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Volumn 80, Issue 6, 2001, Pages 2622-2630

Temperature transition of human hemoglobin at body temperature: Effects of calcium

Author keywords

[No Author keywords available]

Indexed keywords

CALCIMYCIN; CALCIUM ION; HEMOGLOBIN;

EID: 0034995585     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(01)76232-7     Document Type: Article
Times cited : (50)

References (58)
  • 2
    • 0024464866 scopus 로고
    • Echinocytosis and microvesiculation of human erythrocytes induced by insertion of merocyanine 540 into the outer membrane leaflet
    • Allan, D., C. Hagelberg, Kallen, and Haest. 1989. Echinocytosis and microvesiculation of human erythrocytes induced by insertion of merocyanine 540 into the outer membrane leaflet. Biochim. Biophys. Acta. 986:115-122.
    • (1989) Biochim. Biophys. Acta , vol.986 , pp. 115-122
    • Allan, D.1    Hagelberg, C.2    Kallen3    Haest4
  • 3
    • 0016830799 scopus 로고
    • Accumulation of 1,2-diacylglycerol in the plasma membrane lead to echinocyte transformation of erythrocytes
    • Allan, D., and R. H. Michell. 1975. Accumulation of 1,2-diacylglycerol in the plasma membrane lead to echinocyte transformation of erythrocytes. Nature. 258:348-349.
    • (1975) Nature , vol.258 , pp. 348-349
    • Allan, D.1    Michell, R.H.2
  • 4
    • 0019730895 scopus 로고
    • 2+-induced biochemical changes in human erythrocytes and their relation to microvesiculation
    • 2+-induced biochemical changes in human erythrocytes and their relation to microvesiculation. Biochem. J. 198:433-440.
    • (1981) Biochem. J. , vol.198 , pp. 433-440
    • Allan, D.1    Thomas, P.2
  • 5
    • 0019730896 scopus 로고
    • 2+-sensitive biochemical changes in human erythrocytes and their membranes
    • 2+-sensitive biochemical changes in human erythrocytes and their membranes. Biochem. J. 198:441-445.
    • (1981) Biochem. J. , vol.198 , pp. 441-445
    • Allan, D.1    Thomas, P.2
  • 6
    • 0018761655 scopus 로고
    • Calcium-induced erythrocyte membrane changes
    • Allen, D. W., and S. Cadman. 1979. Calcium-induced erythrocyte membrane changes. Biochim. Biophys. Acta. 551:1-9.
    • (1979) Biochim. Biophys. Acta. , vol.551 , pp. 1-9
    • Allen, D.W.1    Cadman, S.2
  • 7
    • 0031795577 scopus 로고    scopus 로고
    • Temperature transitions of protein properties in human red blood cells
    • Artmann, G. M., Ch. Kelemen, D. Porst, G. Büldt, and S. Chien. 1998. Temperature transitions of protein properties in human red blood cells. Biophys. J. 75:3179-3183.
    • (1998) Biophys. J. , vol.75 , pp. 3179-3183
    • Artmann, G.M.1    Kelemen, Ch.2    Porst, D.3    Büldt, G.4    Chien, S.5
  • 8
    • 0019217068 scopus 로고
    • Interaction of divalent cations with human red cell cytoskeletons
    • Beaven, G. H., and W. B. Gratzer. 1980. Interaction of divalent cations with human red cell cytoskeletons. Biochim. Biophys. Acta. 600: 140-149.
    • (1980) Biochim. Biophys. Acta. , vol.600 , pp. 140-149
    • Beaven, G.H.1    Gratzer, W.B.2
  • 9
    • 0015843337 scopus 로고
    • Equations for the spectrophotometric analysis of hemoglobin mixtures
    • Benesch, R. E., R. Benesch, and S. Yung. 1973. Equations for the spectrophotometric analysis of hemoglobin mixtures. Anal. Biochem. 55: 245-248.
    • (1973) Anal. Biochem. , vol.55 , pp. 245-248
    • Benesch, R.E.1    Benesch, R.2    Yung, S.3
  • 10
    • 0002163969 scopus 로고
    • Red cell shapes: An illustrated classification and its rationale
    • Springer-Verlag, New York
    • Bessis, M., R. I. Weed, and P. F. Leblond. 1973. Red cell shapes: an illustrated classification and its rationale. In Red Cell Shape. Springer-Verlag, New York.
    • (1973) Red Cell Shape
    • Bessis, M.1    Weed, R.I.2    Leblond, P.F.3
  • 11
    • 0015512084 scopus 로고
    • Ca-induced K transport in human red cells: Localization of the Ca-sensitive site to the inside of the membrane
