메뉴 건너뛰기




Volumn 245, Issue 1, 1997, Pages 71-83

Model of the pH-dependence of the concentrations of complexes involving metabolites, haemoglobin and magnesium ions in the human erythrocyte

Author keywords

Computer simulation; Erythrocyte glycolysis; Magnesium ions; pH effect; Regulation of metabolism

Indexed keywords

2,3 DIPHOSPHOGLYCERIC ACID; DEOXYHEMOGLOBIN; HEMOGLOBIN; HEMOGLOBIN A; HEXOKINASE; MAGNESIUM ION;

EID: 0030980054     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.00071.x     Document Type: Article
Times cited : (33)

References (67)
  • 1
    • 0013904551 scopus 로고
    • Effect of deoxygenation of intracellular hemoglobin on red cell glycolysis
    • Asakura, T., Sato, Y., Minikami, S. & Yoshikawa, H. (1966) Effect of deoxygenation of intracellular hemoglobin on red cell glycolysis, J. Biochem. 59, 524-526.
    • (1966) J. Biochem. , vol.59 , pp. 524-526
    • Asakura, T.1    Sato, Y.2    Minikami, S.3    Yoshikawa, H.4
  • 3
    • 0015708035 scopus 로고
    • Acid dissociation and complex formation of glycolytic metabolites with magnesium, potassium, and sodium
    • Achilles, W., Cumme, G. A. & Hoppe, H. (1973) Acid dissociation and complex formation of glycolytic metabolites with magnesium, potassium, and sodium, Acta Biol. Med. Germ. 31, 763-770.
    • (1973) Acta Biol. Med. Germ. , vol.31 , pp. 763-770
    • Achilles, W.1    Cumme, G.A.2    Hoppe, H.3
  • 4
    • 0015460659 scopus 로고
    • 2,3-Diphosphoglycerate: Acid dissociation and complex formation with magnesium, potassium, and sodium
    • Achilles, W., Cumme, G. A. & Hoppe, H. (1972) 2,3-Diphosphoglycerate: acid dissociation and complex formation with magnesium, potassium, and sodium, Acta Biol. Med. Germ. 29, 531-538.
    • (1972) Acta Biol. Med. Germ. , vol.29 , pp. 531-538
    • Achilles, W.1    Cumme, G.A.2    Hoppe, H.3
  • 5
    • 0015515865 scopus 로고
    • X-ray diffraction study of binding of 2,3-diphosphoglycerate to human deoxyhaemoglobin
    • Arnone, A. (1972) X-ray diffraction study of binding of 2,3-diphosphoglycerate to human deoxyhaemoglobin, Nature 237, 146-149.
    • (1972) Nature , vol.237 , pp. 146-149
    • Arnone, A.1
  • 6
    • 0015898349 scopus 로고
    • Interaction of haemoglobin with ions: Interactions among magnesium, adenosine 5′-triphosphate, 2,3-bisphosphoglycerate, and oxygenated and deoxygenated human haemoglobin under simulated intracellular conditions
    • Berger, H., Jänig, G.-R., Gerber, G., Ruckpaul, K. & Rapoport, S. M. (1973) Interaction of haemoglobin with ions: interactions among magnesium, adenosine 5′-triphosphate, 2,3-bisphosphoglycerate, and oxygenated and deoxygenated human haemoglobin under simulated intracellular conditions, Eur. J. Biochem. 38, 553-562.
    • (1973) Eur. J. Biochem. , vol.38 , pp. 553-562
    • Berger, H.1    Jänig, G.-R.2    Gerber, G.3    Ruckpaul, K.4    Rapoport, S.M.5
  • 7
    • 0027333165 scopus 로고
    • 13C n.m.r. isotopomer and computer simulation studies of the non-oxidative pentose phosphate pathway of human erythrocytes
    • 13C n.m.r. isotopomer and computer simulation studies of the non-oxidative pentose phosphate pathway of human erythrocytes, Biochem. J. 296, 379-387.
