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Biosci Rep. 1999 Apr;19(2):109-14.

Phosphorylation of H,K-ATPase alpha-subunit in microsomes from rabbit gastric mucosa by cAMP-dependent protein kinase.

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Department of Biochemistry, School of Biology, M.V. Lomonosov Moscow State University, Russia.


A 100-kDa protein that is a main component of the microsomal fraction from rabbit gastric mucosa is phosphorylated by cAMP-dependent protein kinase (PKA) in the presence of 0.2% Triton X-100. Microsomes from rabbit gastric mucosa possess activity of H,K-ATPase but not activity of Na,K-ATPase. Incubation of microsomes with 5 microM fluorescein 5'-isothiocyanate (FITC) results in both an inhibition of H,K-ATPase and labeling of a protein with an electrophoretic mobility corresponding to the mobility of the protein phosphorylated by PKA. The data suggest that the alpha-subunit of H,K-ATPase can be a potential target for PKA phosphorylation.

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