Eosin fluorescence changes during Rb+ occlusion in the Na +/K+-ATPase

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We used suspensions of partially purified Na+/K +-ATPase from pig kidney to compare the effects of Rb+, as a K+ congener, on the time course and on the equilibrium values of eosin fluorescence and of Rb+ occlusion. Both sets of data were collected under identical conditions in the same enzyme prepar...

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Autor principal: Montes, M.R
Otros Autores: González-Lebrero, R.M, Garrahan, P.J, Rossi, R.C
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 2006
Acceso en línea:Registro en Scopus
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Biblioteca Central Dr. Luis F. Leloir (FCEN) de Universidad de Buenos Aires
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024 7 |2 scopus  |a 2-s2.0-33751079883 
024 7 |2 cas  |a eosin, 17372-87-1, 51395-88-1, 548-26-5; rubidium 86, 14932-53-7; Eosine Yellowish-(YS), 17372-87-1; Na(+)-K(+)-Exchanging ATPase, EC 3.6.1.37; Rubidium, 7440-17-7 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a BICHA 
100 1 |a Montes, M.R. 
245 1 0 |a Eosin fluorescence changes during Rb+ occlusion in the Na +/K+-ATPase 
260 |c 2006 
270 1 0 |m Rossi, R.C.; Instituto de Química y Fisicoquímica Biológicas, Departamento de Química Biológica, Universidad de Buenos Aires, Junín 956, C1113AAD Buenos Aires, Argentina; email: rcr@mail.retina.ar 
506 |2 openaire  |e Política editorial 
504 |a Skou, J.C., Esmann, M., The Na, K.-ATPase (1992) J. Bioenerg. Biomembr., 24, pp. 249-281 
504 |a 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 throuah the direct route (2002) J. Biol. Chem., 277, pp. 5910-5921 
504 |a Jørgensen, P.L., Petersen, J., High-affinity 86Rb-binding and structural changes in the alpha-subunil of Na+.K+-ATPase as detected by tryplic digestion and fluorescence analysis (1982) Biochim. Biophys. Acta, 705, pp. 38-47 
504 |a Glynn, I.M., Hara, Y., Richards, D.E., Steinberg, M., Comparison of rates of cation release and of conformational change in dog kidney Na.K-ATPase (1987) J. Physiol., 383, pp. 477-485 
504 |a Esmann, M., Influence of Na+ on conformational states in membrane-bound renal Na, K-ATPase (1994) Biochemistry, 33, pp. 8558-8565 
504 |a Rossi, R.C., Kaufman, S.B., González-Lebrero, R.M., Nørby, J.G., Garrahan, P.J., An attachment for non-destructive, fast quenching of samples in rapid mixing experiments (1999) Anal. Biochem., 270, pp. 276-285 
504 |a Skou, J.C., Esmann, M., Effect of magnesium ions on the high-affinity binding of eosin to the (Na+ + K+)-ATPase (1983) Biochim. Biophys. Acta, 727, pp. 101-107 
504 |a Montes, M.R., González-Lebrero, R.M., Garrahan, P.J., Rossi, R.C., The interaction between the fluorescent probe eosin and the Na +/K+-ATPase studied through Rb+ occlusion (2004) Biochemistry, 43, pp. 2062-2069 
504 |a Jensen, J., Nerby, J.G., Ottolenghi, P., Binding of sodium and potassium to the sodium pump of pig kidney evaluated from nucleotide-binding behaviour (1984) J. Physiol. (Lond.), 346, pp. 219-241 
504 |a Lin, S., Faller, L.D., Ionic-strength dependence of the conformational change in the unphosphorylated sodium pump (2005) Biochemistry, 44, pp. 1482-1494 
504 |a Nerby, J.G., Esmann, M., The effect of ionic strength and specific anions on substrate binding and hydrolytic activities of Na, K.-ATPase (1997) J. Gen. Physiol., 109, pp. 555-570 
504 |a Skou, J.C., Esmann, M., The effects of Na+ and K+ on the conformational transitions of (Na+ + K+)-ATPase (1983) Biochim. Biophys. Acta, 746, pp. 101-113 
504 |a Bumham, K.P., Anderson, D.R., (2002) Model Selection and Multimodel Inference, 2nd Ed., pp. 60-85. , Springer, New York 
