Conformational dynamics of the Na+/K+-ATPase probed by voltage clamp fluorometry
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چکیده
منابع مشابه
Conformational dynamics of the Na+/K+-ATPase probed by voltage clamp fluorometry.
The method of voltage clamp fluorometry combined with site-directed fluorescence labeling was used to detect local protein motions of the fully active Na(+)K(+)-ATPase in real time under physiological conditions. Because helix M5 extends from the cytoplasmic site of ATP hydrolysis into the cation binding region, we chose the extracellular M5-M6 loop of the sheep alpha(1)-subunit for the inserti...
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Whereas electrogenic partial reactions of the Na,K-ATPase have been studied in depth, much less is known about the influence of the membrane potential on the electroneutrally operating gastric H,K-ATPase. In this work, we investigated site-specifically fluorescence-labeled H,K-ATPase expressed in Xenopus oocytes by voltage clamp fluorometry to monitor the voltage-dependent distribution between ...
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The hitherto unknown NT-regulated mechanism of NaK-ATPase localized in the nerve ending membranes is found. The mechanism certainly has a functional significance and must be involved in the regulation – modulation of chemical synaptic transmission. On the other hand , the availability of the discovered specific protein, regulators (SFa and SFi) of synaptic origin, makes it possible to consider ...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2003
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.0337336100