Fe-catalyzed cleavage of the α subunit of Na/K-ATPase: Evidence for conformation-sensitive interactions between cytoplasmic domains

Benzer Materyaller

• The complex ATP–Fe(2+) serves as a specific affinity cleavage reagent in ATP-Mg(2+) sites of Na,K-ATPase: Altered ligation of Fe(2+) (Mg(2+)) ions accompanies the E(1)P→E(2)P conformational change
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• Ankyrin binds to two distinct cytoplasmic domains of Na,K-ATPase alpha subunit.
  Yazar:: Devarajan, P, ve diğerleri
  Baskı/Yayın Bilgisi: (1994)
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• A 19-kDa C-terminal tryptic fragment of the alpha chain of Na/K-ATPase is essential for occlusion and transport of cations.
  Yazar:: Karlish, S J, ve diğerleri
  Baskı/Yayın Bilgisi: (1990)
• The β Subunit of the Na(+)/K(+)-ATPase Follows the Conformational State of the Holoenzyme
  Yazar:: Dempski, Robert E., ve diğerleri
  Baskı/Yayın Bilgisi: (2005)