메뉴 건너뛰기




Volumn 109, Issue 5, 1997, Pages 555-570

The effect of ionic strength and specific anions on substrate binding and hydrolytic activities of Na,K-ATPase

Author keywords

Debye Huckel theory; eosin binding; K+ phosphatase activity; nucleotide binding; protein electrostatics

Indexed keywords

4 NITROPHENYLPHOSPHATASE; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); ANION; CHLORIDE ION; EOSIN; SODIUM CHLORATE; SODIUM NITRITE; THIOCYANATE SODIUM;

EID: 0031021044     PISSN: 00221295     EISSN: None     Source Type: Journal    
DOI: 10.1085/jgp.109.5.555     Document Type: Article
Times cited : (49)

References (81)
  • 1
    • 33947476119 scopus 로고
    • Application of the theory of diffusion-controlled reactions to enzyme kinetics
    • Alberty, R.A., and G.G. Hammes. 1958. Application of the theory of diffusion-controlled reactions to enzyme kinetics. J. Phys. Chem. 62:154-159.
    • (1958) J. Phys. Chem. , vol.62 , pp. 154-159
    • Alberty, R.A.1    Hammes, G.G.2
  • 2
    • 0026314673 scopus 로고
    • Electrostatic effects in protein folding, stability, and function
    • Allewell, N.M., and H. Oberoi. 1991. Electrostatic effects in protein folding, stability, and function. Methods Enzymol. 202:3-19.
    • (1991) Methods Enzymol. , vol.202 , pp. 3-19
    • Allewell, N.M.1    Oberoi, H.2
  • 3
    • 0023194022 scopus 로고
    • Electrostatic control of the rate-determining step of the copper, zinc superoxide dismutase catalytic reaction
    • Argese, E., P. Viglino, G. Rotilio, M. Scarpa, and A. Rigo. 1987. Electrostatic control of the rate-determining step of the copper, zinc superoxide dismutase catalytic reaction. Biochemistry. 26: 3224-3228.
    • (1987) Biochemistry , vol.26 , pp. 3224-3228
    • Argese, E.1    Viglino, P.2    Rotilio, G.3    Scarpa, M.4    Rigo, A.5
  • 6
    • 0023909653 scopus 로고
    • +-ATPase. Enzyme conformations from ligand interactions and Rb occlusion experiments
    • +-ATPase. Enzyme conformations from ligand interactions and Rb occlusion experiments. Biochim. Biophys. Acta. 940:43-50.
    • (1988) Biochim. Biophys. Acta , vol.940 , pp. 43-50
    • Campos, M.1    Berberián, G.2    Beaugé, L.3
  • 7
    • 0030028771 scopus 로고    scopus 로고
    • Salt effects on the amide hydrogen exchange of bovine pancreatic trypsin inhibitor
    • Christoffersen, M., S. Bolvig, and E. Tüchsen. 1996. Salt effects on the amide hydrogen exchange of bovine pancreatic trypsin inhibitor. Biochemistry. 35:2309-2315.
    • (1996) Biochemistry , vol.35 , pp. 2309-2315
    • Christoffersen, M.1    Bolvig, S.2    Tüchsen, E.3
  • 8
    • 50549155520 scopus 로고
    • The kinetics of enzyme-catalyzed reactions with two or more substrates or products. III. Prediction of initial velocity and inhibition patterns by inspection
    • Cleland, W.W. 1963. The kinetics of enzyme-catalyzed reactions with two or more substrates or products. III. Prediction of initial velocity and inhibition patterns by inspection. Biochim. Biophys. Acta. 67:188-196.
    • (1963) Biochim. Biophys. Acta , vol.67 , pp. 188-196
    • Cleland, W.W.1
  • 9
    • 0022147096 scopus 로고
    • The Hofmeister effect and the behaviour of water at interphases
    • Collins, K.D., and M.W. Washabaugh. 1985. The Hofmeister effect and the behaviour of water at interphases. Q. Rev. Biophys. 18: 323-422.
