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  • Title: Phosphorylation of a 43 kdaltons protein from rat heart by a calmodulin-dependent protein kinase.
    Author: Delcayre C, Marotte N, Rappaport L.
    Journal: J Mol Cell Cardiol; 1983 Jan; 15(1):61-5. PubMed ID: 6842615.
    Abstract:
    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.
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