    • (1993) Biochem. J. , vol.296 , pp. 379-387
    • Berthon, H.A.1    Bubb, W.A.2    Kuchel, P.W.3
  • 10
    • 0014765117 scopus 로고
    • Magnesium, potassium, and the adenylate kinase equilibrium: Magnesium as a feedback signal from the adenine nucleotide pool
    • Blair, J. McD. (1970) Magnesium, potassium, and the adenylate kinase equilibrium: magnesium as a feedback signal from the adenine nucleotide pool, Eur. J. Biochem. 13, 384-390.
    • (1970) Eur. J. Biochem. , vol.13 , pp. 384-390
    • Blair, J.Mc.D.1
  • 12
    • 0021797469 scopus 로고
    • 31P nuclear magnetic resonance spectroscopy
    • 31P nuclear magnetic resonance spectroscopy, Blood 65, 1526-1530.
    • (1985) Blood , vol.65 , pp. 1526-1530
    • Bock, J.L.1    Wenz, B.2    Gupta, R.K.3
  • 13
    • 0021715544 scopus 로고
    • A metabolic osmotic model of human erythrocytes
    • Brumen, M. & Heinrich, R. (1984) A metabolic osmotic model of human erythrocytes, BioSystems 17, 155-169.
    • (1984) BioSystems , vol.17 , pp. 155-169
    • Brumen, M.1    Heinrich, R.2
  • 14
    • 0015218615 scopus 로고
    • The interaction between erythrocyte organic phosphates, magnesium ion, and hemoglobin
    • Bunn, H. F., Ransil, B. J. & Chao, A. (1971) The interaction between erythrocyte organic phosphates, magnesium ion, and hemoglobin, J. Biol. Chem. 246, 5273-5279.
    • (1971) J. Biol. Chem. , vol.246 , pp. 5273-5279
    • Bunn, H.F.1    Ransil, B.J.2    Chao, A.3
  • 16
    • 0024473068 scopus 로고
    • Metabolic control theory and biochemical systems theory: Different objectives, different assumptions, different results
    • Cornish-Bowden, A. (1989) Metabolic control theory and biochemical systems theory: different objectives, different assumptions, different results, J. Theor. Biol. 136, 365-377.
    • (1989) J. Theor. Biol. , vol.136 , pp. 365-377
    • Cornish-Bowden, A.1
  • 17
    • 0014992797 scopus 로고
    • On the mechanisms of the hypoxia-induced increase of 2,3-diphosphoglycerate in erythrocytes
    • Duhm, J. & Gerlach, E. (1971) On the mechanisms of the hypoxia-induced increase of 2,3-diphosphoglycerate in erythrocytes, Pflügers Arch. 326, 254-269.
    • (1971) Pflügers Arch. , vol.326 , pp. 254-269
    • Duhm, J.1    Gerlach, E.2
  • 18
    • 0018908733 scopus 로고
    • The effect of buffer composition and deoxygenation on the concentration of ionised magnesium inside human red blood cells
    • Flatman, P. W. (1980) The effect of buffer composition and deoxygenation on the concentration of ionised magnesium inside human red blood cells, J. Physiol. 300, 19-30.
    • (1980) J. Physiol. , vol.300 , pp. 19-30
    • Flatman, P.W.1
  • 19
    • 0017686941 scopus 로고
    • Use of ionophore A23187 to measure and to control free and bound cytoplasmic Mg in intact red cells
    • Flatman, P. & Lew, V. L. (1977) Use of ionophore A23187 to measure and to control free and bound cytoplasmic Mg in intact red cells, Nature 267, 360-362.
    • (1977) Nature , vol.267 , pp. 360-362
    • Flatman, P.1    Lew, V.L.2
  • 20
    • 0015073709 scopus 로고
    • Affinity of human hemoglobin A to 2,3-diphosphoglycerate. Effect of hemoglobin concentration and of pH
    • Garby, L. & de Verdier, C.-H. (1971) Affinity of human hemoglobin A to 2,3-diphosphoglycerate. Effect of hemoglobin concentration and of pH, Scand J. Clin. Lab. Invest. 27, 345-350.
    • (1971) Scand J. Clin. Lab. Invest. , vol.27 , pp. 345-350
    • Garby, L.1    De Verdier, C.-H.2
  • 21
    • 0014559196 scopus 로고
    • Binding of 2,3-diphosphoglycerate and adenosine triphosphate to human haemoglobin A
    • Garby, L., Gerber, G. & de Verdier, C.-H. (1969) Binding of 2,3-diphosphoglycerate and adenosine triphosphate to human haemoglobin A, Eur. J. Biochem. 10, 110-115.
