The steady-state kinetic mechanism of ATP hydrolysis catalyzed by membrane-bound (Na+ + K+)-ATPase from ox brain IV. Rate constant determination
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
Reference9 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. The steady-state kinetic mechanism of ATP hydrolysis catalyzed by membrane-bound (Na+ + K+)-ATPase from ox brain III. A minimal model
4. Bovine brain Na+, K′-stimulated ATP phosphohydrolase studied by a rapid-mixing technique, K′-stimulated liberation of [32P]orthophosphate from [32P]phosphoenzyme and resolution of the dephosphorylation into two phases
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