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XB-ART-9655
Biochem Biophys Res Commun 2001 Feb 09;2805:1364-6. doi: 10.1006/bbrc.2001.4292.
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The functional unit of Na,K-ATPase is a monomeric alphabeta protomer.

Takeda K , Kawamura M .


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The ouabain-resistant and ouabain-sensitive alpha-subunit cRNAs in various molar ratios were injected into Xenopus oocytes together with cRNA for the beta-subunit. The ouabain-resistant ATPase activity, as well as ouabain-resistant Rb+ uptake, of the injected oocytes increased linearly with increasing the amount of cRNA for the ouabain-resistant alpha-subunit. When a functionless mutant was used instead of the ouabain-sensitive alpha-subunit, similar results were obtained in ATPase activity and Rb+ uptake. These results indicate that a monomeric alphabeta protomer is a functional unit of membrane-bound Na,K-ATPase, even if the enzyme exists structurally as a diprotomer or higher oligomers in membranes.

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Species referenced: Xenopus
Genes referenced: atp1a1