Plasma Membrane Adenosine Triphosphatase of Oat Roots
Open Access
- 1 January 1975
- journal article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 55 (1), 83-86
- https://doi.org/10.1104/pp.55.1.83
Abstract
ATPase activity of plasma membrane vesicles isolated from oat (Avena sativa L. cv. Goodfield) roots was examined in the presence of various concentrations of MgCl2 and ATP. A Mg2+: ATP ratio of about 1 was required for maximal activity regardless of the concentrations used; the optimum concentration for both Mg2+ and ATP was 9 mm. Based on the ATPase activity at different concentrations of complexed Mg·ATP and free ATP, it is concluded that Mg·ATP is the true substrate of this enzyme.Keywords
This publication has 13 references indexed in Scilit:
- Nucleotide and divalent cation interactions with the (
Na K Biochimica et Biophysica Acta (BBA) - Enzymology, 1974 - Characterization of Plasma Membrane-associated Adenosine Triphosphase Activity of Oat RootsPlant Physiology, 1973
- Studies on the characterization of the sodium-potassium transport adenosinetriphosphataseArchives of Biochemistry and Biophysics, 1973
- Purification of an Ion-Stimulated Adenosine Triphosphatase from Plant Roots: Association with Plasma MembranesProceedings of the National Academy of Sciences, 1972
- Studies on the characterization of the sodium-potassium transport adenosinetriphosphataseArchives of Biochemistry and Biophysics, 1971
- Correlation between Ion Fluxes and Ion-stimulated Adenosine Triphosphatase Activity of Plant RootsPlant Physiology, 1970
- Kinetic studies of membrane (NA+-K+-Mg2+)-ATPaseBiochimica et Biophysica Acta (BBA) - Enzymology, 1970
- Monovalent Ion Stimulated Adenosine Triphosphatase From Oat RootsPlant Physiology, 1969
- A Molecular Model for a Sodium PumpNature, 1965
- The association constant of the complexes of adenosine triphosphate with magnesium, calcium, strontium, and barium ionsBiochimica et Biophysica Acta, 1961