## Abstract Human red blood cells (RBC) contain a cytoplasmic, nonhemoglobin protein which activates the (Ca^2+^βMg^2+^) ATPase of isolated RBC membranes. Results presented in this paper confirm that activation of (Ca^2+^βMg^2+^)ATPase is associated with binding of the cytoplasmic activator to the
Observations on the protein activator of erythrocyte membrane (Ca2+ + Mg2+)ATPase
β Scribed by K.S. Au
- Publisher
- Elsevier Science
- Year
- 1979
- Tongue
- English
- Weight
- 716 KB
- Volume
- 10
- Category
- Article
- ISSN
- 0020-711X
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Erythrocyte membranes prepared by three different procedures showed (Mg2+ + Ca2+)-ATPase activities differing in specific activity and in affinity for Ca2+. The (Mg2+ + Ca2+)-ATPase activity of the three preparations was stimulated t o different extents by a Ca2+-dependent protein activator isolated
## Abstract Red blood cells contain a protein that activates membraneβbound (Ca^2+^ + Mg^2+^)βATPase and Ca^2+^ transport. The red blood cell activator protein is similar to a modulator protein that stimulates cyclic AMP phosphodiesterase. Wang and Desai [Journal of Biological Chemistry 252:4175β41
## Abstract Crosslinking of membrane proteins of Escherichia coli with dithiobis (succinimidyl propionate) (DSP) resulted in loss of several enzyme activities including the Ca^2+^, Mg^2+^βactivated ATPase. This enzyme was crosslinked by DSP to the membrane and was not released by dialysis at low io