Navegar

Colección

Datos Estadísticas

Artículo

Estamos trabajando para incorporar este artículo al repositorio
Consulte el artículo en la página del editor
Consulte la política de Acceso Abierto del editor

Abstract:

Occlusion of K+ or its congeners in the Na+/K+-ATPase occurs after K+-dependent dephosphorylation (physiological route) or in media lacking ATP and Na+ (direct route). The effects of Pi or ATP on the kinetics of deocclusion of the K+-congener Rb+ formed by each of the above mentioned routes was independent of the route of occlusion, which suggests that both routes lead to the same enzyme intermediate. The time course of occlusion via the direct route can be described by the sum of two exponential functions plus a small component of very high velocity. At equilibrium, occluded Rb+ is a hyperbolic function of free [Rb+] suggesting that the direct route results in enzyme states holding either one or two occluded Rb+. Release of occluded Rb+ follows the sum of two decreasing exponential functions of time, corresponding to two phases with similar sizes. These phases are not caused by independent physical compartments. The rate constant of one of the phases is reduced up to 30 times by free Rb+. When Rb+ is the only pump ligand, the kinetics of occlusion and deocclusion through the direct route are consistent with an ordered-sequential process with additional independent step(s) interposed between the uptake or the release of each occluded Rb+.

Registro:

Documento: Artículo
Título:The occlusion of Rb+ in the Na+/K+-ATPase. I. The identity of occluded states formed by the physiological or the direct routes: Occlusion/deocclusion kinetics through the direct route
Autor:González-Lebrero, R.M.; Kaufman, S.B.; Montes, M.R.; Nørby, J.G.; Garrahan, P.J.; Rossi, R.C.
Filiación:Instituto de Química y Fisicoquímica Biológicas, Departamento de Química Biológica, Universidad de Buenos Aires, Junín 956, 1113 Buenos Aires, Argentina
Institute of Biophysics, University of Aarhus, Ole Worms Allé 185, DK-8000 Aarhus, Denmark
Palabras clave:Physiology; Positive ions; Potassium; Rate constants; Rubidium; Sodium; Congeners; Enzymes; adenosine triphosphatase (potassium sodium); adenosine triphosphate; phosphate; potassium ion; rubidium ion; sodium ion; active transport; article; dephosphorylation; enzyme analysis; hydrolysis; nonhuman; priority journal; swine; Adenosine Triphosphate; Animals; Kidney; Kinetics; Models, Theoretical; Na(+)-K(+)-Exchanging ATPase; Phosphates; Regression Analysis; Rubidium; Swine; Sus scrofa
Año:2002
Volumen:277
Número:8
Página de inicio:5910
Página de fin:5921
DOI: http://dx.doi.org/10.1074/jbc.M105886200
Título revista:Journal of Biological Chemistry
Título revista abreviado:J. Biol. Chem.
ISSN:00219258
CODEN:JBCHA
CAS:Adenosine Triphosphate, 56-65-5; Na(+)-K(+)-Exchanging ATPase, EC 3.6.1.37; Phosphates; Rubidium, 7440-17-7
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00219258_v277_n8_p5910_GonzalezLebrero

Referencias:

