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Journal Abstract Search

262 related items for PubMed ID: 6261818

  • 1. The steady-state kinetic mechanism of ATP hydrolysis catalyzed by membrane-bound (Na+ + K+)-ATPase from ox brain. III. A minimal model.
    Plesner IW, Plesner L, Nørby JG, Klodos I.
    Biochim Biophys Acta; 1981 May 06; 643(2):483-94. PubMed ID: 6261818
    [Abstract] [Full Text] [Related]

  • 2. The steady-state kinetic mechanism of ATP hydrolysis catalyzed by membrane-bound (Na+ + K+)-ATPase from ox brain.
    Plesner IW, Plesner L.
    Biochim Biophys Acta; 1981 Nov 06; 648(2):231-46. PubMed ID: 6272852
    [Abstract] [Full Text] [Related]

  • 3. The steady-state kinetic mechanism of ATP hydrolysis catalyzed by membrane-bound (Na+ + K+)-ATPase from ox brain. I. Substrate identity.
    Plesner L, Plesner IW.
    Biochim Biophys Acta; 1981 May 06; 643(2):449-62. PubMed ID: 6261816
    [Abstract] [Full Text] [Related]

  • 4. The steady-state kinetic mechanism of ATP hydrolysis catalyzed by membrane-bound (Na+ + K+)-ATPase from ox brain. II. Kinetic characterization of phosphointermediates.
    Klodos I, Nørby JG, Plesner IW.
    Biochim Biophys Acta; 1981 May 06; 643(2):463-82. PubMed ID: 6261817
    [Abstract] [Full Text] [Related]

  • 5. Distinction between the intermediates in Na+-ATPase and Na+,K+-ATPase reactions. II. Exchange and hydrolysis kinetics at micromolar nucleotide concentrations.
    Plesner L, Plesner IW.
    Biochim Biophys Acta; 1988 Jan 13; 937(1):63-72. PubMed ID: 2825809
    [Abstract] [Full Text] [Related]

  • 6. Distinction between the intermediates in Na+-ATPase and Na+,K+-ATPase reactions. I. Exchange and hydrolysis kinetics at millimolar nucleotide concentrations.
    Plesner L, Plesner IW.
    Biochim Biophys Acta; 1988 Jan 13; 937(1):51-62. PubMed ID: 2825808
    [Abstract] [Full Text] [Related]

  • 7. (Na+ + K+)-ATPase: confirmation of the three-pool model for the phosphointermediates of Na+-ATPase activity. Estimation of the enzyme-ATP dissociation rate constant.
    Klodos I, Nørby JG.
    Biochim Biophys Acta; 1987 Feb 26; 897(2):302-14. PubMed ID: 3028481
    [Abstract] [Full Text] [Related]

  • 8. Kinetics of (Na+ + K+)-ATPase: analysis of the influence of Na+ and K+ by steady-state kinetics.
    Plesner IW, Plesner L.
    Biochim Biophys Acta; 1985 Aug 27; 818(2):235-50. PubMed ID: 2992590
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  • 9. Kinetic studies on the ADP-ATP exchange reaction catalyzed by Na+, K+-dependent ATPase. Evidence for the K.S.T. mechanism with two enzyme-ATP complexes and two phosphorylated intermediates of high-energy type.
    Yamaguchi M, Tonomura Y.
    J Biochem; 1977 Jan 27; 81(1):249-60. PubMed ID: 14933
    [Abstract] [Full Text] [Related]

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  • 11. An unexpected effect of ATP on the ratio between activity and phosphoenzyme level of Na+/K(+)-ATPase in steady state.
    Schwarzbaum PJ, Kaufman SB, Rossi RC, Garrahan PJ.
    Biochim Biophys Acta; 1995 Jan 26; 1233(1):33-40. PubMed ID: 7833347
    [Abstract] [Full Text] [Related]

  • 12. Effects of ATP and monovalent cations on Mg2+ inhibition of (Na,K)-ATPase.
    Pedemonte CH, Beaugé L.
    Arch Biochem Biophys; 1986 Feb 01; 244(2):596-606. PubMed ID: 3004346
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  • 15. [32P]ATP synthesis in steady state from [32P]Pi and ADP by Na+/K(+)-ATPase from ox brain and pig kidney. Activation by K+.
    Plesner L, Karlsmose B, Lüscher ME.
    Biochim Biophys Acta; 1990 Sep 03; 1040(2):167-74. PubMed ID: 2169305
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  • 17. Inactivation of (Na+ + K+)-ATPase by chromium(III) complexes of nucleotide triphosphates.
    Pauls H, Bredenbröcker B, Schoner W.
    Eur J Biochem; 1980 Aug 03; 109(2):523-33. PubMed ID: 6250846
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  • 19. Identification of potential regulatory sites of the Na+,K+-ATPase by kinetic analysis.
    Kong BY, Clarke RJ.
    Biochemistry; 2004 Mar 02; 43(8):2241-50. PubMed ID: 14979720
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