The steady-state kinetic mechanism of ATP hydrolysis catalyzed by membrane-bound (Na+ + K+)-ATPase from ox brain III. A minimal model
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
Reference24 articles.
1. The steady-state kinetic mechanism of ATP hydrolysis catalyzed by membrane-bound (Na+ + K+)-ATPase from ox brain I. Substrate identity
2. The steady-state kinetic mechanism of ATP hydrolysis catalyzed by membrane-bound (Na+ + K+)-ATPase from ox brain II. Kinetic characterization of phosphointermediates
3. Biochemical Aspects of Active Transport
4. Flexibility of an Active Center in Sodium-Plus-Potassium Adenosine Triphosphatase
5. Conformational transitions between Na+-bound and K+-bound forms of (Na+ + K+)-ATPase, studied with formycin nucleotides
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3. ROLE OF PROTEIN CONFORMATION CHANGES AND TRANSPHOSPHORYLATIONS IN THE FUNCTION OF Na+/K+-TRANSPORTING ADENOSINE TRIPHOSPHATASE: AN ATTEMPT AT AN INTEGRATION INTO THE Na+/K+ PUMP MECHANISM;Biological Reviews;2010-09-06
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