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The Purified Calcium-Pumping ATPase of Plasma Membrane

Structure-Function Relationships
  • Ernesto Carafoli
  • Mauro Zurini
  • Gustavo Benaim

Abstract

The Ca2+-pumping ATPase of plasma membrane, known to exist since 1966 [13], has now been characterized as a high Ca2+ affinity enzyme, present in all likelihood in all eukaryotic plasma membranes (for a recent review, see Ref. 11). The essential properties of this enzyme, as they can be extracted from a very large number of studies, are summarized in Table I. The ATPase is perhaps less well characterized than other members of the E1, E2 class of transport ATPases like the Na+/K+ - ATPase and the Ca2+ - ATPase of sarcoplasmic reticulum. For example, it is still not known whether the acyl phosphate formed during the enzyme cycle is an aspartyl phosphate. It is also not established to the satisfaction of all specialists whether the Ca2+ /ATP stoichiometry is, as indicated in Table I, always and invariably 1. Recent reviews on the ATPase have appeared, the most comprehensive being perhaps the one by Schatzmann [14].

Keywords

Erythrocyte Membrane Liver Plasma Membrane Purify Plasma Membrane Eukaryotic Plasma Membrane Silver Impregnation Method 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1985

Authors and Affiliations

  • Ernesto Carafoli
    • 1
  • Mauro Zurini
    • 1
  • Gustavo Benaim
    • 1
    • 2
  1. 1.Laboratory of BiochemistrySwiss Federal Institute of Technology (ETH)ZurichSwitzerland
  2. 2.Facultad de Ciencias, Escuela de Biologia, Apartado 21201, Departamento de Biologia CelularUniversidad Central de VenezuelaCaracasVenezuela

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