In vitro Inhibition of Na+-K+ and Mg2+ ATPases by Mono, Di and Trivalent Cations.
- 1 December 1965
- journal article
- research article
- Published by Frontiers Media SA in Experimental Biology and Medicine
- Vol. 120 (3), 802-804
- https://doi.org/10.3181/00379727-120-30658
Abstract
Summary Na+-K+ ATPase has been found to be strongly inhibited in vitro by addition of silver, vanadium, copper, zinc, cadmium, lead and mercury. Calcium, strontium and barium enhance the dephosphorylation of ATP in the presence of Mg2+ dependent ATPase, while exerting an inhibitory effect on the monovalent cation stimulated portion. Cesium acts as an activator of Mg2+ ATPase in the system studied.This publication has 11 references indexed in Scilit:
- ‘Transport adenosinetriphosphatase’ in electric organ. The relation between ion transport and oxidative phosphorylationThe Journal of Physiology, 1963
- Studies on sodium-potassium-activated adenosinetriphosphatase. V. Correlation of enzyme activity with cation flux in six tissuesArchives of Biochemistry and Biophysics, 1963
- Some properties of a kidney adenosine triphosphatase relevant to active cation transportBiochemical Journal, 1962
- Cadmium enhancement of proximal tubular sodium reabsorptionAmerican Journal of Physiology-Legacy Content, 1962
- Effect of cadmium on renal tubular sodium transportAmerican Journal of Physiology-Legacy Content, 1962
- Evidence for a Prolonged Biological Half-Life of Na 22 in Patients with HypertensionCirculation Research, 1962
- Hypertension induced in rats by small doses of cadmiumAmerican Journal of Physiology-Legacy Content, 1962
- Adenosinetriphosphatase activity and the active movements of alkali metal ionsThe Journal of Physiology, 1961
- Membrane Adenosine Triphosphatase as a Participant in the Active Transport of Sodium and Potassium in the Human ErythrocyteJournal of Biological Chemistry, 1960
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951