    • (1969) Eur. J. Biochem. , vol.10 , pp. 110-115
    • Garby, L.1    Gerber, G.2    De Verdier, C.-H.3
  • 22
    • 0014026916 scopus 로고
    • A simulation study of mammalian phosphofructokinase
    • Garfinkel, D. (1966) A simulation study of mammalian phosphofructokinase, J. Biol. Chem. 241, 286-294.
    • (1966) J. Biol. Chem. , vol.241 , pp. 286-294
    • Garfinkel, D.1
  • 23
    • 0021765897 scopus 로고
    • 2+ concentration in adenosine 5′-triphosphate containing solutions in vitro and in vivo
    • 2+ concentration in adenosine 5′-triphosphate containing solutions in vitro and in vivo, Biochemistry 23, 3547-3552.
    • (1984) Biochemistry , vol.23 , pp. 3547-3552
    • Garfinkel, L.1    Garfinkel, D.2
  • 24
    • 0015899453 scopus 로고
    • Interaction of haemoglobin with ions: Quantitative description of the state of magnesium, adenosine 5′-triphosphate, 2,3-bisphosphoglycerate, and human haemoglobin under simulated intracellular conditions
    • Gerber, G., Berger, H., Jänig, G.-R. & Rapoport, S. M. (1973) Interaction of haemoglobin with ions: quantitative description of the state of magnesium, adenosine 5′-triphosphate, 2,3-bisphosphoglycerate, and human haemoglobin under simulated intracellular conditions, Eur. J. Biochem. 38, 563-571.
    • (1973) Eur. J. Biochem. , vol.38 , pp. 563-571
    • Gerber, G.1    Berger, H.2    Jänig, G.-R.3    Rapoport, S.M.4
  • 25
    • 0016161516 scopus 로고
    • Hexokinase of human erythrocytes: Purification, kinetic model and its application to the conditions in the cell
    • Gerber, G., Preissler, H., Heinrich, R. & Rapoport, S. M. (1974) Hexokinase of human erythrocytes: purification, kinetic model and its application to the conditions in the cell, Eur. J. Biochem. 45, 39-52.
    • (1974) Eur. J. Biochem. , vol.45 , pp. 39-52
    • Gerber, G.1    Preissler, H.2    Heinrich, R.3    Rapoport, S.M.4
  • 27
    • 0018676916 scopus 로고
    • Location of the allosteric site for 2,3-hisphosphoglycerate on human oxy- and de-oxyhemoglobin concentration as observed by magnetic resonance spectroscopy
    • Gupta, R. K., Benovic, J. L. & Rose, Z. B. (1979) Location of the allosteric site for 2,3-hisphosphoglycerate on human oxy- and de-oxyhemoglobin concentration as observed by magnetic resonance spectroscopy, J. Biol. Chem. 254, 8250-8265.
    • (1979) J. Biol. Chem. , vol.254 , pp. 8250-8265
    • Gupta, R.K.1    Benovic, J.L.2    Rose, Z.B.3
  • 28
    • 0018119413 scopus 로고
    • Magnetic resonance studies of the binding of ATP and cations to human hemoglobin
    • Gupta, R. K., Benovic, J. L. & Rose, Z. B. (1978a) Magnetic resonance studies of the binding of ATP and cations to human hemoglobin, J. Biol. Chem. 253, 6165-6171.
    • (1978) J. Biol. Chem. , vol.253 , pp. 6165-6171
    • Gupta, R.K.1    Benovic, J.L.2    Rose, Z.B.3
  • 30
    • 37049141937 scopus 로고
    • Magnesium and manganese complexes of citric and isocitric acids
    • Grzybowski, A. K., Tate, S. S. & Datta, S. P. (1970) Magnesium and manganese complexes of citric and isocitric acids, J. Chem. Soc. 1970, 241-245.
    • (1970) J. Chem. Soc. , vol.1970 , pp. 241-245
    • Grzybowski, A.K.1    Tate, S.S.2    Datta, S.P.3
  • 31
    • 0016328150 scopus 로고
    • The binding of phosphorylated red cell metabolites to human hemoglobin A
    • Hamasaki, N. & Rose, Z. B. (1974) The binding of phosphorylated red cell metabolites to human hemoglobin A, J. Biol. Chem. 249, 7896-7901.
