Interaction of Sodium and Potassium Ions with Na+,K+ ATpase. III. Cooperative Effect of ATP and Na+ on Complete Release of K+ from E2K

The effects of Na+ and ATP on the K+ binding to Na+,K+-ATPase were investigated by the centrifugation method with radioactive K+ in the absence of Mg2+ In the presence of 10 μM 43KCl 0.6 and 10 mM Na+ decreased the amount of bound K+ to one-half and zero, respectively. On the other hand, 10μM and 10...

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Published inJournal of biochemistry (Tokyo) Vol. 101; no. 3; pp. 789 - 793
Main Authors HOMAREDA, Haruo, NOZAKI, Tadashi, MATSUI, Hideo
Format Journal Article
LanguageEnglish
Published Oxford Oxford University Press 01.03.1987
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Summary:The effects of Na+ and ATP on the K+ binding to Na+,K+-ATPase were investigated by the centrifugation method with radioactive K+ in the absence of Mg2+ In the presence of 10 μM 43KCl 0.6 and 10 mM Na+ decreased the amount of bound K+ to one-half and zero, respectively. On the other hand, 10μM and 10 mM ATP decreased the amount of K+ to 60 and 25–40%, respectively. When the combined effect of ATP and Na+ was tested, 10 μM ATP decreased the Na+ concentration giving half-maximal inhibition of the K+ binding to one-third, showing synergistic inhibition by both ligands, though increase in ATP concentration seemed to depress the inhibitory effect of Na+. The synergistic inhibition by ATP and Na+ suggests that the release of K+ from E2K is not completed by the binding of ATP alone but is completed by the binding of Na+ in addition to ATP during the cycle of Na+,K+-dependent ATP-hydrolysis as well as ion-transport.
Bibliography:ark:/67375/HXZ-NM9KRPCG-5
istex:4F87A114C571AA2D2072B06BBBFAB69EE37376BC
ArticleID:101.3.789
1This study was supported in part by Grants-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan.
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SourceType-Scholarly Journals-1
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ISSN:0021-924X
1756-2651
DOI:10.1093/jb/101.3.789