    • Blum, R. M., and J. F. Hoffman. 1972. Ca-induced K transport in human red cells: localization of the Ca-sensitive site to the inside of the membrane. Biochem. Biophys. Res. Commun. 46:1146-1152.
    • (1972) Biochem. Biophys. Res. Commun. , vol.46 , pp. 1146-1152
    • Blum, R.M.1    Hoffman, J.F.2
  • 12
    • 0024445677 scopus 로고
    • Enrichment of two glycosyl-phosphatidylinositol-anchored proteins, acetylcholinesterase and decay accelerating factor, in vesicles released from human RBCs
    • Bütikofer, P., F. A. Kuypers, C. M. Xu, D. T. Y. Chiu, and B. Lubin. 1989. Enrichment of two glycosyl-phosphatidylinositol-anchored proteins, acetylcholinesterase and decay accelerating factor, in vesicles released from human RBCs. Blood. 74:1481-1485.
    • (1989) Blood , vol.74 , pp. 1481-1485
    • Bütikofer, P.1    Kuypers, F.A.2    Xu, C.M.3    Chiu, D.T.Y.4    Lubin, B.5
  • 13
    • 0024203899 scopus 로고
    • Water hydration in the intra- and extracellular environment of human erythrocytes
    • Cameron, I. V., and V. A. Ord. 1988. Water hydration in the intra- and extracellular environment of human erythrocytes. Biochem. Cell Biol. 66:1186-1199.
    • (1988) Biochem. Cell Biol. , vol.66 , pp. 1186-1199
    • Cameron, I.V.1    Ord, V.A.2
  • 14
    • 0018872612 scopus 로고
    • Calmodulin plays a pivotal role in cellular regulation
    • Cheung, W. Y. 1980. Calmodulin plays a pivotal role in cellular regulation. Science. 207:9-27.
    • (1980) Science , vol.207 , pp. 9-27
    • Cheung, W.Y.1
  • 15
    • 0023943252 scopus 로고
    • Senescence of red blood cells: Progress and problems
    • Clark, M. R. 1988. Senescence of red blood cells: progress and problems. Physiol. Rev. 68:503-554.
    • (1988) Physiol. Rev. , vol.68 , pp. 503-554
    • Clark, M.R.1
  • 16
    • 0019429025 scopus 로고
    • Separate mechanisms of deformability loss in ATP-depleted and Ca-loaded erythrocytes
    • Clark, M. R., N. Mohandas, C. Feo, and M. S. Jacobs. 1981. Separate mechanisms of deformability loss in ATP-depleted and Ca-loaded erythrocytes. J. Clin. Invest. 67:531-539.
    • (1981) J. Clin. Invest. , vol.67 , pp. 531-539
    • Clark, M.R.1    Mohandas, N.2    Feo, C.3    Jacobs, M.S.4
  • 17
    • 0017172150 scopus 로고
    • Ca binding to the human red cell membrane: Characterization of membrane preparations and binding sites
    • Cohen, C. M., and A. K. Solomon. 1976. Ca binding to the human red cell membrane: characterization of membrane preparations and binding sites. J. Membr. Biol. 29:345-372.
    • (1976) J. Membr. Biol. , vol.29 , pp. 345-372
    • Cohen, C.M.1    Solomon, A.K.2
  • 18
    • 0027938023 scopus 로고
    • Molecular maps of red cell deformation: Hidden elasticity and in situ connectivity
    • Discher, D. E., N. Mohandas, and E. A. Evans. 1994. Molecular maps of red cell deformation: hidden elasticity and in situ connectivity. Science. 266:1032-1035.
    • (1994) Science , vol.266 , pp. 1032-1035
    • Discher, D.E.1    Mohandas, N.2    Evans, E.A.3
  • 19
    • 0001132561 scopus 로고
    • Spectrophotometric studies. XV. Hydration of macro sized crystals of human hemoglobin, and osmotic concentrations in red cells
    • Drabkin, D. L. 1950. Spectrophotometric studies. XV. Hydration of macro sized crystals of human hemoglobin, and osmotic concentrations in red cells. J. Biol. Chem. 185:231-245.
    • (1950) J. Biol. Chem. , vol.185 , pp. 231-245
    • Drabkin, D.L.1
  • 20
    • 0019295798 scopus 로고
    • Anion channel blockade: Effects upon erythrocyte membrane calcium response
    • Eaton, J. W., R. F. Branda, C. Hadland, and K. Dreher. 1980. Anion channel blockade: effects upon erythrocyte membrane calcium response. Am. J. Hematol. 9:391-399.
    • (1980) Am. J. Hematol. , vol.9 , pp. 391-399
    • Eaton, J.W.1    Branda, R.F.2    Hadland, C.3    Dreher, K.4
