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Calcium and calmodulin-dependent phosphorylation of kappa-casein by a bovine mammary casein kinase.

A calcium and calmodulin-dependent kappa-casein kinase activity has been described in the bovine mammary gland. This kinase required previously dephosphorylated kappa-casein for substrate, thus suggesting a physiological role for this enzyme. The kappa-casein kinase required magnesium and the presence of both calcium and calmodulin for full activity. Calmodulin concentrations of .32 microM achieved one-half maximal activation of this enzyme. The calcium and calmodulin-dependent kappa-casein kinase was found in preparations of mammary acini and could be localized in a membranous fraction by centrifugation. The particles containing this activity had a high density (1.309 g/cc) and cofractionated with caseins, suggesting this enzyme may be present in secretory granules.