Molecular Weights of Na^+, K^+-Dependent ATPase and K^+-Dependent Phosphatase
スポンサーリンク
概要
- 論文の詳細を見る
1. In guinea pig brain microsome preparations treated with 2 M sodium iodide, the target molecular weight of Na^+, K^+-ATPase (ATP phosphohydrolase E.C.3.6.1.3) and that of K^+-dependent phosphatase (orthophosphoric acid monoester phosphohydrolase E.C.3.1.3.1) were compared by the inactivation method using electron irradiation. The latter target size corresponded to 64% of the former one. 2. Although K^+-dependent phosphatase activity was stimulated in the coexistence of ATP and Na^+, the target size of K^+-dependent phosphatase was not enlarged in the both presences of ATP and Na^+. 3. These results suggest that Na^+, K^+-ATPase may consist of at least two main subunits, intermediate entity anti K^+-dependent phosphatase entity, and also suggest that action sites of ATP and N^+ stimulating K^+-dependent phosphatase activity may be the phosphatase entity of Na^+, K^+-ATPase.
- 近畿大学の論文
- 1976-12-28
著者
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Kaniike Kenichi
Department Of Physiology Kinki University School Of Medicine
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Miyamoto Hiroshi
Department Of Physiology Kinki University School Of Medicine
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Miyamoto Hiroshi
Department Of Anesthesiology Showa University Fujigaoka Hospital
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KUROGOCHI Yutaka
Department of Pharmacology, Nara Medical College
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Kurogochi Yutaka
Department Of Pharmacology Nara Medical College
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KANIIKE KENICHI
Department of Pharmacology, Osaka University Medical School
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KUROGOCHI YUTAKA
Department o f Pharmacology, Nara Medical College
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