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.
Phosphorylation of H,K-ATPase α-Subunit in Microsomes from Rabbit Gastric Mucosa by cAMP-Dependent Protein Kinase
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Dilyara A. Murtazina, Sergei P. Petukhov, Kenneth B. Storey, Alexander M. Rubtsov, Olga D. Lopina; Phosphorylation of H,K-ATPase α-Subunit in Microsomes from Rabbit Gastric Mucosa by cAMP-Dependent Protein Kinase. Biosci Rep 1 April 1999; 19 (2): 109–114. doi: https://doi.org/10.1023/A:1020110510609
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