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The Plasma Membrane Calcium Pump

Some Molecular Properties of the Purified Enzyme, with Emphasis on the Calmodulin-Binding Domain
  • Ernesto Carafoli
Part of the GWUMC Department of Biochemistry Annual Spring Symposia book series (GWUN)

Abstract

The Ca pump of plasma membranes is an ATPase that has a high affinity for Ca (K m 0.5µM or less) and thus it interacts with it even at the normal low cytosolic concentration (about 0.2µM). The ATPase can therefore be considered as a fine regulator of cell Ca, as opposed to the other Ca-exporting system, the Na/Ca exchanger, which is particularly active in excitable tissues, and handles much larger amounts of Ca with lower affinity. A number of regulators of potential physiological significance modulate (i.e., activate) the ATPase, among them calmodulin (Jarret and Penniston, 1987; Gopinath and Vincenzi, 1987), acidic phos pholipids and polyunsaturated fatty acids (Niggliet al., 1981), and a cAMP-dependent phosphorylation reaction (Neyseset al., 1985). Of interest, although probably not significant physiologically, is the activation of the ATPase by a controlled exposure to proteases like trypsin (Taverna and Hanahan, 1980; Sarkadiet al., 1980).

Keywords

ATPase Activity Erythrocyte Membrane Cell Calcium Calmodulin Binding Excitable Tissue 
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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References

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Copyright information

© Plenum Press, New York 1989

Authors and Affiliations

  • Ernesto Carafoli
    • 1
  1. 1.Laboratory of BiochemistrySwiss Federal Institute of Technology (ETH)ZurichSwitzerland

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