The functional unit of Na,K-ATPase is a monomeric alphabeta protomer |
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Authors: | Takeda K Kawamura M |
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Affiliation: | Department of Biology, University of Occupational and Environmental Health, Kitakyushu, 807-8555, Japan. |
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Abstract: | 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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