Functional regulation of reconstituted Na, K-ATPase by protein kinase A phosphorylation |
| |
Authors: | Flemming Cornelius Ninel Logvinenko |
| |
Institution: | aDepartment of Biophysics, University of Aarhus, DK-8000 Aarhus C, Denmark;bDepartment of Paediatrics, St. Göran's Cildren's Hospital, Karolinska Institutet, S-112 81 Lund, Sweden |
| |
Abstract: | Reconstituted Na+,K+-ATPase from either pig kidney or shark rectal glands was phosphorylated by cAMP dependent protein kinase, PKA. The stoichiometry was 0.9 mole Pi/mole -subunit in the pig kidney enzyme and 0.2 mol Pi/mol -subunit in the shark enzyme. In shark Na+,K+-ATPase PKA phosphorylation increased the maximum hydrolytic activity for cytoplasmic Na+ activation and extracellular K+ activation without affecting the apparent Km values. In contrast, no significant functional effect after PKA phosphorylation was observed in pig kidney Na+,K+-ATPase. |
| |
Keywords: | Protein kinase A (PKA) Regulation Na+ K+-ATPase Reconstitution Phosphorylation |
本文献已被 ScienceDirect 等数据库收录! |
|