메뉴 건너뛰기




Volumn 75, Issue 3, 1998, Pages 1340-1353

Kinetics of Na+-dependent conformational changes of rabbit kidney Na+, K+-ATPase

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); ADENOSINE TRIPHOSPHATE; FLUORESCENT DYE;

EID: 0031688516     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)74052-4     Document Type: Article
Times cited : (46)

References (64)
  • 1
    • 0000770960 scopus 로고
    • Biochemical aspects of active transport
    • Albers, R. W. 1967. Biochemical aspects of active transport. Annu. Rev. Biochem. 36:727-756.
    • (1967) Annu. Rev. Biochem. , vol.36 , pp. 727-756
    • Albers, R.W.1
  • 2
    • 0025321575 scopus 로고
    • Na, K-ATPase in artificial vesicles. Comparison of Na, K and Na-only pumping mode
    • Apell, H.-J., V. Häring, and M. Roudna. 1990. Na, K-ATPase in artificial vesicles. Comparison of Na, K and Na-only pumping mode. Biochim. Biophys. Acta. 1023:81-90.
    • (1990) Biochim. Biophys. Acta , vol.1023 , pp. 81-90
    • Apell, H.-J.1    Häring, V.2    Roudna, M.3
  • 3
    • 0029775234 scopus 로고    scopus 로고
    • Kinetics of the phosphorylation of Na, K-ATPase by inorganic phosphate detected by a fluorescence method
    • Apell, H.-J., M. Roudna, J. E. T. Corrie, and D. R. Trentham. 1996. Kinetics of the phosphorylation of Na, K-ATPase by inorganic phosphate detected by a fluorescence method. Biochemistry. 35: 10922-10930.
    • (1996) Biochemistry , vol.35 , pp. 10922-10930
    • Apell, H.-J.1    Roudna, M.2    Corrie, J.E.T.3    Trentham, D.R.4
  • 4
    • 0023853833 scopus 로고
    • +-ATPase after an ATP concentration jump: Dependence on sodium and ATP concentration
    • +-ATPase after an ATP concentration jump: dependence on sodium and ATP concentration. Biochim. Biophys. Acta. 939:197-206.
    • (1988) Biochim. Biophys. Acta , vol.939 , pp. 197-206
    • Borlinghaus, R.1    Apell, H.-J.2
  • 5
    • 0023216968 scopus 로고
    • Fast charge translocations associated with partial reactions of the Na, K-pump. I. Current and voltage transients after photochemical release of ATP
    • Borlinghaus, R., H.-J. Apell, and P. Läuger. 1987. Fast charge translocations associated with partial reactions of the Na, K-pump. I. Current and voltage transients after photochemical release of ATP. J. Membr. Biol. 97:161-178.
    • (1987) J. Membr. Biol. , vol.97 , pp. 161-178
    • Borlinghaus, R.1    Apell, H.-J.2    Läuger, P.3
  • 6
    • 0001768593 scopus 로고    scopus 로고
    • High-pressure stopped-flow spectrometer for kinetic studies of fast bioinorganic reactions by absorbance and fluorescence detection
    • K. Heremans, editor. Leuven University Press, Leuven, Belgium
    • Bugnon, P., M. Doludda, E. Grell, and A. E. Merbach. 1997. High-pressure stopped-flow spectrometer for kinetic studies of fast bioinorganic reactions by absorbance and fluorescence detection. In High Pressure Research in the Biosciences and Biotechnology. K. Heremans, editor. Leuven University Press, Leuven, Belgium. 143-146.
    • (1997) High Pressure Research in the Biosciences and Biotechnology , pp. 143-146
    • Bugnon, P.1    Doludda, M.2    Grell, E.3    Merbach, A.E.4
  • 7
    • 0028997221 scopus 로고
    • Sequential potassium binding at the extracellular side of the Na, K-pump
    • Bühler, R., and H.-J. Apell. 1995. Sequential potassium binding at the extracellular side of the Na, K-pump. J. Membr. Biol. 145:165-173.
    • (1995) J. Membr. Biol. , vol.145 , pp. 165-173
    • Bühler, R.1    Apell, H.-J.2
  • 8
    • 0025818726 scopus 로고
    • Charge translocation by the Na, K-pump. I. Kinetics of local field changes studied by time-resolved fluorescence measurements
    • Bühler, R., W. Stürmer, H.-J. Apell, and P. Läuger. 1991. Charge translocation by the Na, K-pump. I. Kinetics of local field changes studied by time-resolved fluorescence measurements. J. Membr. Biol. 121: 141-161.
