The steady-state kinetic mechanism of ATP hydrolysis catalyzed by membrane-bound (Na+ + K+)-ATPase from ox brain IV. Rate constant determination
- 1 November 1981
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Biomembranes
- Vol. 648 (2) , 231-246
- https://doi.org/10.1016/0005-2736(81)90039-0
Abstract
No abstract availableKeywords
This publication has 7 references indexed in Scilit:
- The steady-state kinetic mechanism of ATP hydrolysis catalyzed by membrane-bound (Na+ + K+)-ATPase from ox brain III. A minimal modelBiochimica et Biophysica Acta (BBA) - Biomembranes, 1981
- The steady-state kinetic mechanism of ATP hydrolysis catalyzed by membrane-bound (Na+ + K+)-ATPase from ox brain II. Kinetic characterization of phosphointermediatesBiochimica et Biophysica Acta (BBA) - Biomembranes, 1981
- The steady-state kinetic mechanism of ATP hydrolysis catalyzed by membrane-bound (Na+ + K+)-ATPase from ox brain I. Substrate identityBiochimica et Biophysica Acta (BBA) - Biomembranes, 1981
- Conformational transitions between Na+-bound and K+-bound forms of (Na+ + K+)-ATPase, studied with formycin nucleotidesBiochimica et Biophysica Acta (BBA) - Enzymology, 1978
- 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 phasesBiochimica et Biophysica Acta (BBA) - Enzymology, 1975
- Phosphorylation and dephosphorylation reactions of bovine brain (Na+K+)-stimulated ATP phosphohydrolase studied by a rapid-mixing techniqueBiochimica et Biophysica Acta (BBA) - Enzymology, 1974
- Relaxations-spektrometrische Untersuchungen schneller Reaktionen von ATP in wässeriger LösungZeitschrift für Naturforschung B, 1960