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Functional regulation of reconstituted Na, K‐ATPase by protein kinase A phosphorylation
Author(s) -
Cornelius Flemming,
Logvinenko Ninel
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00032-4
Subject(s) - phosphorylation , chemistry , microbiology and biotechnology , protein kinase a , kinase , atpase , biochemistry , enzyme , biology
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 P i /mole α‐subunit in the pig kidney enzyme and ∼ 0.2 mol P i /mol α‐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 K m values. In contrast, no significant functional effect after PKA phosphorylation was observed in pig kidney Na + ,K + ‐ATPase.