    • (1991) J. Membr. Biol. , vol.121 , pp. 141-161
    • Bühler, R.1    Stürmer, W.2    Apell, H.-J.3    Läuger, P.4
  • 11
    • 0025978278 scopus 로고
    • Functional reconsitution of the sodium pump. Kinetics of exchange reactions
    • Cornelius, F. 1991. Functional reconsitution of the sodium pump. Kinetics of exchange reactions. Biochim. Biophys. Acta. 1071:19-66.
    • (1991) Biochim. Biophys. Acta , vol.1071 , pp. 19-66
    • Cornelius, F.1
  • 13
    • 0000413288 scopus 로고
    • The development and application of photosensitive caged compounds to aid time-resolved structure determinations of macromolecules
    • Corrie, J. E. T., Y. Katayama, G. P. Reid, M. Anson, and D. R. Trentham. 1992. The development and application of photosensitive caged compounds to aid time-resolved structure determinations of macromolecules. Philos. Trans. R. Soc. Lond. A. 340:233-244.
    • (1992) Philos. Trans. R. Soc. Lond. A , vol.340 , pp. 233-244
    • Corrie, J.E.T.1    Katayama, Y.2    Reid, G.P.3    Anson, M.4    Trentham, D.R.5
  • 15
    • 0031282997 scopus 로고    scopus 로고
    • 2P phosphoforms of Na,K-ATPase
    • Na/K-ATPase and related transport ATPases. Structure, mechanism and regulation. L. A. Beaugé, D. C. Gadsby, and P. J. Garrahan, editors
    • 2P phosphoforms of Na,K-ATPase. In Na/K-ATPase and related transport ATPases. Structure, mechanism and regulation. L. A. Beaugé, D. C. Gadsby, and P. J. Garrahan, editors. Ann. N.Y. Acad. Sci. 834:386-389.
    • (1997) Ann. N.Y. Acad. Sci. , vol.834 , pp. 386-389
    • Fedosova, N.U.1    Cornelius, F.2    Forbush B. III3    Klodos, I.4
  • 16
    • 0029598780 scopus 로고
    • Fluorescent styryl dyes as probes for Na, K-ATPase reaction mechanism: Significance of the charge of the hydrophobic moiety of RH dyes
    • Fedosova, N. U., F. Cornelius, and I. Klodos. 1995. Fluorescent styryl dyes as probes for Na, K-ATPase reaction mechanism: significance of the charge of the hydrophobic moiety of RH dyes. Biochemistry. 34: 16806-16814.
    • (1995) Biochemistry , vol.34 , pp. 16806-16814
    • Fedosova, N.U.1    Cornelius, F.2    Klodos, I.3
  • 19
  • 20
    • 0021127472 scopus 로고
    • + movement in a single turnover of the Na pump
    • + movement in a single turnover of the Na pump. Proc. Natl. Acad. Sci. USA. 81:5310-5314.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 5310-5314
    • Forbush B. III1
  • 21
    • 0023655684 scopus 로고
    • 86Rb from an occluded state of the Na,K-pump in the presence of ATP or ADP
    • 86Rb from an occluded state of the Na,K-pump in the presence of ATP or ADP. J. Biol. Chem. 262:11104-11115.
    • (1987) J. Biol. Chem. , vol.262 , pp. 11104-11115
    • Forbush B. III1
  • 22
    • 0025743067 scopus 로고
    • Rate-limiting steps in Na translocation by the Na/K pump
    • J. H. Kaplan and P. DeWeer, editors. Rockefeller University Press, New York
    • Forbush, B., III, and I. Klodos. 1991. Rate-limiting steps in Na translocation by the Na/K pump. In The Sodium Pump: Structure, Mechanism, and Regulation. J. H. Kaplan and P. DeWeer, editors. Rockefeller University Press, New York. 211-225.
    • (1991) The Sodium Pump: Structure, Mechanism, and Regulation , pp. 211-225
    • Forbush B. III1    Klodos, I.2
  • 24
    • 0029913538 scopus 로고    scopus 로고
    • +-ATPase pump currents in giant excised patches activated by an ATP concentration jump
    • +-ATPase pump currents in giant excised patches activated by an ATP concentration jump. Biophys. J. 71:2486-2500.
