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Abstract:

We used partially purified Na+/K+-ATPase from pig kidney to study dephosphorylation, occlusion, and ATPase activity in the same enzyme preparation and in media of identical composition containing 10 μM ATP and different concentrations of Rb+, used as a K+ congener. The experiments were performed using a rapid-mixing apparatus with a time resolution of 3.5 ms. The main findings were as follows. (i) At sufficiently low Rb+ concentration the initial rate of dephosphorylation was higher than that of occlusion, (ii) as [Rb+] tended to zero the slope of the time course of occlusion but not that of the time course of dephosphorylation approached zero and, (iii) as Rb+ concentration increased, ATPase activity first increased and, after passing through a maximum, tended to a value that was lower than that observed in media without Rb+. None of these results is compatible with the currently held idea that binding of a single Rb+ to the E2P conformer of the ATPase does not modify the rate of dephosphorylation and strongly suggest that a single Rb+ does promote dephosphorylation through a mechanism that is not stoichiometrically coupled to Rb+ occlusion. If this mechanism is included in the currently accepted scheme for ATP hydrolysis by the Na+/K+-ATPase, a reasonable prediction of the experimental results is obtained. © 2006 by The American Society for Biochemistry and Molecular Biology, Inc.

Registro:

Documento: Artículo
Título:Binding of a single Rb+ increases Na+/K +-ATPase, activating dephosphorylation without stoichiometric occlusion
Autor:Kaufman, S.B.; González-Lebrero, R.M.; Rossi, R.C.; Garrahan, P.J.
Filiación:Instituto de Química Y Fisicoquímica Biológicas, Departamento de Química Biológica, Universidad de Buenos Aires, Junín 956, C1113AAD Buenos Aires, Argentina
Palabras clave:Adenosinetriphosphate; Biochemistry; Biological organs; Hydrolysis; Rubidium; Sodium; Stoichiometry; ATP hydrolysis; ATPase; Dephosphorylation; Stoichiometric occlusion; Enzyme kinetics; adenosine triphosphatase; adenosine triphosphatase (potassium sodium); rubidium ion; animal tissue; article; binding affinity; controlled study; enzyme activity; hydrolysis; nonhuman; occlusion; priority journal; protein dephosphorylation; steady state; stoichiometry; swine; Animals; Kidney; Kinetics; Na(+)-K(+)-Exchanging ATPase; Phosphorylation; Protein Binding; Rubidium; Swine; Sus scrofa
Año:2006
Volumen:281
Número:23
Página de inicio:15721
Página de fin:15726
DOI: http://dx.doi.org/10.1074/jbc.M600953200
Título revista:Journal of Biological Chemistry
Título revista abreviado:J. Biol. Chem.
ISSN:00219258
CODEN:JBCHA
CAS:adenosine triphosphatase, 37289-25-1, 9000-83-3; rubidium ion, 22537-38-8; Na(+)-K(+)-Exchanging ATPase, EC 3.6.1.37; Rubidium, 7440-17-7
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00219258_v281_n23_p15721_Kaufman

Referencias:

  • Skou, J.C., Esmann, M., (1992) J. Bioenerg. Biomembr., 24, pp. 249-281
  • Glynn, I.M., Karlish, S.J.D., (1990) Annu. Rev. Biochem., 59, pp. 171-205
  • Beaugé, L.A., Glynn, I.M., (1979) Nature, 280, pp. 510-512
  • Rossi, R.C., Nørby, J.G., (1993) J. Biol. Chem., 268, pp. 12579-12590
  • Kaufman, S.B., González-Lebrero, R.M., Schwarzbaum, P.J., Nørby, J.G., Garrahan, P.J., Rossi, R.C., (1999) J. Biol. Chem., 274, pp. 20779-20790
  • Kaufman, S.B., González-Lebrero, R.M., Garrahan, P.J., Rossi, R.C., (2003) Ann. New York Acad. Sci., 986, pp. 155-158
  • Jensen, J., Nørby, J.G., Ottolenghi, P., (1984) J. Physiol. (Lond.), 346, pp. 219-241
  • Schwarzbaum, P.J., Kaufman, S.B., Rossi, R.C., Garrahan, P.J., (1995) Biochim. Biophys. Acta, 1233, pp. 33-40
  • Rossi, R.C., Kaufman, S.B., González-Lebrero, R.M., Nørby, J.G., Garrahan, P.J., (1999) Anal. Biochem., 270, pp. 276-285
  • Glynn, I.M., Chappell, J.B., (1964) Biochem. J., 90, pp. 147-149
  • Rossi, R.C., Garrahan, P.J., (1989) Biochim. Biophys. Acta, 981, pp. 105-114
  • Post, R.L., Hegyvary, C., Kume, S., (1972) J. Biol. Chem., 247, pp. 6530-6540
  • Blostein, R., Whittington, E.S., (1973) J. Biol. Chem., 248, pp. 1772-1777
  • Vilsen, B., (1999) Biochemistry, 38, pp. 11389-11400
  • Forbush III, B., (1988) J. Biol. Chem., 265, pp. 7961-7969
  • Heyse, S., Wuddel, I., Apell, H.J., Stürmer, W., (1994) J. Gen. Physiol., 104, pp. 197-240
  • González-Lebrero, R.M., Kaufman, S.B., Montes, M.R., Nørby, J.G., Garrahan, P.J., Rossi, R.C., (2002) J. Biol. Chem., 277, pp. 5910-5921
  • Beaugé, L.A., Glynn, I.M., Richards, D.E., (1979) J. Physiol. (Lond.), 295, pp. 88P
  • Garrahan, P.J., Glynn, I.M., (1967) J. Physiol. (Lond), 192, pp. 217-235

Citas:

---------- APA ----------
Kaufman, S.B., González-Lebrero, R.M., Rossi, R.C. & Garrahan, P.J. (2006) . Binding of a single Rb+ increases Na+/K +-ATPase, activating dephosphorylation without stoichiometric occlusion. Journal of Biological Chemistry, 281(23), 15721-15726.
http://dx.doi.org/10.1074/jbc.M600953200
---------- CHICAGO ----------
Kaufman, S.B., González-Lebrero, R.M., Rossi, R.C., Garrahan, P.J. "Binding of a single Rb+ increases Na+/K +-ATPase, activating dephosphorylation without stoichiometric occlusion" . Journal of Biological Chemistry 281, no. 23 (2006) : 15721-15726.
http://dx.doi.org/10.1074/jbc.M600953200
---------- MLA ----------
Kaufman, S.B., González-Lebrero, R.M., Rossi, R.C., Garrahan, P.J. "Binding of a single Rb+ increases Na+/K +-ATPase, activating dephosphorylation without stoichiometric occlusion" . Journal of Biological Chemistry, vol. 281, no. 23, 2006, pp. 15721-15726.
http://dx.doi.org/10.1074/jbc.M600953200
---------- VANCOUVER ----------
Kaufman, S.B., González-Lebrero, R.M., Rossi, R.C., Garrahan, P.J. Binding of a single Rb+ increases Na+/K +-ATPase, activating dephosphorylation without stoichiometric occlusion. J. Biol. Chem. 2006;281(23):15721-15726.
http://dx.doi.org/10.1074/jbc.M600953200