Phosphorylation of H,K-ATPase α-subunit in microsomes from rabbit gastric mucosa by cAMP-dependent protein kinase
Public Deposited- Resource Type
- Creator
- Abstract
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.
- Language
- Publisher
- Identifier
- Citation
- 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
- Date Created
- 1999-07-27
Relations
- In Collection:
Items
| Thumbnail | Title | Date Uploaded | Visibility | Actions |
|---|---|---|---|---|
|
|
109.full.pdf | 2022-08-26 | Public | Download |