme.
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