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Interaction between cytoplasmic (Ca2+—Mg2+) ATPase activator and the erythrocyte membrane

✍ Scribed by Vincenzi, Frank F. ;Farrance, Martha L.

Publisher
Wiley (John Wiley & Sons)
Year
1977
Tongue
English
Weight
376 KB
Volume
7
Category
Article
ISSN
0091-7419

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✦ Synopsis

Abstract

Human red blood cells (RBC) contain a cytoplasmic, nonhemoglobin protein which activates the (Ca^2+^‐Mg^2+^) ATPase of isolated RBC membranes. Results presented in this paper confirm that activation of (Ca^2+^‐Mg^2+^)ATPase is associated with binding of the cytoplasmic activator to the membrane. Binding of the cytoplasmic activator is reversible and dependent on ionic strength and Ca^2+^. Cytoplasmic activator is sensitive to trypsin but is not degraded when intact RBC are exposed to trypsin. Cytoplasmic activator does not modify the (Ca^2+^‐Mg^2+^)‐ATPase of membranes from RBC exposed to activator prior to hemolysis. Thus, the activator is located in the cell and appears to act by binding to the inner membrane surface.

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