  • 22
    • 0017195859 scopus 로고
    • The effects of ionophore A23187 on erythrocytes: Relationship of ATP and 2,3-diphosphoglycerate to calcium-binding capacity
    • Edmonson, J. W., and T.-K. Li. 1976. The effects of ionophore A23187 on erythrocytes: relationship of ATP and 2,3-diphosphoglycerate to calcium-binding capacity. Biochim. Biophys. Acta. 443:106-113.
    • (1976) Biochim. Biophys. Acta. , vol.443 , pp. 106-113
    • Edmonson, J.W.1    Li, T.-K.2
  • 23
    • 0024431573 scopus 로고
    • Structure and deformation properties of red blood cells: Concepts and quantitative methods
    • Evans, E. A. 1989. Structure and deformation properties of red blood cells: concepts and quantitative methods. Methods Enzymol. 173:3-35.
    • (1989) Methods Enzymol. , vol.173 , pp. 3-35
    • Evans, E.A.1
  • 24
    • 0026662815 scopus 로고
    • Influence of calcium permeabilization and membrane-attached hemoglobin on erythrocyte deformability
    • Friederichs, E., R. A. Farley, and H. J. Meiselman. 1992. Influence of calcium permeabilization and membrane-attached hemoglobin on erythrocyte deformability. Am. J. Hematol. 41:170-177.
    • (1992) Am. J. Hematol. , vol.41 , pp. 170-177
    • Friederichs, E.1    Farley, R.A.2    Meiselman, H.J.3
  • 26
    • 0000659323 scopus 로고
    • The function of calcium in the potassium permeability of human erythrocytes
    • Gardos, G. 1958. The function of calcium in the potassium permeability of human erythrocytes. Biochim. Biophys. Acta. 30:653-654.
    • (1958) Biochim. Biophys. Acta. , vol.30 , pp. 653-654
    • Gardos, G.1
  • 27
    • 0004217418 scopus 로고    scopus 로고
    • Gustav Fischer Verlag, Jena, Germany
    • Glaser, R. 1996. Biophysik. Gustav Fischer Verlag, Jena, Germany.
    • (1996) Biophysik
    • Glaser, R.1
  • 28
    • 0025173015 scopus 로고
    • Restricted diffusion of integral membrane proteins and polyphosphoinositides leads to their depletion in microvesicles released from human erythrocytes
    • Hagelberg, C., and D. Allan. 1990. Restricted diffusion of integral membrane proteins and polyphosphoinositides leads to their depletion in microvesicles released from human erythrocytes. Biochem. J. 271: 831-834
    • (1990) Biochem. J. , vol.271 , pp. 831-834
    • Hagelberg, C.1    Allan, D.2
  • 29
    • 0014381540 scopus 로고
    • The calcium content of human erythrocytes
    • Harrison, D. G., and C. Long. 1968. The calcium content of human erythrocytes. J. Physiol. 199:367-381.
    • (1968) J. Physiol. , vol.199 , pp. 367-381
    • Harrison, D.G.1    Long, C.2
  • 30
    • 0018913076 scopus 로고
    • Temperature dependence of the viscoelastic recovery of red cell membrane
    • Hochmuth, R. M., K. L. Buxbaum, and E. A. Evans. 1980. Temperature dependence of the viscoelastic recovery of red cell membrane. Biophys. J. 29:177-182.
    • (1980) Biophys. J. , vol.29 , pp. 177-182
    • Hochmuth, R.M.1    Buxbaum, K.L.2    Evans, E.A.3
  • 34
    • 0017338859 scopus 로고
    • Effect of ionophore A23187 upon membrane function and ion movement in human and toad erythrocytes
    • Lake, W., H. Rasmussen, and D. B. P. Goodman. 1977. Effect of ionophore A23187 upon membrane function and ion movement in human and toad erythrocytes. J. Membr. Biol. 32:93-113.
    • (1977) J. Membr. Biol. , vol.32 , pp. 93-113
    • Lake, W.1    Rasmussen, H.2    Goodman, D.B.P.3
  • 36
    • 0019176180 scopus 로고
    • Ionophore A23187-induced calcium permeability of intact human red blood cells
    • Lew, V. L., and L. O. Simonsen. 1980. Ionophore A23187-induced calcium permeability of intact human red blood cells. J. Physiol. 308:60.P
    • (1980) J. Physiol. , vol.308
    • Lew, V.L.1    Simonsen, L.O.2
  • 37
    • 0027527892 scopus 로고
    • Mechanical and geometrical properties of density-separated neonatal and adult erythrocytes