    • (1974) J. Biol. Chem. , vol.249 , pp. 7896-7901
    • Hamasaki, N.1    Rose, Z.B.2
  • 33
    • 0014889067 scopus 로고
    • Interaction of haemoglobin with ions: Thermodynamic data on binding of adenosine triphosphate to methaemoglobin
    • Jänig, G.-H., Gerber, G., Ruckpaul, K., Rapoport, S. & Jung, F. (1970) Interaction of haemoglobin with ions: thermodynamic data on binding of adenosine triphosphate to methaemoglobin, Eur. J. Biochem. 17, 441-444.
    • (1970) Eur. J. Biochem. , vol.17 , pp. 441-444
    • Jänig, G.-H.1    Gerber, G.2    Ruckpaul, K.3    Rapoport, S.4    Jung, F.5
  • 34
    • 0024842144 scopus 로고
    • Metabolic dynamics in the human red cell. Part I - A comprehensive kinetic model
    • Joshi, A. & Palsson, B. O. (1989a) Metabolic dynamics in the human red cell. Part I - a comprehensive kinetic model, J. Theor. Biol. 141, 515-528.
    • (1989) J. Theor. Biol. , vol.141 , pp. 515-528
    • Joshi, A.1    Palsson, B.O.2
  • 35
    • 0024799182 scopus 로고
    • Metabolic dynamics in the human red cell. Part II - Interactions with the environment
    • Joshi, A. & Palsson, B. O. (1989b) Metabolic dynamics in the human red cell. Part II - interactions with the environment, J. Theor. Biol. 141, 529-545.
    • (1989) J. Theor. Biol. , vol.141 , pp. 529-545
    • Joshi, A.1    Palsson, B.O.2
  • 36
    • 0025095641 scopus 로고
    • Metabolic dynamics in the human red cell. Part III - Metabolic reaction rates
    • Joshi, A. & Palsson, B. O. (1989c) Metabolic dynamics in the human red cell. Part III - metabolic reaction rates, J. Theor. Biol. 142, 41-68.
    • (1989) J. Theor. Biol. , vol.142 , pp. 41-68
    • Joshi, A.1    Palsson, B.O.2
  • 37
    • 0025166450 scopus 로고
    • Metabolic dynamics in the human red cell. Part IV - Data prediction and some model computations
    • Joshi, A. & Palsson, B. O. (1989d) Metabolic dynamics in the human red cell. Part IV - data prediction and some model computations, J. Theor. Biol. 142, 69-85.
    • (1989) J. Theor. Biol. , vol.142 , pp. 69-85
    • Joshi, A.1    Palsson, B.O.2
  • 38
    • 0025675701 scopus 로고
    • Computer simulation of the pentose-phosphate pathway and associated metabolism used in conjunction with NMR experimental data from human erythrocytes
    • Kuchel, P. W., Berthon, H. A., Bubb, W. A., Bulliman, B. T. & Collins, J. G. (1990a) Computer simulation of the pentose-phosphate pathway and associated metabolism used in conjunction with NMR experimental data from human erythrocytes, Biomed. Biochim. Acta 49, 757-770.
    • (1990) Biomed. Biochim. Acta , vol.49 , pp. 757-770
    • Kuchel, P.W.1    Berthon, H.A.2    Bubb, W.A.3    Bulliman, B.T.4    Collins, J.G.5
  • 40
    • 0021188133 scopus 로고
    • The relationship between glucose concentration and rate of lactate production by human erythrocytes in an open perfusion system
    • Kuchel, P. W., Chapman, B. E., Lovric, V. A., Raftos, J. E., Stewart, I. M. & Thorburn, D. R. (1984) The relationship between glucose concentration and rate of lactate production by human erythrocytes in an open perfusion system, Biochim. Biophys. Acta 805, 191-203.