    • (1996) Biophys. J. , vol.71 , pp. 2486-2500
    • Friedrich, T.1    Bamberg, E.2    Nagel, G.3
  • 25
    • 0030918526 scopus 로고    scopus 로고
    • +-ATPase pump currents activated by ATP concentration or voltage jumps
    • +-ATPase pump currents activated by ATP concentration or voltage jumps. Biophys. J. 73:186-194.
    • (1997) Biophys. J. , vol.73 , pp. 186-194
    • Friedrich, T.1    Nagel, G.2
  • 27
    • 0002591052 scopus 로고
    • +-transporting adenosine triphosphatase
    • A. N. Martonosi, editor. Plenum Press, New York
    • +-transporting adenosine triphosphatase. In The Enzymes of Biological Membranes, Vol. 3, 2nd Ed. A. N. Martonosi, editor. Plenum Press, New York. 34-114.
    • (1985) The Enzymes of Biological Membranes, Vol. 3, 2nd Ed. , vol.3 , pp. 34-114
    • Glynn, I.M.1
  • 28
    • 0002597645 scopus 로고
    • +-ATPase as detected by fluorescence spectroscopy and characterized by equilibrium binding studies
    • E. Bamberg and W. Schoner, editors. Steinkopff Verlag, Darmstadt, Germany
    • +-ATPase as detected by fluorescence spectroscopy and characterized by equilibrium binding studies. In The Sodium Pump: Structure Mechanism, Hormonal Control and Its Role in Disease. E. Bamberg and W. Schoner, editors. Steinkopff Verlag, Darmstadt, Germany. 617-620.
    • (1994) The Sodium Pump: Structure Mechanism, Hormonal Control and Its Role in Disease , pp. 617-620
    • Grell, E.1    Lewitzki, E.2    Ruf, H.3    Doludda, M.4
  • 29
    • 0001882118 scopus 로고
    • Precision titrations to determine affinity and stoichiometry of alkali, alkaline earth, and buffer cation binding to Na,K-ATPase
    • J. H. Kaplan, and P. De Weer, editors. Rockefeller University Press, New York
    • Grell, E., R. Warmuth, E. Lewitzki, and H. Ruf. 1991. Precision titrations to determine affinity and stoichiometry of alkali, alkaline earth, and buffer cation binding to Na,K-ATPase. In The Sodium Pump: Recent Developments. J. H. Kaplan, and P. De Weer, editors. Rockefeller University Press, New York. 441-445.
    • (1991) The Sodium Pump: Recent Developments , pp. 441-445
    • Grell, E.1    Warmuth, R.2    Lewitzki, E.3    Ruf, H.4
  • 30
    • 0026664942 scopus 로고
    • Ionics and conformational transitions of Na, K-ATPase
    • erratum 147:343-344
    • Grell, E., R. Warmuth, E. Lewitzki, and H. Ruf. 1992. Ionics and conformational transitions of Na, K-ATPase. Acta Physiol. Scand. 146: 213-221 (erratum 147:343-344).
    • (1992) Acta Physiol. Scand. , vol.146 , pp. 213-221
    • Grell, E.1    Warmuth, R.2    Lewitzki, E.3    Ruf, H.4
  • 31
    • 0028058903 scopus 로고
    • Partial reactions of the Na,K-ATPase: Determination of rate constants
    • Heyse, S., I. Wuddel, H.-J. Apell, and W. Stürmer. 1994. Partial reactions of the Na,K-ATPase: determination of rate constants. J. Gen. Physiol. 104:197-240.
    • (1994) J. Gen. Physiol. , vol.104 , pp. 197-240
    • Heyse, S.1    Wuddel, I.2    Apell, H.-J.3    Stürmer, W.4
  • 33
    • 0023754769 scopus 로고
    • Complex time dependence of phosphoenzyme formation and decomposition in electroplax Na,K-ATPase
    • J. C. Skou, J. G. Nørby, A. B. Maunsbach, and M. Esmann, editors. Alan R. Liss, New York
    • +-Pump, Part A: Molecular Aspects. J. C. Skou, J. G. Nørby, A. B. Maunsbach, and M. Esmann, editors. Alan R. Liss, New York. 307-314.
    • (1988) +-Pump, Part A: Molecular Aspects , pp. 307-314
    • Hobbs, A.S.1    Albers, R.W.2    Froehlich, J.P.3
  • 34
    • 0016184723 scopus 로고
    • +)-ATPase III. Purification from the outer medulla of mammalian kidney after selective removal of membrane components by sodium dodecylsulphate
    • +)-ATPase III. Purification from the outer medulla of mammalian kidney after selective removal of membrane components by sodium dodecylsulphate. Biochim. Biophys. Acta. 356:36-52.