504 |a Smirnova, I.N., Faller, L.D., Mechanism of the conformational change in sodium pump reported by eosin (1995) Biochemistry, 34, pp. 13159-13169 
504 |a Fedosova, N.U., Esmann, M., Nucleotide-binding kinetics of Na, K-ATPase: Cation dependence (2004) Biochemistry, 43, pp. 4212-4218 
504 |a 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 (2006) J. Biol. Chem., 281, pp. 15721-15726 
504 |a Rossi, R.C., González-Lebrero, R.M., Kaufman, S.B., Garrahan, P.J., Testing K+-like occlusion of cations in the Na +/K+-ATPase (2005) J. Gen. Physiol., 126, pp. 29a 
520 3 |a We used suspensions of partially purified Na+/K +-ATPase from pig kidney to compare the effects of Rb+, as a K+ congener, on the time course and on the equilibrium values of eosin fluorescence and of Rb+ occlusion. Both sets of data were collected under identical conditions in the same enzyme preparations. The incubation media lacked ATP so that all changes led to an equilibrium distribution between enzyme conformers with and without bound eosin and with and without bound or occluded Rb+. Results showed that as Rb+ concentration was increased, the equilibrium value of fluorescence decreased and occlusion increased along rectangular hyperbolas with similar half-maximal values. The time courses of attainment of equilibrium showed an initial phase which was so quick as to fall below the time resolution of our rapid-mixing apparatus. This phase was followed by the sum of at least two exponential functions of time. In the case of fluorescence the fast exponential term accounted for a larger fraction of the time course than in the case of occlusion. Comparison between experimental and simulated results suggests that fluorescence changes express a process that is coupled to Rb+ occlusion but that is completed before occlusion reaches equilibrium. © 2006 American Chemical Society.  |l eng 
593 |a Instituto de Química y Fisicoquímica Biológicas, Departamento de Química Biológica, Universidad de Buenos Aires, Junín 956, C1113AAD Buenos Aires, Argentina 
690 1 0 |a ADENOSINETRIPHOSPHATE 
690 1 0 |a DATA STRUCTURES 
690 1 0 |a FLUORESCENCE 
690 1 0 |a POSITIVE IONS 
690 1 0 |a RUBIDIUM 
690 1 0 |a SODIUM 
690 1 0 |a SUSPENSIONS (FLUIDS) 
690 1 0 |a CONGENERS 
690 1 0 |a EOSIN FLUORESCENCE 
690 1 0 |a HYPERBOLAS 
690 1 0 |a OCCLUSIONS 
690 1 0 |a ENZYMES 
690 1 0 |a ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM) 
690 1 0 |a EOSIN 
690 1 0 |a RUBIDIUM 86 
690 1 0 |a ARTICLE 
690 1 0 |a ENZYME ACTIVITY 
690 1 0 |a ENZYME KINETICS 
690 1 0 |a ENZYME PURIFICATION 
690 1 0 |a FLUORESCENCE 
690 1 0 |a KIDNEY 
690 1 0 |a NONHUMAN 
690 1 0 |a PRIORITY JOURNAL 
690 1 0 |a SWINE 
690 1 0 |a ALGORITHMS 
690 1 0 |a ANIMALS 
690 1 0 |a EOSINE YELLOWISH-(YS) 
690 1 0 |a FLUORESCENCE 
690 1 0 |a ION TRANSPORT 
690 1 0 |a KINETICS 
690 1 0 |a MODELS, CHEMICAL 
690 1 0 |a NA(+)-K(+)-EXCHANGING ATPASE 
690 1 0 |a PROTEIN BINDING 
690 1 0 |a RUBIDIUM 
690 1 0 |a SWINE 
690 1 0 |a SUS SCROFA 
700 1 |a González-Lebrero, R.M. 
700 1 |a Garrahan, P.J. 
700 1 |a Rossi, R.C. 
773 0 |d 2006  |g v. 45  |h pp. 13093-13100  |k n. 43  |p Biochemistry  |x 00062960  |w (AR-BaUEN)CENRE-755  |t Biochemistry 
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856 4 0 |u https://doi.org/10.1021/bi060778i  |y DOI 
856 4 0 |u https://hdl.handle.net/20.500.12110/paper_00062960_v45_n43_p13093_Montes  |y Handle 
856 4 0 |u https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00062960_v45_n43_p13093_Montes  |y Registro en la Biblioteca Digital 
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963 |a VARI 
999 |c 82685 

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