    • (1985) Q. Rev. Biophys. , vol.18 , pp. 323-422
    • Collins, K.D.1    Washabaugh, M.W.2
  • 10
    • 0001166734 scopus 로고
    • Zur Theorie der Elektrolyte. I. Gefrierpunktsniedrigung und verwandte Erscheinungen
    • Debye, P., and E. Hückel. 1923. Zur Theorie der Elektrolyte. I. Gefrierpunktsniedrigung und verwandte Erscheinungen. Physik. Z. 24:185-208.
    • (1923) Physik. Z. , vol.24 , pp. 185-208
    • Debye, P.1    Hückel, E.2
  • 11
    • 0025351241 scopus 로고
    • Anion-coupled Na efflux mediated by the human red cell Na/K pump
    • Dissing, S., and J.F. Hoffman. 1990. Anion-coupled Na efflux mediated by the human red cell Na/K pump. J. Gen. Physiol. 96:167-193.
    • (1990) J. Gen. Physiol. , vol.96 , pp. 167-193
    • Dissing, S.1    Hoffman, J.F.2
  • 13
    • 0023802003 scopus 로고
    • +-ATPase: Molar and specific activity, protein determination
    • +-ATPase: molar and specific activity, protein determination. Methods Enzymol. 156:105-115.
    • (1988) Methods Enzymol. , vol.156 , pp. 105-115
    • Esmann, M.1
  • 14
    • 0026057738 scopus 로고
    • Conformational transitions of detergent-solubilized Na,K-ATPase are conveniently monitored by the fluorescent probe 6-carboxy-eosin
    • Esmann, M. 1991. Conformational transitions of detergent-solubilized Na,K-ATPase are conveniently monitored by the fluorescent probe 6-carboxy-eosin. Biochem. Biophys. Res. Commun. 174: 63-70.
    • (1991) Biochem. Biophys. Res. Commun. , vol.174 , pp. 63-70
    • Esmann, M.1
  • 15
    • 0026706202 scopus 로고
    • Determination of rates of nucleotide binding and dissociation from Na,K-ATPase
    • Esmann, M. 1992. Determination of rates of nucleotide binding and dissociation from Na,K-ATPase. Biochim. Biophys. Acta. 1110: 20-28.
    • (1992) Biochim. Biophys. Acta , vol.1110 , pp. 20-28
    • Esmann, M.1
  • 16
    • 0031472918 scopus 로고    scopus 로고
    • Eosin as a probe for conformational transitions and nucleotide binding in Na,K-ATPase
    • In press
    • Esmann, M., and N.U. Fedosova. 1997. Eosin as a probe for conformational transitions and nucleotide binding in Na,K-ATPase. Ann. NY Acad. Sci. In press.
    • (1997) Ann. NY Acad. Sci.
    • Esmann, M.1    Fedosova, N.U.2
  • 17
    • 0028673458 scopus 로고
    • Estimating binding constants for site-specific interactions between monovalent ions and proteins
    • García-Moreno E, B. 1994. Estimating binding constants for site-specific interactions between monovalent ions and proteins. Methods Enzymol. 240:645-667.
    • (1994) Methods Enzymol. , vol.240 , pp. 645-667
    • García-Moreno, E.B.1
  • 19
    • 0020002086 scopus 로고
    • Occlusion of rubidium by the sodium-potassium pump: Its implications for the mechanism of potassium transport
    • Glynn, I.M., and D.E. Richards. 1982. Occlusion of rubidium by the sodium-potassium pump: its implications for the mechanism of potassium transport. J. Physiol. (Lond.). 303:17-43.
    • (1982) J. Physiol. (Lond.) , vol.303 , pp. 17-43
    • Glynn, I.M.1    Richards, D.E.2
  • 20
    • 0026026676 scopus 로고
    • Surface charge and ion channel function
    • Green, W.N., and O.S. Andersen. 1991. Surface charge and ion channel function. Annu. Rev. Physiol. 53:341-359.
