The anticalmodulin drugs trifluoperazine and R24571 remove the activation of the purified erythrocyte Ca2+-ATPase by acidic phospholipids and by controlled proteolysis
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(82)80274-3/fullpdf
Reference11 articles.
1. Purified (Ca2+-Mg2+)-ATPase of the erythrocyte membrane. Reconstitution and effect of calmodulin and phospholipids.
2. Acidic phospholipids, unsaturated fatty acids, and limited proteolysis mimic the effect of calmodulin on the purified erythrocyte Ca2+ - ATPase.
3. Metal requirement of the isolated red cell Ca-pump ATPase after elimination of calmodulin dependence by trypsin attack
4. Specificity of the binding of trifluoperazine to the calcium-dependent activator of phosphodiesterase and to a series of other calcium-binding proteins
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