The Functional Unit of Na,K-ATPase Is a Monomeric αβ Protomer
Biochemical and Biophysical Research Communications, ISSN: 0006-291X, Vol: 280, Issue: 5, Page: 1364-1366
2001
- 9Citations
- 6Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations9
- Citation Indexes9
- CrossRef5
- Captures6
- Readers6
Article Description
The ouabain-resistant and ouabain-sensitive α-subunit cRNAs in various molar ratios were injected into Xenopus oocytes together with cRNA for the β-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 α-subunit. When a functionless mutant was used instead of the ouabain-sensitive α-subunit, similar results were obtained in ATPase activity and Rb + uptake. These results indicate that a monomeric αβ 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.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0006291X01942925; http://dx.doi.org/10.1006/bbrc.2001.4292; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0034815977&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/11162680; https://linkinghub.elsevier.com/retrieve/pii/S0006291X01942925; https://dx.doi.org/10.1006/bbrc.2001.4292
Elsevier BV
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