    • (1991) Annu. Rev. Physiol. , vol.53 , pp. 341-359
    • Green, W.N.1    Andersen, O.S.2
  • 21
    • 0001154227 scopus 로고
    • The influence of net protein charge on the rate of formation of enzyme-substrate complexes
    • Hammes, G.G., and R.A. Alberty. 1959. The influence of net protein charge on the rate of formation of enzyme-substrate complexes. J. Phys. Chem. 63:274-279.
    • (1959) J. Phys. Chem. , vol.63 , pp. 274-279
    • Hammes, G.G.1    Alberty, R.A.2
  • 22
    • 0015218603 scopus 로고
    • Binding of adenosine triphosphate to sodium and potassium ion-stimulated adenosine triphosphatase
    • Hegyvary, C., and R.L. Post. 1971. Binding of adenosine triphosphate to sodium and potassium ion-stimulated adenosine triphosphatase. J. Biol. Chem. 246:5234-5240.
    • (1971) J. Biol. Chem. , vol.246 , pp. 5234-5240
    • Hegyvary, C.1    Post, R.L.2
  • 23
    • 0001126867 scopus 로고
    • Characterization of tonoplast enzyme activities and transport
    • Jacoby, B. 1987. Characterization of tonoplast enzyme activities and transport. Methods Enzymol. 148:105-114.
    • (1987) Methods Enzymol. , vol.148 , pp. 105-114
    • Jacoby, B.1
  • 24
    • 0026664778 scopus 로고
    • Heterogeneity of pig kidney Na,K-ATPase as indicated by ADP- And ouabain-binding stoichiometry
    • Jensen, J. 1992. Heterogeneity of pig kidney Na,K-ATPase as indicated by ADP-and ouabain-binding stoichiometry. Biochim. Biophys. Acta. 1110:81-87.
    • (1992) Biochim. Biophys. Acta , vol.1110 , pp. 81-87
    • Jensen, J.1
  • 25
    • 0021210752 scopus 로고
    • Binding of sodium and potassium to the sodium pump of pig kidney evaluated from nucleotide-binding behaviour
    • Jensen, J., J.G. Nørby, and P. Ottolenghi. 1984. Binding of sodium and potassium to the sodium pump of pig kidney evaluated from nucleotide-binding behaviour. J. Physiol. (Lond.) 346:219-241.
    • (1984) J. Physiol. (Lond.) , vol.346 , pp. 219-241
    • Jensen, J.1    Nørby, J.G.2    Ottolenghi, P.3
  • 26
    • 0021099661 scopus 로고
    • +)-ATPase. The abolition of subunit-subunit interaction and the maximum weight of the nucleotide binding unit
    • +)-ATPase. The abolition of subunit-subunit interaction and the maximum weight of the nucleotide binding unit. Biochim. Biophys. Acta. 731:282-289.
    • (1983) Biochim. Biophys. Acta , vol.731 , pp. 282-289
    • Jensen, J.1    Ottolenghi, P.2
  • 28
    • 0017812373 scopus 로고
    • Intermediate states of subfragment 1 and actosubfragment 1 ATPase: Reevaluation of mechanism
    • Johnson, K.A., and E.W. Taylor. 1978. Intermediate states of subfragment 1 and actosubfragment 1 ATPase: reevaluation of mechanism. Biochemistry. 17: 3432-3442.
    • (1978) Biochemistry , vol.17 , pp. 3432-3442
    • Johnson, K.A.1    Taylor, E.W.2
  • 29
    • 15144354332 scopus 로고
    • Enzymic equilibria and thermodynamics
    • second edition. P.D. Boyer, H. Lardy, and K. Myrbäck, editors. Academic Press, New York/London
    • Johnson, M.J. 1960. Enzymic equilibria and thermodynamics. In The Enzymes, Vol. 3B, second edition. P.D. Boyer, H. Lardy, and K. Myrbäck, editors. Academic Press, New York/London. 407-441.
