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Structurally Different Nucleotide Binding Sites in Na,K-ATPase

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Koepsell,  Hermann
Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Ollig,  Doris
Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Koepsell, H., & Ollig, D. (1983). Structurally Different Nucleotide Binding Sites in Na,K-ATPase. In F. Bronner, & A. Kleinzeller (Eds.), Current Topics in Membranes and Transport (pp. 355-359). doi:10.1016/S0070-2161(08)60587-0.


Cite as: http://hdl.handle.net/21.11116/0000-0008-1D16-0
Abstract
Publisher Summary: This chapter discusses the structurally different nucleotide binding sites in Na, K-ATPase. Information on nucleotide binding sites of purified membrane-bound Na, K-ATPase isolated from the outer medulla of rat kidneys was obtained by three independent methods: (1) by measuring nucleotide effects on the inhibition of the enzyme with the ATP analog 6-[(3-carboxy-4-nitrophenyl)thiol]-98-V-ribo­furanosylpurine 5’-triphosphate (Nbs6ITP), (2) by measuring nucleotide effects on the enzyme inhibition with the SH-group reagent 5,5’-dithio­bis(2-nitrobenzoic acid) (DTNB), and (3) by analyzing the effects of ADP and AMP-PNP on the K+-dependent phosphatase activity of the Na, K-ATPase. The chapter graphically represents the inhibition of K+-dependent phosphatase activity by ADP in the presence and absence of additional nucleotides. The data presented in the chapter provide arguments for the existence of two simultaneously present nucleotide-binding sites in the Na, K-ATPase. The irreversible interaction of the Na, K­ATPase substrate Nbs6ITP is at nonhydrolyzing conditions differentially affected by low and high nucleotide concentrations. A nucleotide effect on the DTNB inactivation of the Na, K-ATPase observed in the absence of Na+ was specific for ATP and AMP-PNP but was not found with ADP.