Comparison of E1 and E2 Conformers of Membrane Bound Na+/K+-ATPase Using Time-Resolved Phosphorescence Anisotropy Measurements
Na+/K+-ATPase is known to form oligomeric complexes in the membrane bilayer. On the other hand, there are strong evidence that monomelic form possesses all of the main hydrolytic and transport properties of the Na+-pump. This raises the question as to whether formation of oligomeric complexes is a the necessary step in the biochemical processes associated with the translocation of cations across the membrane or simply an architectural feature of the intercalation of the proteins into the phospholipid bilayer. We have addressed this question by measuring the rotational relaxation of the ATPase in different conformational states of the pump cycle using flash-photolysis methods.
KeywordsAnisotropy Glycol Oligomer Dodecyl Eosin
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