    • (1960) The Enzymes , vol.3 B , pp. 407-441
    • Johnson, M.J.1
  • 30
    • 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
  • 31
    • 0016786376 scopus 로고
    • +)-ATPase. V. Conformational changes in the enzyme. Transitions between the Na-form and the K-form studied with tryptic digestion as a tool
    • +)-ATPase. V. Conformational changes in the enzyme. Transitions between the Na-form and the K-form studied with tryptic digestion as a tool. Biochim. Biophys. Acta. 401:399-415.
    • (1975) Biochim. Biophys. Acta , vol.401 , pp. 399-415
    • Jørgensen, P.L.1
  • 32
    • 0023772728 scopus 로고
    • +-ATPase: Enzyme sources, preparative problems, and preparation from mammalian kidney
    • +-ATPase: enzyme sources, preparative problems, and preparation from mammalian kidney. Methods Enzymol. 156:29-43.
    • (1988) Methods Enzymol. , vol.156 , pp. 29-43
    • Jørgensen, P.L.1
  • 33
    • 0025883332 scopus 로고
    • Localization of ligand binding from studies of chemical modification
    • J.H. Kaplan and P. De Weer, editors. Society of General Physiologists series, The Rockefeller University Press, New York
    • Kaplan, J.H. 1991. Localization of ligand binding from studies of chemical modification. In The Sodium Pump: Structure, Mechanism and Regulation. J.H. Kaplan and P. De Weer, editors. Society of General Physiologists series, Vol. 46. The Rockefeller University Press, New York. 117-128.
    • (1991) The Sodium Pump: Structure, Mechanism and Regulation , vol.46 , pp. 117-128
    • Kaplan, J.H.1
  • 34
    • 27744564562 scopus 로고
    • Individual activity coefficients of ions in aqueous solutions
    • Kielland, J. 1937. Individual activity coefficients of ions in aqueous solutions. J. Am. Chem. Soc. 59:1675-1678.
    • (1937) J. Am. Chem. Soc. , vol.59 , pp. 1675-1678
    • Kielland, J.1
  • 35
  • 36
    • 0345098218 scopus 로고
    • Effect of lyotropic anions on the dephosphorylation of Na,K-ATPase phosphointermediates
    • J.H. Kaplan and P. De Weer, editors. Society of General Physiologists series, The Rockefeller University Press, New York
    • Klodos, I. 1991. Effect of lyotropic anions on the dephosphorylation of Na,K-ATPase phosphointermediates. In The Sodium Pump, Recent Developments. J.H. Kaplan and P. De Weer, editors. Society of General Physiologists series, Vol. 46. The Rockefeller University Press, New York. 333-337.
    • (1991) The Sodium Pump, Recent Developments , vol.46 , pp. 333-337
    • Klodos, I.1
  • 37
    • 10544249106 scopus 로고
    • Transient kinetics of dephosphorylation of Na,K-ATPase after dilution of NaCl
    • J.H. Kaplan and P. De Weer, editors. Society of General Physiologists series, The Rockefeller University Press, New York
    • Klodos, I., and B. Forbush III. 1991. Transient kinetics of dephosphorylation of Na,K-ATPase after dilution of NaCl. In The Sodium Pump, Recent Developments. J.H. Kaplan and P. De Weer, editors. Society of General Physiologists series, Vol. 46. The Rockefeller University Press, New York. 327-331.
    • (1991) The Sodium Pump, Recent Developments , vol.46 , pp. 327-331
    • Klodos, I.1    Forbush III, B.2
  • 38
    • 0028089326 scopus 로고
    • Kinetic heterogeneity of phosphoenzyme of Na,K-ATPase modeled by unmixed phases. Competence of the phosphointermediate
    • Klodos, I., R.L. Post, and B. Forbush III. 1994. Kinetic heterogeneity of phosphoenzyme of Na,K-ATPase modeled by unmixed phases. Competence of the phosphointermediate. J. Biol. Chem. 269:1734-1743.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1734-1743
    • Klodos, I.1    Post, R.L.2    Forbush III, B.3
  • 40
    • 0015211001 scopus 로고
    • +)-activated ATPase. I. Effects of simple anions and nucleoside triphosphates on the alkali-cation specificity of the p-nitrophenylphosphatase
    • +)-activated ATPase. I. Effects of simple anions and nucleoside triphosphates on the alkali-cation specificity of the p-nitrophenylphosphatase. Biochim. Biophys. Acta. 225:11-19.