    • (1984) Biochim. Biophys. Acta , vol.805 , pp. 191-203
    • Kuchel, P.W.1    Chapman, B.E.2    Lovric, V.A.3    Raftos, J.E.4    Stewart, I.M.5    Thorburn, D.R.6
  • 41
    • 0021716497 scopus 로고
    • Measurement of intracellular pH and deoxyhemoglobin concentration in deoxygenated erythrocytes by phosphorous-31 nuclear magnetic resonance
    • Labotka, R. J. (1984) Measurement of intracellular pH and deoxyhemoglobin concentration in deoxygenated erythrocytes by phosphorous-31 nuclear magnetic resonance, Biochemistry 23, 5549-5555.
    • (1984) Biochemistry , vol.23 , pp. 5549-5555
    • Labotka, R.J.1
  • 42
    • 0018696222 scopus 로고
    • 2+ on the Keq of the creatine kinase reaction and other phosphate hydrolyses and phosphate transfer reactions
    • 2+ on the Keq of the creatine kinase reaction and other phosphate hydrolyses and phosphate transfer reactions, J. Biol. Chem. 254, 6528-6537.
    • (1979) J. Biol. Chem. , vol.254 , pp. 6528-6537
    • Lawson, J.W.R.1    Veech, R.L.2
  • 43
    • 0025687613 scopus 로고
    • A comprehensive model of human erythrocyte metabolism: Extensions to include pH
    • Lee, I.-D. & Palsson, B. O. (1990) A comprehensive model of human erythrocyte metabolism: extensions to include pH, Biomed. Biochim. Acta 49, 771-789.
    • (1990) Biomed. Biochim. Acta , vol.49 , pp. 771-789
    • Lee, I.-D.1    Palsson, B.O.2
  • 45
    • 0028073141 scopus 로고
    • Hemoglobin affinity for 2,3-bisphosphoglycerate in solutions and intact erythrocytes: Studies using pulsed-field gradient nuclear magnetic resonance and Monte Carlo simulations
    • Lennon, A. J., Scott, N. R., Chapman, B. E. & Kuchel, P. W., (1994) Hemoglobin affinity for 2,3-bisphosphoglycerate in solutions and intact erythrocytes: studies using pulsed-field gradient nuclear magnetic resonance and Monte Carlo simulations, Biophys. J. 67, 2096-2109.
    • (1994) Biophys. J. , vol.67 , pp. 2096-2109
    • Lennon, A.J.1    Scott, N.R.2    Chapman, B.E.3    Kuchel, P.W.4
  • 48
    • 0008489562 scopus 로고
    • Sodium and potassium complexes of adenosine-triphosphate: Equilibrium studies
    • Melchior, N. C. (1954) Sodium and potassium complexes of adenosine-triphosphate: equilibrium studies, J. Biol. Chem. 208, 615-627.
    • (1954) J. Biol. Chem. , vol.208 , pp. 615-627
    • Melchior, N.C.1
  • 49
    • 0029261550 scopus 로고
    • Red blood cell magnesium concentrations: Analytical problems and significance
    • Millart, H., Durlach, V. & Durlach, J. (1995) Red blood cell magnesium concentrations: analytical problems and significance, Magnes. Res. 8, 65-76.
    • (1995) Magnes. Res. , vol.8 , pp. 65-76
    • Millart, H.1    Durlach, V.2    Durlach, J.3
  • 50
    • 0013882352 scopus 로고
    • Studies on erythrocyte glycolysis. III. The effects of active cation transport, pH and inorganic phosphate concentration on erythrocyte glycolysis
    • Minakami, S. & Yoshikawa, H. (1966) Studies on erythrocyte glycolysis. III. The effects of active cation transport, pH and inorganic phosphate concentration on erythrocyte glycolysis, J. Biochem. 59, 145-150.
    • (1966) J. Biochem. , vol.59 , pp. 145-150
    • Minakami, S.1    Yoshikawa, H.2
  • 51
    • 0014766662 scopus 로고
    • Kinetic study of yeast hexokinase: Inhibition of the reaction by magnesium and ATP
    • Noat, G., Ricard, J., Borel, M. & Got, C. (1970) Kinetic study of yeast hexokinase: inhibition of the reaction by magnesium and ATP, Eur. J. Biochem. 13, 347-363.
    • (1970) Eur. J. Biochem. , vol.13 , pp. 347-363
    • Noat, G.1    Ricard, J.2    Borel, M.3    Got, C.4
  • 52
    • 0018719364 scopus 로고
    • Stability constants for biologically important metal-ligand complexes
    • O'Sullivan, W. J. & Smithers, G. W. (1979) Stability constants for biologically important metal-ligand complexes, Methods Enzymol. 63, 294-336.
