Different conformational states of the purified Ca2+-ATPase of the erythrocyte plasma membrane revealed by controlled trypsin proteolysis.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference16 articles.
1. Acidic phospholipids, unsaturated fatty acids, and limited proteolysis mimic the effect of calmodulin on the purified erythrocyte Ca2+ - ATPase.
2. Molecular properties of calcium-pumping ATPase from human erythrocytes
3. Metal requirement of the isolated red cell Ca-pump ATPase after elimination of calmodulin dependence by trypsin attack
4. Controlled proteolysis of the purified Ca2+-ATPase of the erythrocyte membrane. A correlation between the structure and the function of the enzyme.
5. Trypsin activation of the red cell Ca2+-pump ATPase is calcium-sensitive
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