메뉴 건너뛰기




Volumn 77, Issue 2, 1999, Pages 934-942

Rate determination in phosphorylation of shark rectal Na,K-ATPase by ATP: Temperature sensitivity and effects of ADP

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); ADENOSINE TRIPHOSPHATE; POTASSIUM ION; SODIUM ION;

EID: 0032774450     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)76944-4     Document Type: Article
Times cited : (26)

References (36)
  • 1
    • 0000770960 scopus 로고
    • Biochemical aspects of active transport
    • Albers, R. W. 1967. Biochemical aspects of active transport. Anna. Rev. Biochem. 36:727-756.
    • (1967) Anna. Rev. Biochem. , vol.36 , pp. 727-756
    • Albers, R.W.1
  • 2
    • 0025818726 scopus 로고
    • Charge translocation by the Na,K-pump. I. Kinetics of local field changes studied by time-resolved fluorescence measurements
    • Bühner, 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
    • Bühner, R.1    Stürmer, W.2    Apell, H.-J.3    Läuger, P.4
  • 6
    • 77957117234 scopus 로고    scopus 로고
    • The sodium pump
    • A. G. Lee, editor. JAI Press, Greenwich, CT
    • Cornelius, F. 1996. The sodium pump. In Biomembranes, Vol. 5. A. G. Lee, editor. JAI Press, Greenwich, CT. 133-184.
    • (1996) Biomembranes , vol.5 , pp. 133-184
    • Cornelius, F.1
  • 7
    • 0032564276 scopus 로고    scopus 로고
    • 2P phosphoforms of Na,K-ATPase. II. Interaction of substrate and cation binding sites in Pi-phosphorylation of Na,K-ATPase
    • 2P phosphoforms of Na,K-ATPase. II. Interaction of substrate and cation binding sites in Pi-phosphorylation of Na,K-ATPase. Biochemistry. 37:16686-16696.
    • (1998) Biochemistry , vol.37 , pp. 16686-16696
    • Cornelius, F.1    Fedosova, N.U.2    Klodos, I.3
  • 8
    • 0023652796 scopus 로고
    • + exchange accompanied by ATP hydrolysis. I. The ATP activation curve
    • + exchange accompanied by ATP hydrolysis. I. The ATP activation curve. Biochim. Biophys. Acta. 904:353-364.
    • (1987) Biochim. Biophys. Acta , vol.904 , pp. 353-364
    • Cornelius, F.1    Skou, J.C.2
  • 10
    • 0029598780 scopus 로고
    • Fluorescent styryl dyes as probes for Na,K-ATPase reaction mechanism. Significance of the charge of the hydrophilic 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 hydrophilic 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
  • 11
    • 0032578354 scopus 로고    scopus 로고
    • 2P phosphoforms of Na,K-ATPase. I. Comparison of intermediates formed from ATP and Pi. The reactivity towards vanadate and hydroxylamine
    • 2P phosphoforms of Na,K-ATPase. I. Comparison of intermediates formed from ATP and Pi. The reactivity towards vanadate and hydroxylamine. Biochemistry. 37: 13634-13642.
    • (1998) Biochemistry , vol.37 , pp. 13634-13642
    • Fedosova, N.U.1    Cornelius, F.2    Klodos, I.3
  • 12
    • 0025743067 scopus 로고
    • Rate-limiting steps in Na translocation by the Na/K pump
    • J. H. Kaplan and P. De Weer, editors. Rockefeller University Press, New York
    • Forbush, B., 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. De Weer, editors. Rockefeller University Press, New York. 211-225.
    • (1991) The Sodium Pump. Structure, Mechanism, and Regulation , pp. 211-225
    • Forbush, B.1    Klodos, I.2
  • 14
    • 0025868113 scopus 로고
    • +-activated adenosine triphosphatases
    • J. H. Kaplan and P. De Weer, editors. Rockefeller University Press, New York
    • +-activated adenosine triphosphatases. In The Sodium Pump. Structure, Mechanism, and Regulation. J. H. Kaplan and P. De Weer, editors. Rockefeller University Press, New York. 227-247.
    • (1991) The Sodium Pump. Structure, Mechanism, and Regulation , pp. 227-247
    • Froehlich, J.P.1    Fendler, K.2
  • 15
    • 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
  • 17
    • 0008699526 scopus 로고
    • What is a coupled vectorial process?
    • Jencks, W. P. 1983. What is a coupled vectorial process? Curr. Top. Memb. Transp. 19:1-19.
    • (1983) Curr. Top. Memb. Transp. , vol.19 , pp. 1-19
    • Jencks, W.P.1
  • 20
    • 0029875545 scopus 로고    scopus 로고