    • (1971) Biochim. Biophys. Acta , vol.225 , pp. 11-19
    • Koyal, D.1    Rao, S.N.2    Askari, A.3
  • 41
    • 0024298964 scopus 로고
    • How do enzymes work?
    • Kraut, J. 1988. How do enzymes work? Science (Wash. DC). 242:533-540.
    • (1988) Science (Wash. DC) , vol.242 , pp. 533-540
    • Kraut, J.1
  • 42
    • 0001863950 scopus 로고
    • Transition state theory
    • fourth edition. C. Bernasconi, editor. John Wiley and Sons, New York
    • Kreevoy, M.M, and D.G. Truhlar. 1986. Transition state theory. In Investigations of Rates and Mechanisms of Reactions. Part I. fourth edition. C. Bernasconi, editor. John Wiley and Sons, New York. 14-95.
    • (1986) Investigations of Rates and Mechanisms of Reactions , Issue.1 PART , pp. 14-95
    • Kreevoy, M.M.1    Truhlar, D.G.2
  • 43
    • 0025877774 scopus 로고
    • The Hofmeister series and ionic strength
    • Leberman, R. 1991. The Hofmeister series and ionic strength. FEBS Lett. 284:293-294.
    • (1991) FEBS Lett. , vol.284 , pp. 293-294
    • Leberman, R.1
  • 44
    • 0002619244 scopus 로고
    • Effect of high salt concentrations on water structure
    • Leberman, R., and A.K. Soper. 1995. Effect of high salt concentrations on water structure. Nature (Lond.). 378:364-366.
    • (1995) Nature (Lond.) , vol.378 , pp. 364-366
    • Leberman, R.1    Soper, A.K.2
  • 46
    • 0027257747 scopus 로고
    • Long-range surface charge-charge interactions in proteins. Comparison of experimental results with calculations from a theoretical method
    • Loewenthal, R., J. Sancho, T. Reinikainen, and A.R. Fersht. 1993. Long-range surface charge-charge interactions in proteins. Comparison of experimental results with calculations from a theoretical method. J. Mol. Biol. 232:574-583.
    • (1993) J. Mol. Biol. , vol.232 , pp. 574-583
    • Loewenthal, R.1    Sancho, J.2    Reinikainen, T.3    Fersht, A.R.4
  • 48
    • 0028290302 scopus 로고
    • Phosphate from the phosphointermediate (EP) of the human red blood cell Na/K pump is coeffluxed with Na, in the absence of external K
    • Marín, R., and J.F. Hoffman. 1994a. Phosphate from the phosphointermediate (EP) of the human red blood cell Na/K pump is coeffluxed with Na, in the absence of external K. J. Gen. Physiol. 104:1-32.
    • (1994) J. Gen. Physiol. , vol.104 , pp. 1-32
    • Marín, R.1    Hoffman, J.F.2
  • 50
    • 0029665127 scopus 로고    scopus 로고
    • Asp70 in the peripheral anionic site of human butyrylcholineesterase
    • Masson, P., M.-T. Froment, C.F. Bartels, and O. Lockridge. 1996. Asp70 in the peripheral anionic site of human butyrylcholineesterase. Eur. J. Biochem. 235:36-48.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 36-48
    • Masson, P.1    Froment, M.-T.2    Bartels, C.F.3    Lockridge, O.4
  • 53
    • 84962439356 scopus 로고    scopus 로고
    • Roles of electrostatic interactions in proteins
    • Nakamura, H. 1996. Roles of electrostatic interactions in proteins. Q. Rev. Biophys. 29:1-90.
