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.
Defective phosphorylation of a calmodulin-binding protein in cystic-fibrosis submandibular glands
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D K Shori, R L Dormer, M C Goodchild, M A McPherson; Defective phosphorylation of a calmodulin-binding protein in cystic-fibrosis submandibular glands. Biochem J 15 October 1989; 263 (2): 613–616. doi: https://doi.org/10.1042/bj2630613
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