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  • Title: Minimal functional unit for transport and enzyme activities of (Na+ + K+)-ATPase as determined by radiation inactivation.
    Author: Karlish SJ, Kempner ES.
    Journal: Biochim Biophys Acta; 1984 Oct 03; 776(2):288-98. PubMed ID: 6089887.
    Abstract:
    Frozen aqueous suspensions of partially purified membrane-bound renal (Na+ + K+)-ATPase have been irradiated at -135 degrees C with high-energy electrons. (Na+ + K+)-ATPase and K+-phosphatase activities are inactivated exponentially with apparent target sizes of 184 +/- 4 kDa and 125 +/- 3 kDa, respectively. These values are significantly lower then found previously from irradiation of lyophilized membranes. After reconstitution of irradiated (Na+ + K+)-ATPase into phospholipid vesicles the following transport functions have been measured and target sizes calculated from the exponential inactivation curves: ATP-dependent Na+-K+ exchange, 201 +/- 4 kDa; (ATP + Pi)-activated Rb+-Rb+ exchange, 206 +/- 7 kDa and ATP-independent Rb+-Rb+ exchange, 117 +/- 4 kDa. The apparent size of the alpha-chain, judged by disappearance of Coomassie stain on SDS-gels, lies between 115 and 141 kDa. That for the beta-glycoprotein, though clearly smaller, could not be estimated. We draw the following conclusions: (1) The simplest interpretation of the results is that the minimal functional unit for (Na+ + K+)-ATPase is alpha beta. (2) The inactivation target size for (Na+ + K+)-dependent ATP hydrolysis is the same as for ATP-dependent pumping of Na+ and K+. (3) The target sizes, for K+-phosphatase (125 kDa) and ATP-independent Rb+-Rb+ exchange (117 kDa) are indistinguishable from that of the alpha-chain itself, suggesting that cation binding sites and transport pathways, and the p-nitrophenyl phosphate binding site are located exclusively on the alpha-chain. (4) ATP-dependent activities appear to depend on the integrity of an alpha beta complex.
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