Shift to the Na+ from of Na+/K+-transporting ATPase due to modification of the low-affinity ATP-binding site by Co(NH3)4ATP
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1989.tb14910.x/fullpdf
Reference38 articles.
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3. Characterization of 2',3'-O-(2,4,6-trinitrocyclohexadienylidine)adenosine 5'-triphosphate as a fluorescent probe of the ATP site of sodium and potassium transport adenosine triphosphatase. Determination of nucleotide binding stoichiometry and ion-induced changes in affinity for ATP.
4. Inhibition of sodium and potassium adenosine triphosphatase by 2‘,3‘-O-(2,4,6-trinitrocyclohexadienylidene) adenine nucleotides. Implications for the structure and mechanism of the Na:K pump.
5. A study of the vanadate-trapped state of the (Na,K)-ATPase. Evidence against interacting nucleotide site models.
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2. Stimulation of p-nitrophenylphosphatase activity of Na+/K+-ATPase by NaCl with oligomycin or ATP;FEBS Journal;2005-01-10
3. Independent Access of Fluorescein Isothiocyanate and Co(NH3)4ATP to Their Binding Sites on the Protomer of Na,K-ATPase;Annals of the New York Academy of Sciences;2003-04
4. Inactivation of Na,K-ATPase Following Co(NH3)4ATP Binding at a Low Affinity Site in the Protomeric Enzyme Unit;Journal of Biological Chemistry;2003-04
5. Affinity labelling with MgATP analogues reveals coexisting Na+ and K+ forms of the alpha-subunits of Na+/K+-ATPase;European Journal of Biochemistry;1999-03-19
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