The pH dependence of the effects of Na+, K+ and ouabain on the ATPase activity of NaI-treated brain microsomes with Mg2+, Mn2+, Ca2+ and Zn2+ as divalent metal activators
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
Reference20 articles.
1. Highly specific sodium-potassium-activated adenosine triphosphatase from various tissues of rabbit
2. Ouabain-Sensitive Mg++-ATPase, K+-ATPase and Na+-ATPase Activities Accompanying a Highly Specific Na+-K+-ATPase Preparation
3. Comparison of some minor activities accompanying a preparation of sodium-plus-potassium ion-stimulated adenosine triphosphatase from pig brain
4. The role of bound potassium ions in the hydrolysis of low concentrations of adenosine triphosphate by preparations of membrane fragments from ox brain cerebral cortex
5. The sodium-stimulated adenosine-triphosphatase activity and other properties of cerebral microsomal fractions and subfractions
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1. (Un)suitability of the use of pH buffers in biological, biochemical and environmental studies and their interaction with metal ions – a review;RSC Advances;2015
2. Effects of pH changes on sodium pump fluxes in squid giant axon;American Journal of Physiology-Cell Physiology;1987-10-01
3. Ca2+-dependent activities of (Na+ + K+)-ATPase;Archives of Biochemistry and Biophysics;1982-07
4. Binding of divalent cation to phosphoenzyme of sodium- and potassium-transport adenosine triphosphatase.;Journal of Biological Chemistry;1978-10
5. The pre-steady-state hydrolysis of ATP by porcine brain ()-dependent ATPase;Biochimica et Biophysica Acta (BBA) - Enzymology;1977-04
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