  • Post, R.L., Hegyvary, C., Kume, S., (1972) J. Biol. Chem., 247, pp. 6530-6540
  • Beaugé, L.A., Glynn, I.M., (1979) Nature, 280, pp. 510-512
  • Forbush B. III, (1987) J. Biol. Chem., 262, pp. 11104-11115
  • Kaufman, S.B., González-Lebrero, R.M., Schwarzbaum, P.J., Norby, J.G., Garrahan, P.J., Rossi, R.C., (1999) J. Biol. Chem., 274, pp. 20779-20790
  • Rossi, R.C., Nørby, J.G., (1993) J. Biol. Chem., 268, pp. 12579-12590
  • Glynn, I.M., Richards, D.E., (1982) J. Physiol. (Lond.), 330, pp. 17-43
  • Glynn, I.M., Karlish, S.J.D., (1990) Annu. Rev. Biochem., 59, pp. 171-205
  • Karlish, S.J.D., Yates, D.W., (1978) Biochim. Biophys. Acta, 527, pp. 115-130
  • Joergensen, P.L., (1975) Biochim. Biophys. Acta, 401, pp. 399-415
  • Karlish, S.J.D., Stein, W.D., (1982) J. Physiol., 328, pp. 295-316
  • González-Lebrero, R.M., Kaufman, S.B., Garrahan, P.J., Rossi, R.C., (2002) J. Biol. Chem., 277, pp. 5922-5928
  • Garrahan, P.J., Glynn, I.M., (1967) J. Physiol. (Lond.), 192, pp. 217-235
  • Rossi, R.C., Kaufman, S.B., González-Lebrero, R.M., Nørby, J.G., Garrahan, P.J., (1999) Anal. Biochem., 270, pp. 276-285
  • González-Lebrero, R.M., Kaufman, S.B., Nørby, J.G., Garrahan, P.J., Rossi, R.C., (2000) Excerpta Med. Int. Congr. Ser., 120, pp. 433-436
  • Jensen, J., Nørby, J.G., Ottolenghi, P., (1984) J. Physiol. (Lond.), 346, pp. 219-241
  • Glynn, I.M., Chappell, J.B., (1964) Biochem. J., 90, pp. 147-149
  • Schwarzbaum, P.J., Kaufman, S.B., Rossi, R.C., Garrahan, P.J., (1995) Biochim. Biophys. Acta, 1233, pp. 33-40
  • Yamaoka, K., Nakagawa, T., Uno, T., (1978) J. Pharmacokin. Biopharm., 6, pp. 165-175
  • González-Lebrero, R.M., (2001) Caracterización cinética del fenómeno de oclusión de K+ en la Na+/K+-ATPasa, , Ph.D. thesis, University of Buenos Aires
  • Fraser, R.D.B., Suzuki, E., (1973) Physical Principles and Techniques of Protein Chemistry: Part C, pp. 301-355. , (Leach, S. J., ed), Academic Press, New York
  • Forbush B. III, (1988) The Na+,K+-Pump. Part A, Molecular Aspects, pp. 229-248. , (Skou, J. C., Norby J. G, Maunsbach, A. B., and Esmann M., eds), Alan Liss, Inc., New York
  • Post, R.L., Taniguchi, K., Toda, G., (1974) Ann. N. Y. Acad. Sci., 242, pp. 80-91
  • Shani, M., Goldschleger, R., Karlish, S.J.D., (1987) Biochim. Biophys. Acta, 904, pp. 13-21
  • Jensen, J., Nørby, J.G., (1989) Biochim. Biophys. Acta, 985, pp. 248-254
  • Esmann, M., (1994) Biochemistry, 33, pp. 8558-8565
  • Pedemonte, C.H., Beaugé, L.A., (1983) Biochim. Biophys. Acta, 748, pp. 245-253
  • Sachs, J.R., (1988) J. Physiol. (Lond.), 400, pp. 545-574
  • Forbush B. III, (1987) J. Biol. Chem., 262, pp. 11116-11127
  • Glynn, I.M., Howland, J.L., Richards, D.E., (1985) J. Physiol., 368, pp. 453-469
  • Hasenauer, J., Huang, W.-H., Askari, A., (1993) J. Biol. Chem., 268, pp. 3289-3297

Citas:

---------- APA ----------
González-Lebrero, R.M., Kaufman, S.B., Montes, M.R., Nørby, J.G., Garrahan, P.J. & Rossi, R.C. (2002) . The occlusion of Rb+ in the Na+/K+-ATPase. I. The identity of occluded states formed by the physiological or the direct routes: Occlusion/deocclusion kinetics through the direct route. Journal of Biological Chemistry, 277(8), 5910-5921.
http://dx.doi.org/10.1074/jbc.M105886200
---------- CHICAGO ----------
González-Lebrero, R.M., Kaufman, S.B., Montes, M.R., Nørby, J.G., Garrahan, P.J., Rossi, R.C. "The occlusion of Rb+ in the Na+/K+-ATPase. I. The identity of occluded states formed by the physiological or the direct routes: Occlusion/deocclusion kinetics through the direct route" . Journal of Biological Chemistry 277, no. 8 (2002) : 5910-5921.
http://dx.doi.org/10.1074/jbc.M105886200
---------- MLA ----------
González-Lebrero, R.M., Kaufman, S.B., Montes, M.R., Nørby, J.G., Garrahan, P.J., Rossi, R.C. "The occlusion of Rb+ in the Na+/K+-ATPase. I. The identity of occluded states formed by the physiological or the direct routes: Occlusion/deocclusion kinetics through the direct route" . Journal of Biological Chemistry, vol. 277, no. 8, 2002, pp. 5910-5921.
http://dx.doi.org/10.1074/jbc.M105886200
---------- VANCOUVER ----------
González-Lebrero, R.M., Kaufman, S.B., Montes, M.R., Nørby, J.G., Garrahan, P.J., Rossi, R.C. The occlusion of Rb+ in the Na+/K+-ATPase. I. The identity of occluded states formed by the physiological or the direct routes: Occlusion/deocclusion kinetics through the direct route. J. Biol. Chem. 2002;277(8):5910-5921.
http://dx.doi.org/10.1074/jbc.M105886200