    • (1979) Methods Enzymol. , vol.63 , pp. 294-336
    • O'Sullivan, W.J.1    Smithers, G.W.2
  • 53
    • 0002465050 scopus 로고
    • The stability constants of metaladenine nucleotide complexes
    • O'Sullivan, W. J. & Perrin, D. D. (1964) The stability constants of metaladenine nucleotide complexes, Biochemistry 3, 18-26.
    • (1964) Biochemistry , vol.3 , pp. 18-26
    • O'Sullivan, W.J.1    Perrin, D.D.2
  • 54
    • 0021186575 scopus 로고
    • A multinuclear NMR study of 2,3-bisphosphoglycerate metabolism in the human erythrocyte
    • Oxley, S. T., Porteous, R., Brindle, K. M., Boyd, J. & Campbell, I. D. (1984) A multinuclear NMR study of 2,3-bisphosphoglycerate metabolism in the human erythrocyte, Biochim. Biophys. Acta 805, 19-24.
    • (1984) Biochim. Biophys. Acta , vol.805 , pp. 19-24
    • Oxley, S.T.1    Porteous, R.2    Brindle, K.M.3    Boyd, J.4    Campbell, I.D.5
  • 55
    • 0000477435 scopus 로고
    • Computer calculations of equilibrium concentration in mixtures of metal ions and complexing species
    • Perrin, D. D. & Sayce, I. G. (1967) Computer calculations of equilibrium concentration in mixtures of metal ions and complexing species, Talanta 14, 833-842.
    • (1967) Talanta , vol.14 , pp. 833-842
    • Perrin, D.D.1    Sayce, I.G.2
  • 56
    • 0014023005 scopus 로고
    • Thermodynamic studies of the formation and ionization of the magnesium(II) complexes of ADP and ATP over the pH range 5 to 9
    • Phillips, R. C., George, S. J. P. & Rutman, R. J. (1966) Thermodynamic studies of the formation and ionization of the magnesium(II) complexes of ADP and ATP over the pH range 5 to 9, J. Am. Chem. Soc. 88, 2631-2640.
    • (1966) J. Am. Chem. Soc. , vol.88 , pp. 2631-2640
    • Phillips, R.C.1    George, S.J.P.2    Rutman, R.J.3
  • 57
    • 0001123138 scopus 로고
    • Effects of crowding in protein solutions
    • Ralston, G. B. (1990) Effects of crowding in protein solutions, J. Chem. Ed. 67, 857-860.
    • (1990) J. Chem. Ed. , vol.67 , pp. 857-860
    • Ralston, G.B.1
  • 58
    • 0017306757 scopus 로고
    • The regulatory principles of glycolysis in erythrocytes in vivo and in vitro. A minimal comprehensive model describing steady states, quasi-steady states and time-dependent processes
    • Rapoport, T. A., Heinrich, R. & Rapoport, S. M. (1976) The regulatory principles of glycolysis in erythrocytes in vivo and in vitro. A minimal comprehensive model describing steady states, quasi-steady states and time-dependent processes, Biochem. J. 154, 449-469.
    • (1976) Biochem. J. , vol.154 , pp. 449-469
    • Rapoport, T.A.1    Heinrich, R.2    Rapoport, S.M.3
  • 59
    • 0016524924 scopus 로고
    • Mathematical analysis of multienzyme systems; I. Modelling of the glycolysis of human erythrocytes
    • Rapoport, T. A. & Heinrich, R. (1975) Mathematical analysis of multienzyme systems; I. modelling of the glycolysis of human erythrocytes, BioSystems 7, 120-129.
    • (1975) BioSystems , vol.7 , pp. 120-129
    • Rapoport, T.A.1    Heinrich, R.2
  • 60
    • 0015949375 scopus 로고
    • A linear steady-state treatment of enzymatic chains. A mathematical model of glycolysis of human erythrocytes
    • Rapoport, T. A., Heinrich, R., Jacobasch, G. & Rapoport, S. (1974) A linear steady-state treatment of enzymatic chains. A mathematical model of glycolysis of human erythrocytes, Eur. J. Biochem. 42, 107-120.