    • Phosphorylation of the sodium-potassium adenosinetriphosphatase proceeds through a rate-limiting conformational change followed by a rapid phosphoryl transfer
    • Keillor, J. W., and W. P. Jencks. 1996. Phosphorylation of the sodium-potassium adenosinetriphosphatase proceeds through a rate-limiting conformational change followed by a rapid phosphoryl transfer. Biochemistry. 35:2750-2753.
    • (1996) Biochemistry , vol.35 , pp. 2750-2753
    • Keillor, J.W.1    Jencks, W.P.2
  • 22
    • 0031443377 scopus 로고    scopus 로고
    • Fluorescent styryl dyes as probes for Na,K-ATPase reaction: Enzyme source and fluorescence response
    • Na/K-ATPase and Related Transport ATPases: Structure, Mechanism, and Regulation. L. A. Beaugé, D. C. Gadsby, and P. J. Garrahan, editors
    • Klodos, I., N. U. Fedosova, and F. Cornelius. 1997. Fluorescent styryl dyes as probes for Na,K-ATPase reaction: enzyme source and fluorescence response. In Na/K-ATPase and Related Transport ATPases: Structure, Mechanism, and Regulation. L. A. Beaugé, D. C. Gadsby, and P. J. Garrahan, editors. Ann. NY Acad. Sci. 834:394-396.
    • (1997) Ann. NY Acad. Sci. , vol.834 , pp. 394-396
    • Klodos, I.1    Fedosova, N.U.2    Cornelius, F.3
  • 23
    • 0029902679 scopus 로고    scopus 로고
    • Program dynafit for the analysis of enzyme kinetic data: Application to HIV proteinase
    • Kuzmic, P. 1996. Program dynafit for the analysis of enzyme kinetic data: application to HIV proteinase. Anal. Biochem. 237:260-273.
    • (1996) Anal. Biochem. , vol.237 , pp. 260-273
    • Kuzmic, P.1
  • 25
    • 0016396322 scopus 로고
    • +)-stimulated ATP phosphohydrolase studied by rapid-mixing technique
    • +)-stimulated ATP phosphohydrolase studied by rapid-mixing technique. Biochim. Biophys. Acta. 350:473-483.
    • (1974) Biochim. Biophys. Acta , vol.350 , pp. 473-483
    • Mårdh, S.1    Zetterqvist, Ö.2
  • 26
    • 0016760293 scopus 로고
    • The reversible delipidation of a solubilized sodium-plus-potassium ion-dependent adenosine triphosphatase from the salt gland of the spiny dogfish
    • Ottolenghi, P. 1975. The reversible delipidation of a solubilized sodium-plus-potassium ion-dependent adenosine triphosphatase from the salt gland of the spiny dogfish. Biochem. J. 151:61-66.
    • (1975) Biochem. J. , vol.151 , pp. 61-66
    • Ottolenghi, P.1
  • 27
    • 85025408146 scopus 로고
    • Flexibility of an active centre in sodium-plus-potassium adenosine triphosphatase
    • Post, R. L., T. Kume, T. Tobin, B. Orcutt, and A. K. Sen. 1969. Flexibility of an active centre in sodium-plus-potassium adenosine triphosphatase. J. Gen. Physiol. 54:306-326.
    • (1969) J. Gen. Physiol. , vol.54 , pp. 306-326
    • Post, R.L.1    Kume, T.2    Tobin, T.3    Orcutt, B.4    Sen, A.K.5
  • 28
    • 0016610287 scopus 로고
    • Phosphorylation by inorganic phosphate of sodium plus potassium ion transport adenosine triphosphatase
    • Post, R. L., G. Toda, and F. N. Rogers. 1975. Phosphorylation by inorganic phosphate of sodium plus potassium ion transport adenosine triphosphatase. J. Biol. Chem. 250:691-701.
    • (1975) J. Biol. Chem. , vol.250 , pp. 691-701
    • Post, R.L.1    Toda, G.2    Rogers, F.N.3
  • 29
    • 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
  • 30
    • 0003106620 scopus 로고
    • The Na-K pump
    • Skou, J. C. 1992. The Na-K pump. NIPS. 7:95-100.
    • (1992) NIPS , vol.7 , pp. 95-100
    • Skou, J.C.1
  • 32
    • 0023800199 scopus 로고
    • +-ATPase from rectal glands of Squalus acanthias
    • +-ATPase from rectal glands of Squalus acanthias. Methods Enzymol. 156:43-46.
    • (1988) Methods Enzymol. , vol.156 , pp. 43-46
    • Skou, J.C.1    Esmann, M.2
  • 34
    • 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
  • 36
    • 0029089396 scopus 로고
    • Electrogenicity of the sodium transport pathway in the Na,K-ATPase probed by charge-pulse experiments
    • Wuddel, I., and H.-J. Apell. 1995. Electrogenicity of the sodium transport pathway in the Na,K-ATPase probed by charge-pulse experiments. Biophys. J. 69:909-921.
    • (1995) Biophys. J. , vol.69 , pp. 909-921
    • Wuddel, I.1    Apell, H.-J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.