Calmodulin-binding proteins in fractions purified from human submandibular glands by calmodulin-Sepharose were phosphorylated with [gamma-32P]ATP, in the absence of exogenous protein kinase. The major proteins phosphorylated had molecular masses of 45, 51 and 61 kDa. Phosphorylation was increased by activators of protein kinase C and inhibited by H-7. Phosphorylation of the 61 kDa band was markedly decreased in cystic-fibrosis submandibular glands.

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