    • (1974) Biochim. Biophys. Acta , vol.356 , pp. 36-52
    • Jørgensen, P.L.1
  • 40
    • 0017867017 scopus 로고
    • Rapid photolytic release of adenosine 5′-triphosphate from a protected analogue: Utilization by the Na:K pump of human red blood cell ghosts
    • Kaplan, J. H., B. Forbush III, and J. F. Hoffman. 1978. Rapid photolytic release of adenosine 5′-triphosphate from a protected analogue: utilization by the Na:K pump of human red blood cell ghosts. Biochemistry. 17:1929-1935.
    • (1978) Biochemistry , vol.17 , pp. 1929-1935
    • Kaplan, J.H.1    Forbush B. III2    Hoffman, J.F.3
  • 41
    • 0019052331 scopus 로고
    • Characterization of conformational changes in (Na, K) ATPase labeled with fluorescein at the active site
    • Karlish, S. J. D. 1980. Characterization of conformational changes in (Na, K) ATPase labeled with fluorescein at the active site. J. Bioenerg. Biomembr. 12:111-136.
    • (1980) J. Bioenerg. Biomembr. , vol.12 , pp. 111-136
    • Karlish, S.J.D.1
  • 42
    • 0018265473 scopus 로고
    • +)-ATPase as a tool for the study of the enzyme mechanism
    • +)-ATPase as a tool for the study of the enzyme mechanism. Biochim. Biophys. Acta. 527:115-130.
    • (1978) Biochim. Biophys. Acta , vol.527 , pp. 115-130
    • Karlish, S.J.D.1    Yates, D.W.2
  • 43
    • 0029875545 scopus 로고    scopus 로고
    • Phosphorylation of the sodium-potassium adenosinetriphosphatase proceeds through a rate-limiting conformafional change followed by rapid phosphoryl transfer
    • Keillor, J. W., and W. P. Jencks. 1996. Phosphorylation of the sodium-potassium adenosinetriphosphatase proceeds through a rate-limiting conformafional change followed by rapid phosphoryl transfer. Biochemistry. 35:2750-2753.
    • (1996) Biochemistry , vol.35 , pp. 2750-2753
    • Keillor, J.W.1    Jencks, W.P.2
  • 44
    • 0013139112 scopus 로고
    • +-ATPase studied with voltage-sensitive fluorescent dyes
    • E. Bamberg and W. Schoner, editors. Steinkopff Verlag, Darmstadt, Germany
    • +-ATPase studied with voltage-sensitive fluorescent dyes. In The Sodium Pump: Structure Mechanism, Hormonal Control and Its Role in Disease. E. Bamberg and W. Schoner, editors. Steinkopff Verlag, Darmstadt, Germany. 517-528.
    • (1994) The Sodium Pump: Structure Mechanism, Hormonal Control and Its Role in Disease , pp. 517-528
    • Klodos, I.1
  • 45
    • 0003249822 scopus 로고
    • Rapid conformational changes of the Na/K pump revealed by a fluorescent dye, RH-160
    • Klodos, I., and B. Forbush III. 1988. Rapid conformational changes of the Na/K pump revealed by a fluorescent dye, RH-160. J. Gen. Physiol. 92:46a.
    • (1988) J. Gen. Physiol. , vol.92
    • Klodos, I.1    Forbush B. III2
  • 46
    • 0004068805 scopus 로고
    • Sinauer Associates, Sunderland, MA
    • Läuger, P. 1991. Electrogenic Ion Pumps. Sinauer Associates, Sunderland, MA. 168-225.
    • (1991) Electrogenic Ion Pumps , pp. 168-225
    • Läuger, P.1
  • 48
    • 0016396322 scopus 로고
    • +)-stimulated ATP phosphohydrolase studied by a rapid-mixing technique
    • +)-stimulated ATP phosphohydrolase studied by a rapid-mixing technique. Biochim. BiophYs. Acta. 350:473-483.
    • (1974) Biochim. BiophYs. Acta , vol.350 , pp. 473-483
    • Mårdh, S.1    Zetterqvist, Ö.2
  • 50
    • 0015523849 scopus 로고
    • Activation by adenosine triphosphate in the phosphorylation kinetics of sodium and potassium transporting adenosine triphosphatase
    • Post, R. L., C. Hegyvary, and S. Kume. 1972. Activation by adenosine triphosphate in the phosphorylation kinetics of sodium and potassium transporting adenosine triphosphatase. J. Biol. Chem. 247:6530-6540.
