Abstract
THREE types of high affinity ligands are available for studies with (Na+ + K+)ATPase: nucleotide substrates, vanadate and ouabain. Of these, the last is unique in apparently being absolutely specific for (Na+ + K+)ATPase. One of the generally accepted facts regarding (Na+ + K+)ATPase is that there are equal numbers of measurable (high affinity) binding sites for ATP and ouabain per molecule of enzyme1–5. There is a majority opinion that direct binding experiments yield binding capacities for these ligands of 1 mol site per 250–300 kg protein in the purest preparations available3,6–8. From these data, from determinations of the peptide composition and from estimates of the apparent molecular weight of solubilised enzyme the idea of (Na+ + K+)ATPase as a dimer (with respect to the large, so-called catalytic, peptide) has emerged9–14. Such a dimer would have one high affinity binding site for nucleotide and one for ouabain. The present report on binding site determinations on mammalian kidney microsomes before and after detergent treatment casts serious doubts on the general validity of the above simple relationship between sites and peptide composition.
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HANSEN, O., JENSEN, J., NØRBY, J. et al. A new proposal regarding the subunit composition of (Na+ + K+)ATPase. Nature 280, 410–412 (1979). https://doi.org/10.1038/280410a0
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DOI: https://doi.org/10.1038/280410a0
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