    • (1974) Eur. J. Biochem. , vol.42 , pp. 107-120
    • Rapoport, T.A.1    Heinrich, R.2    Jacobasch, G.3    Rapoport, S.4
  • 61
    • 84982622771 scopus 로고
    • Binding of multivalent anions to oxygenated hemoglobin and the role of the imidazole group
    • (Rørth, M. & Astrup, P., eds) Alfred Benzon Symposium IV, Munksgaard, Copenhagen
    • Rapoport, S., Gerber, G., Ruckpaul, K., Jänig, G.-R., Frunder, H. & Jung, F. (1972) Binding of multivalent anions to oxygenated hemoglobin and the role of the imidazole group, in Oxygen affinity of hemoglobin and red cell acid base status (Rørth, M. & Astrup, P., eds) Alfred Benzon Symposium IV, Munksgaard, Copenhagen.
    • (1972) Oxygen Affinity of Hemoglobin and Red Cell Acid Base Status
    • Rapoport, S.1    Gerber, G.2    Ruckpaul, K.3    Jänig, G.-R.4    Frunder, H.5    Jung, F.6
  • 62
    • 0017754136 scopus 로고
    • Regulation of human erythrocyte hexokinase - The influence of glycolytic intermediates and inorganic phosphate
    • Rijksen, G. & Staal, G. E. J. (1977) Regulation of human erythrocyte hexokinase - the influence of glycolytic intermediates and inorganic phosphate, Biochim. Biophys. Acta 485, 75-86.
    • (1977) Biochim. Biophys. Acta , vol.485 , pp. 75-86
    • Rijksen, G.1    Staal, G.E.J.2
  • 63
    • 0016289146 scopus 로고
    • Specificity for the glucose-6-P inhibition site of hexokinase
    • Rose, I. A., Warms, J. V. B. & Kosow, D. P. (1974) Specificity for the glucose-6-P inhibition site of hexokinase, Arch. Biochem. Biophys. 164, 729-735.
    • (1974) Arch. Biochem. Biophys. , vol.164 , pp. 729-735
    • Rose, I.A.1    Warms, J.V.B.2    Kosow, D.P.3
  • 64
    • 0025196186 scopus 로고
    • 31P nuclear magnetic resonance investigation of the interaction between 2,3-bisphosphoglycerate and human normal adult hemoglobin
    • 31P nuclear magnetic resonance investigation of the interaction between 2,3-bisphosphoglycerate and human normal adult hemoglobin, Biochemistry 29, 3785-3792.
    • (1990) Biochemistry , vol.29 , pp. 3785-3792
    • Russu, I.M.1    Wu, S.2    Bupp, K.A.3    Ho, N.T.4    Ho, C.5
  • 65
    • 0001632076 scopus 로고
    • The apparent stability constants of ionic complexes of various adenosine phosphates with monovalent cations
    • Smith, R. M. & Alberty, R. A. (1956) The apparent stability constants of ionic complexes of various adenosine phosphates with monovalent cations, J. Phys. Chem. 60, 180-184.
    • (1956) J. Phys. Chem. , vol.60 , pp. 180-184
    • Smith, R.M.1    Alberty, R.A.2
  • 66
    • 0017146584 scopus 로고
    • 2 and other ions in solution: Calculation of the true concentration of species present in mixtures of associating ions
    • 2 and other ions in solution: calculation of the true concentration of species present in mixtures of associating ions, Biochem. J. 159, 1-5.
    • (1976) Biochem. J. , vol.159 , pp. 1-5
    • Storer, A.C.1    Cornish-Bowden, A.2
  • 67
    • 0022376486 scopus 로고
    • Regulation of the human-erythrocyte hexose-monophosphate shunt under conditions of oxidative stress. A study using NMR spectroscopy, a kinetic isotope effect, a reconstituted system and computer simulation
    • Thorburn, D. R. & Kuchel, P. W. (1985) Regulation of the human-erythrocyte hexose-monophosphate shunt under conditions of oxidative stress. A study using NMR spectroscopy, a kinetic isotope effect, a reconstituted system and computer simulation, Eur. J. Biochem. 150, 371-386.
    • (1985) Eur. J. Biochem. , vol.150 , pp. 371-386
    • Thorburn, D.R.1    Kuchel, P.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.