Functional regulation of reconstituted Na,K-ATPase by protein kinase A phosphorylation.

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 Lett

journal_title

FEBS letters

authors

Cornelius F,Logvinenko N

doi

10.1016/0014-5793(96)00032-4

subject

Has Abstract

pub_date

1996-02-19 00:00:00

pages

277-80

issue

3

eissn

0014-5793

issn

1873-3468

pii

0014-5793(96)00032-4

journal_volume

380

pub_type

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