    • (1996) Q. Rev. Biophys. , vol.29 , pp. 1-90
    • Nakamura, H.1
  • 58
    • 0021095114 scopus 로고
    • +)-ATPase can only be due to the oligomeric structure of the enzyme
    • +)-ATPase can only be due to the oligomeric structure of the enzyme. Biochim. Biophys. Acta. 727:89-100.
    • (1983) Biochim. Biophys. Acta , vol.727 , pp. 89-100
    • Ottolenghi, P.1    Jensen, J.2
  • 60
    • 0000738293 scopus 로고
    • Hopes for Hofmeister
    • Parsegian, V.A. 1995. Hopes for Hofmeister. Nature (Lond.). 378: 335-336.
    • (1995) Nature (Lond.) , vol.378 , pp. 335-336
    • Parsegian, V.A.1
  • 61
    • 33646830005 scopus 로고
    • Ion motive ATPases. I. Ubiquity, properties, and significance to cell function
    • Pedersen, P.L., and E. Carafoli. 1987. Ion motive ATPases. I. Ubiquity, properties, and significance to cell function. TIBS. 12:146-150.
    • (1987) TIBS , vol.12 , pp. 146-150
    • Pedersen, P.L.1    Carafoli, E.2
  • 62
    • 0030027897 scopus 로고    scopus 로고
    • Expression in high yield of pig α1β1 Na,K-ATPase and inactive mutants D369N and D807N in Saccharomyces cerevisiae
    • Pedersen, P.A., J.H. Rasmussen, and P.L. Jørgensen. 1996. Expression in high yield of pig α1β1 Na,K-ATPase and inactive mutants D369N and D807N in Saccharomyces cerevisiae. J. Biol. Chem. 271: 2514-2522.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2514-2522
    • Pedersen, P.A.1    Rasmussen, J.H.2    Jørgensen, P.L.3
  • 64
    • 0022800960 scopus 로고
    • m is a misleading kinetic indicator
    • m is a misleading kinetic indicator. Biochem J. 239:175-178.
    • (1986) Biochem J. , vol.239 , pp. 175-178
    • Plesner, I.1
  • 65
    • 0025821297 scopus 로고
    • A Hofmeister effect on the phosphoenzyme of Na,K-ATPase
    • J.H. Kaplan and P. De Weer, editors. Society of General Physiologists series, The Rockefeller University Press, New York
    • Post, R.L., and K. Suzuki. 1991. A Hofmeister effect on the phosphoenzyme of Na,K-ATPase. In The Sodium Pump: Structure, Mechanism, and Regulation. J.H. Kaplan and P. De Weer, editors. Society of General Physiologists series, Vol. 46. The Rockefeller University Press, New York. 201-209.
    • (1991) The Sodium Pump: Structure, Mechanism, and Regulation , vol.46 , pp. 201-209
    • Post, R.L.1    Suzuki, K.2
  • 66
    • 0017820499 scopus 로고
    • Thermodynamic analysis of ion effects on the binding and conformational equilibria of proteins and nucleic acids: The roles of ion association or release, screening, and ion effects on water activity
    • Record, M.T., Jr., C.F. Anderson, and T.M. Lohman. 1978. Thermodynamic analysis of ion effects on the binding and conformational equilibria of proteins and nucleic acids: the roles of ion association or release, screening, and ion effects on water activity. Q. Rev. Biophys. 11:103-178.
    • (1978) Q. Rev. Biophys. , vol.11 , pp. 103-178
    • Record Jr., M.T.1    Anderson, C.F.2    Lohman, T.M.3
  • 68
    • 0027242014 scopus 로고
    • +. The possibility of differences between the first turnover and steady state
    • +. The possibility of differences between the first turnover and steady state. J. Biol. Chem. 268: 12579-12590.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12579-12590
    • Rossi, R.C.1    Nørby, J.G.2
  • 69
    • 0023660015 scopus 로고
    • Electrostatic effects on modification of charged groups in the active site cleft of subtilisin by protein engineering
    • Russell, A.J., P.G. Thomas, and A.R. Fersht. 1987. Electrostatic effects on modification of charged groups in the active site cleft of subtilisin by protein engineering. J. Mol. Biol. 193:803-813.
