Abstract:
:We have examined slow changes in the rate of ATP hydrolysis for purified dog kidney Na+ and K+ stimulated adenosine triphosphatase [(Na-K)ATPase] at various concentrations of free Mg2+, Mg-ATP, K+, and Na+. The effect of these ligands on the rate of ATP hydrolysis is explained by a rapid binding step determining the initial rate of turnover followed by a slow conformational change. Inactivation of enzyme stored in the presence of ethylenediaminetetraacetic acid occurs upon adding free Mg2+, Mg-ATP, and K+; reactivation may be achieved if the concentration of these ligands is reduced. Because of the slow conformational change, the affinities for ligands affecting inactivation are time dependent. A model is presented to explain the effects of free Mg2+ and Ma-ATP on (Na-K)ATPase activity.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Cantley LC Jr,Josephson Ldoi
10.1021/bi00669a013subject
Has Abstractpub_date
1976-11-30 00:00:00pages
5280-7issue
24eissn
0006-2960issn
1520-4995journal_volume
15pub_type
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