    • (1972) J. Biol. Chem. , vol.247 , pp. 6530-6540
    • Post, R.L.1    Hegyvary, C.2    Kume, S.3
  • 52
    • 0027268148 scopus 로고
    • +-ATPase distinguish among different criteria for conformational change
    • +-ATPase distinguish among different criteria for conformational change. Biochim. Biophys. Acta. 1151:89-98.
    • (1993) Biochim. Biophys. Acta , vol.1151 , pp. 89-98
    • Pratap, P.R.1    Robinson, J.D.2
  • 54
    • 0028930414 scopus 로고
    • Investigations of ion binding to the cytoplasmic binding sites of the Na,K-pump
    • Schulz, S., and H.-J. Apell. 1995. Investigations of ion binding to the cytoplasmic binding sites of the Na,K-pump. Eur. Biophys. J. 23: 413-421.
    • (1995) Eur. Biophys. J. , vol.23 , pp. 413-421
    • Schulz, S.1    Apell, H.-J.2
  • 58
    • 0029040520 scopus 로고
    • + binding to sodium pump and control of the conformational change reported by fluorescein 5′-isothiocyanate modification
    • + binding to sodium pump and control of the conformational change reported by fluorescein 5′-isothiocyanate modification. Biochemistry. 34:8657-8667.
    • (1995) Biochemistry , vol.34 , pp. 8657-8667
    • Smirnova, I.N.1    Lin, S.-H.2    Faller, L.D.3
  • 59
    • 0031969082 scopus 로고    scopus 로고
    • Fast transient currents in the Na,K-ATPase induced by ATP concentration jumps from DMB-caged ATP
    • Sokolov, V. S., H.-J. Apell, J. E. T. Corrie, and D. R. Trentham. 1998. Fast transient currents in the Na,K-ATPase induced by ATP concentration jumps from DMB-caged ATP. Biophys. J. 74:2285-2298.
    • (1998) Biophys. J. , vol.74 , pp. 2285-2298
    • Sokolov, V.S.1    Apell, H.-J.2    Corrie, J.E.T.3    Trentham, D.R.4
  • 60
    • 0024596122 scopus 로고
    • Studies on conformational changes in Na,K-ATPase labeled with 5-iodoacetamidofluorescein
    • Steinberg, M., and S. J. D. Karlish. 1989. Studies on conformational changes in Na,K-ATPase labeled with 5-iodoacetamidofluorescein. J. Biol. Chem. 264:2726-2734.
    • (1989) J. Biol. Chem. , vol.264 , pp. 2726-2734
    • Steinberg, M.1    Karlish, S.J.D.2
  • 61
    • 0024474080 scopus 로고
    • Conformational transitions and charge translocation by the Na,K pump: Comparison of optical and electrical transients elicited by ATP-concentration jumps
    • Stürmer, W., H.-J. Apell, I. Wuddel, and P. Läuger. 1989. Conformational transitions and charge translocation by the Na,K pump: comparison of optical and electrical transients elicited by ATP-concentration jumps. J. Membr. Biol. 110:67-86.
    • (1989) J. Membr. Biol. , vol.110 , pp. 67-86
    • Stürmer, W.1    Apell, H.-J.2    Wuddel, I.3    Läuger, P.4
  • 62
    • 0025890342 scopus 로고
    • Charge translocation by the Na,K-pump. II. Ion binding and release at the extracellular face
    • Stürmer, W., R. Bühler, H.-J. Apell, and P. Läuger. 1991. Charge translocation by the Na,K-pump. II. Ion binding and release at the extracellular face. J. Membr. Biol. 121:163-176.
    • (1991) J. Membr. Biol. , vol.121 , pp. 163-176
    • Stürmer, W.1    Bühler, R.2    Apell, H.-J.3    Läuger, P.4
  • 63
    • 0028053976 scopus 로고
    • Kinetics of relaxation from rigor of permeabilized fast-twitch skeletal fibers from the rabbit using a novel caged ATP and apyrase
    • Thirlwell, H., J. E. T. Corrie, G. P. Reid, D. R. Trentham, and M. A. Ferenczi. 1994. Kinetics of relaxation from rigor of permeabilized fast-twitch skeletal fibers from the rabbit using a novel caged ATP and apyrase. Biophys. J. 67:2436-2447.
    • (1994) Biophys. J. , vol.67 , pp. 2436-2447
    • Thirlwell, H.1    Corrie, J.E.T.2    Reid, G.P.3    Trentham, D.R.4    Ferenczi, M.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.