    • (1987) J. Mol. Biol. , vol.193 , pp. 803-813
    • Russell, A.J.1    Thomas, P.G.2    Fersht, A.R.3
  • 71
    • 0015977390 scopus 로고
    • +)- Dependent enzyme system. III. Effect on the p-nitrophenylphosphatase activity of the system
    • +)-dependent enzyme system. III. Effect on the p-nitrophenylphosphatase activity of the system. Biochim. Biophys. Acta. 339:258-273.
    • (1974) Biochim. Biophys. Acta , vol.339 , pp. 258-273
    • Skou, J.C.1
  • 72
    • 0018788561 scopus 로고
    • + and on hydrolysis at different pH and temperature
    • + and on hydrolysis at different pH and temperature. Biochim. Biophys. Acta. 567:421-435.
    • (1979) Biochim. Biophys. Acta , vol.567 , pp. 421-435
    • Skou, J.C.1
  • 73
    • 0019328131 scopus 로고
    • +)-ATPase studied by ligand effects on intrinsic and extrinsic fluorescence
    • +)-ATPase studied by ligand effects on intrinsic and extrinsic fluorescence. Biochim. Biophys. Acta. 601:386-402.
    • (1980) Biochim. Biophys. Acta , vol.601 , pp. 386-402
    • Skou, J.C.1    Esmann, M.2
  • 75
    • 0019877708 scopus 로고
    • Electrostatic influence of local cysteine environments on disulfide exchange kinetics
    • Snyder, G.H., M.J. Cennerazzo, A.J. Karalis, and D. Field. 1981. Electrostatic influence of local cysteine environments on disulfide exchange kinetics. Biochemistry. 20:6509-6519.
    • (1981) Biochemistry , vol.20 , pp. 6509-6519
    • Snyder, G.H.1    Cennerazzo, M.J.2    Karalis, A.J.3    Field, D.4
  • 76
    • 0000600604 scopus 로고
    • +-translocating ATPases: Advances using membrane vesicles
    • +-translocating ATPases: advances using membrane vesicles. Annu. Rev. Plant Physiol. 36:175-208.
    • (1985) Annu. Rev. Plant Physiol. , vol.36 , pp. 175-208
    • Sze, H.1
  • 77
    • 0003903810 scopus 로고
    • John Wiley and Sons, Inc., New York/London/Sidney
    • Tanford, C. 1961. Physical Chemistry of Macromolecules. John Wiley and Sons, Inc., New York/London/Sidney. pp. 710.
    • (1961) Physical Chemistry of Macromolecules , pp. 710
    • Tanford, C.1
  • 78
    • 0026784847 scopus 로고
    • Lysine 480 is not an essential residue for ATP binding or hydrolysis by Na,K-ATPase
    • Wang, K., and R.A. Farley. 1992. Lysine 480 is not an essential residue for ATP binding or hydrolysis by Na,K-ATPase. J. Biol. Chem. 267:3577-3580.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3577-3580
    • Wang, K.1    Farley, R.A.2
  • 79
    • 0021476470 scopus 로고
    • Calculation of electrostatic interactions in biological systems and in solutions
    • Warshel, A., and S.T. Russell. 1984. Calculation of electrostatic interactions in biological systems and in solutions. Q. Rev. Biophys. 17:283-422.
    • (1984) Q. Rev. Biophys. , vol.17 , pp. 283-422
    • Warshel, A.1    Russell, S.T.2
  • 80
    • 77956904558 scopus 로고
    • Creatine kinase (adenosine 5′-triphosphate-creatine phosphotransferase)
    • third edition. P.D. Boyer, editor. Academic Press, London
    • Watts, D.C. 1973. Creatine kinase (adenosine 5′-triphosphate-creatine phosphotransferase). In The Enzymes, Vol. IIIA, third edition. P.D. Boyer, editor. Academic Press, London. 383-455.
    • (1973) The Enzymes , vol.3 A , pp. 383-455
    • Watts, D.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.