[The effect of the phosphorylation of the Na+,K(+)-ATPase alpha subunit in rat kidneys by protein kinase C on the activity of the enzyme].
Phosphorylation was shown to lead to a change in the conformational equilibrium toward E1 form associated with a decrease in apparent affinity for the K+ in alpha-1 subunit of the rat kidney Na+, K(+)-ATPase. Rate of transition from E2 to E1 was apparently unaffected by phosphorylation. ATP hydrolysis by the protein kinase C-phosphorylated Na+, K(+)-ATPase shows a decrease in the Vmax and Km for K+.
Logvinenko
N S
NS
Institute of Cytology and Genetics, Russian Acad. Sci., Siberian Branch, Novosibirsk, Russia.
Averia
A
A
Ivanova
L N
LN
D000818:Animals; D006868:Hydrolysis; D066298:In Vitro Techniques; D007668:Kidney / Q000201:enzymology*; D010766:Phosphorylation; D011493:Protein Kinase C / Q000378:metabolism*; D051381:Rats; D000254:Sodium-Potassium-Exchanging ATPase / Q000302:isolation & purification / Q000378:metabolism*; D013050:Spectrometry, Fluorescence / Q000706:statistics & numerical data; D014882:Water-Electrolyte Balance / Q000502:physiology
D011493:Protein Kinase C; D000254:Sodium-Potassium-Exchanging ATPase