Affinity labelling with MgATP analogues reveals coexisting Na+ and K+ forms of the alpha-subunits of Na+/K+-ATPase
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1046/j.1432-1327.1999.00260.x/fullpdf
Reference46 articles.
1. Na+,K(+)-ATPase.
2. 2′-O-Dansyl Analogs of ATP Bind with High Affinity to the Low Affinity ATP Site of Na+/K+-ATPase and Reveal the Interaction of Two ATP Sites during Catalysis
3. A Two-Site Model of Interacting ATP Sites
4. Phosphate binding and ATP-binding sites coexist in Na+/K+-transporting ATPase, as demonstrated by the inactivating MgPO4 complex analogue Co(NH3)4PO4
5. Modification of the E1ATP binding site of Na+/K+-ATPase by the chromium complex of adenosine 5'-[beta,gamma-methylene]triphosphate blocks the overall reaction but not the partial activities of the E2 conformation
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