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 μM 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 α-subunit of H,K-ATPase can be a potential target for PKA phosphorylation.

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Keywords cAMP-dependent protein kinase, Gastric mucosa, H, K-ATPase, H+-secretion, Phosphorylation
Persistent URL dx.doi.org/10.1023/A:1020110510609
Journal Bioscience Reports
Murtazina, D.A. (Dilyara A.), Petukhov, S.P. (Sergei P.), Storey, K, Rubtsov, A.M. (Alexander M.), & Lopina, O.D. (Olga D.). (1999). Phosphorylation of H,K-ATPase α-subunit in microsomes from rabbit gastric mucosa by cAMP-dependent protein kinase. Bioscience Reports, 19(2), 109–114. doi:10.1023/A:1020110510609