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… 

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.

Diazacholesterol effect upon membrane ATPase.

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).

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.

Organization of enzymes in human erythrocyte membranes 1

The data are interpreted as showing that membrane phosphoglycerate kinase was oriented toward the lipid core of the membrane, whereas membrane glyceraldehyde phosphate dehydrogenase was directed toward the interior of the erythrocyte.

Localization of red cell membrane constituents.

...

References

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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.

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