Delcayre C, Marotte N, Rappaport L
J Mol Cell Cardiol. 1983 Jan;15(1):61-5. doi: 10.1016/0022-2828(83)90308-5.
The Ca2+ -dependent phosphorylation of proteins has been recognized as a major regulatory mechanism of biological processes. In the heart, protein kinases that are activated by Ca2+ include phosphorylase kinase, myosin light chain kinase, phospholamban kinase [review in 4], and the kinases responsible for phosphorylation of endogenous proteins in the membrane [11] and soluble [6] fractions of the cell. All of these Ca2+-dependent enzymes require the presence, either as an enzyme subunit or as a cofactor, of calmodulin, a Ca2+-binding protein which is involved in various other Ca2+-requiring reactions or processes [review in 3]. We demonstrate here the presence, in the rat heart, of a soluble calmodulin-dependent protein kinase which seems different from those already described in this tissue. The substrate for this enzyme is a 43 kdaltons protein, present in the same soluble fraction.
蛋白质的钙离子依赖性磷酸化已被公认为是生物过程的主要调节机制。在心脏中，由钙离子激活的蛋白激酶包括磷酸化酶激酶、肌球蛋白轻链激酶、受磷蛋白激酶[见参考文献4中的综述]，以及负责细胞内膜[11]和可溶性[6]部分中内源性蛋白质磷酸化的激酶。所有这些钙离子依赖性酶都需要钙调蛋白的存在，钙调蛋白作为酶亚基或辅助因子，是一种钙离子结合蛋白，参与各种其他需要钙离子的反应或过程[见参考文献3中的综述]。我们在此证明，在大鼠心脏中存在一种可溶性钙调蛋白依赖性蛋白激酶，它似乎与该组织中已描述的激酶不同。这种酶的底物是一种43千道尔顿的蛋白质，存在于相同的可溶性部分中。
