Schwerzmann K, Müller M, Carafoli E
Biochim Biophys Acta. 1985 Jun 11;816(1):63-7. doi: 10.1016/0005-2736(85)90393-1.
The binding of calmodulin to the mitochondrial F1.F0-ATPase has been studied. [125I]Iodoazidocalmodulin binds to the epsilon-subunit and to the endogeneous ATPase inhibitor peptide in a Ca2+-dependent reaction. The effect of the mitochondrial ATPase inhibitor peptide on the purified Ca2+-ATPase of erythrocytes has also been analyzed. The inhibitor peptide stimulates the ATPase when pre-incubated with the enzyme. The activation of the Ca2+-ATPase by calmodulin is not influenced by the inhibitor peptide, indicating that the two mechanisms of activation are different. These in vitro effects of the two regulatory proteins may reflect a common origin of the two ATPases considered and/or of the regulatory proteins.
已对钙调蛋白与线粒体F1.F0 - ATP酶的结合进行了研究。[125I]碘叠氮钙调蛋白在Ca2 +依赖反应中与ε亚基及内源性ATP酶抑制肽结合。还分析了线粒体ATP酶抑制肽对纯化的红细胞Ca2 + - ATP酶的作用。该抑制肽与酶预孵育时可刺激ATP酶。钙调蛋白对Ca2 + - ATP酶的激活不受抑制肽影响，表明这两种激活机制不同。这两种调节蛋白的这些体外效应可能反映了所考虑的两种ATP酶和/或调节蛋白的共同起源。
