Abstract:
:Reconstituted Na+,K+-ATPase from either pig kidney or shark rectal glands was phosphorylated by cAMP dependent protein kinase, PKA. The stoichiometry was approximately 0.9 mol P(i)/mol alpha-subunit in the pig kidney enzyme and approximately 0.2 mol P(i)/mol alpha-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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Cornelius F,Logvinenko Ndoi
10.1016/0014-5793(96)00032-4subject
Has Abstractpub_date
1996-02-19 00:00:00pages
277-80issue
3eissn
0014-5793issn
1873-3468pii
0014-5793(96)00032-4journal_volume
380pub_type
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