Lipoprotein Nature of Red Cell Adenosine Triphosphatase

@article{Schatzmann1962LipoproteinNO,
  title={Lipoprotein Nature of Red Cell Adenosine Triphosphatase},
  author={Hans J. Schatzmann},
  journal={Nature},
  year={1962},
  volume={196},
  pages={677-677}
}
THE adenosine triphosphatase activity of stromata prepared from human red cells has recently been thoroughly investigated by Post et al.1 and by Dunham and Glynn2. The authors were able to demonstrate that in this ATPase, which is activated by magnesium and shows optimal efficacy at pH 7, two fractions can be distinguished, one being activated by calcium and another being inhibited by calcium and activated by sodium and potassium. The part activated by sodium and potassium amounts to 30–50 per… 
View on Nature
nature.com
92 Citations
Background Citations
1

92 Citations

Effects of Organic Solvents on the Adenosine Triphosphatase Activity of Erythrocyte Ghosts

The involvement of lipid fractions in the ATPase activities is investigated and a specific inactivation of the Na+–plus–K+ stimulated ATPase is reported after treatment of ghosts with phospholipase A.

EFFECT OF MONOVALENT CATIONS ON THE ADENOSINETRIPHOSPHATASE OF SONICATED ERYTHROCYTE MEMBRANE.

The nature of phospholipase C from Acinetobacter calcoaceticus: effects on whole red cells and red cell membranes.

  • V. Lehmann
  • Biology, Chemistry
    Acta pathologica et microbiologica Scandinavica. Section B: Microbiology and immunology
  • 1973
The effect of chelating agents and divalent metal ions on the enzymatic reaction of phospholipase C (haemolysin) of Acinetobacter calcoaceticus has been examined and the total enzyme activity was found to consist of a basal activity (BA) in the absence of Mg2+, plus an increase in activity induced by the addition of M g2+ (MgA).

Sodium-potassium-activated adenosine triphosphatase. IV. Characterization of the phosphoprotein formed from orthophosphate in the presence of ouabain.

ATPase Activity of the Sodium Pump needs Phosphatidylserine

Evidence has accumulated that the Na+, K+-activated ATPase is eliminated when lipids are removed from membranes by solvent extraction, treatment with detergents, or exposure to phospholipases, so the question arises whether phospholIPid might provide a carrier system in which the protein of the ATP enzyme is also involved, such that the ATPase activity depends on lipid as well as protein.

Localization of red cell membrane constituents.

Purification and properties of adenosinetriphosphatase from Zea mays seedling microsomes

Ro le of phospholipids in the NA + ,K + -stimulated adenosine triphosphatase system of brain microsomes.

  • W. L. Stahl
  • Biology, Computer Science
    Archives of biochemistry and biophysics
  • 1973

Studies on the characterization of the sodium-potassium transport adenosine triphosphatase. 8. Effects of ligands on fluorescence due to interaction of the enzyme with a fluorescent derivative of hellebrigenin.

THE EFFECT OF PHOSPHOLIPASE C ON THE ACTIVITY OF ADENOSINE TRIPHOSPHATASE AND ACETYLCHOLINESTERASE IN SYNAPTIC MEMBRANES ISOLATED FROM THE CEREBRAL CORTEX OF SQUIRREL MONKEY 1

Kinetic studies revealed that treatment with phospholipase C may produce a non‐competitive type of inhibition as a result of the cleavage of a charged phosphorylated nitrogen base from membrane lipids.
...

References

SHOWING 1-6 OF 6 REFERENCES

STUDIES ON ADENOSINETRIPHOSPHATASE OF MUSCLE III. THE LIPOPROTEIN NATURE OF THE MAGNESIUM-ACTIVATED ADENOSINETRIPHOSPHATASE

Continued attempts to purify the ATPase by separation of the protein and lipide components have produced substantial evidence that the association between lipide and protein is essential for the characteristic ATPase activity.

Adenosinetriphosphatase activity and the active movements of alkali metal ions

The experiments to be described in the present paper were designed to see whether the red cell membrane possesses adenosinetriphosphatase activity and whether this ATP-ase activity is connected with the mechanisms responsible for ion transport.

The influence of some cations on an adenosine triphosphatase from peripheral nerves.

  • J. Skou
  • Biology
    Biochimica et biophysica acta
  • 1957

Further investigations on a Mg++ + Na+-activated adenosintriphosphatase, possibly related to the active, linked transport of Na+ and K+ across the nerve membrane

Membrane adenosine triphosphatase as a participant in the active transport of sodium and potassium in the human erythrocyte.

Der Arbeitszyklus geordneter Aktomyosinsysteme (Muskel und Muskelmodelle)

. 1. Das Aktomyosin des Warmblütermuskels befindet sich in Abwesenheit von ATP im Zustand der Starre. Der Elastizitätsmodul (EM) des intakten Warmblütermuskels wie des Fasermodells aus…