    • Linderkamp, O., E. Friedrichs, and H. J. Meiselman. 1993. Mechanical and geometrical properties of density-separated neonatal and adult erythrocytes. Pediatr. Res. 34:688-693.
    • (1993) Pediatr. Res. , vol.34 , pp. 688-693
    • Linderkamp, O.1    Friedrichs, E.2    Meiselman, H.J.3
  • 38
    • 0015101181 scopus 로고
    • The binding of calcium ions by erythrocytes and 'ghost'-cell membranes
    • Long, C., and B. Mouat. 1971. The binding of calcium ions by erythrocytes and 'ghost'-cell membranes. Biochem. J. 123:829-836.
    • (1971) Biochem. J. , vol.123 , pp. 829-836
    • Long, C.1    Mouat, B.2
  • 40
    • 0022922389 scopus 로고
    • Structure and function of the cytoplasmic domain of band3: Center of erythrocyte membrane-peripheral protein interactions. Biochim
    • Low, P. S. 1986. Structure and function of the cytoplasmic domain of band3: center of erythrocyte membrane-peripheral protein interactions. Biochim. Biophys. Acta. 864:145-167.
    • (1986) Biophys. Acta. , vol.864 , pp. 145-167
    • Low, P.S.1
  • 41
    • 0021323213 scopus 로고
    • An electro-optic study of human erythrocyte spectrin dimers; the presence of Ca ions does not alter spectrin flexibility
    • Mikkelsen, A., B. T. Stokke, and A. Elgsaeter. 1984. An electro-optic study of human erythrocyte spectrin dimers; the presence of Ca ions does not alter spectrin flexibility. Biochim. Biophys. Acta. 786:95-102.
    • (1984) Biochim. Biophys. Acta. , vol.786 , pp. 95-102
    • Mikkelsen, A.1    Stokke, B.T.2    Elgsaeter, A.3
  • 42
    • 0019301261 scopus 로고
    • Changes in surface and volume measured by micropipette aspiration for erythrocytes aging in vivo
    • Nash, G. B., and S. J. Wyard. 1980. Changes in surface and volume measured by micropipette aspiration for erythrocytes aging in vivo. Biorheology. 17:479-484.
    • (1980) Biorheology , vol.17 , pp. 479-484
    • Nash, G.B.1    Wyard, S.J.2
  • 43
    • 0019829471 scopus 로고
    • Erythrocyte membrane elasticity during in vivo aging
    • Nash, G. B., and S. J. Wyard. 1981. Erythrocyte membrane elasticity during in vivo aging. Biochim. Biophys. Acta. 643:269-275.
    • (1981) Biochim. Biophys. Acta. , vol.643 , pp. 269-275
    • Nash, G.B.1    Wyard, S.J.2
  • 44
    • 0018140656 scopus 로고
    • Polymerization of red cell membrane protein contributes to sphero-echinocyte shape irreversibility
    • Palek, J., P. A. Liu, and S. C. Liu. 1978. Polymerization of red cell membrane protein contributes to sphero-echinocyte shape irreversibility. Nature. 274:505-507.
    • (1978) Nature , vol.274 , pp. 505-507
    • Palek, J.1    Liu, P.A.2    Liu, S.C.3
  • 45
    • 0022322068 scopus 로고
    • Early days of protein crystallography
    • Perutz, M. 1985. Early days of protein crystallography. Methods Enzymol. 114:3-18
    • (1985) Methods Enzymol. , vol.114 , pp. 3-18
    • Perutz, M.1
  • 46
    • 0016157532 scopus 로고
    • Influence of globin structure on the state of the heme. II. Allosteric transitions in methemoglobin
    • Perutz, M. F., A. R. Fersht, S. R. Simon, and Roberts, G. C. K. 1974. Influence of globin structure on the state of the heme. II. Allosteric transitions in methemoglobin. Biochemistry. 13:2174-2186.
    • (1974) Biochemistry , vol.13 , pp. 2174-2186
    • Perutz, M.F.1    Fersht, A.R.2    Simon, S.R.3    Roberts, G.C.K.4
  • 47
    • 0020456458 scopus 로고
    • Reduced erythrocyte deformability associated with calcium accumulation
    • O'Rear, E. A., M. M. Udden, L. V. McIntire, and E. C. Lynch. 1982. Reduced erythrocyte deformability associated with calcium accumulation. Biochim. Biophys. Acta. 691:274-280.
    • (1982) Biochim. Biophys. Acta , vol.691 , pp. 274-280
    • O'Rear, E.A.1    Udden, M.M.2    McIntire, L.V.3    Lynch, E.C.4
  • 48
    • 0018941204 scopus 로고
    • Calcium distribution within human erythrocytes
    • Schrier, S. L., M. Johnson, I. Junga, and J. Krueger. 1980. Calcium distribution within human erythrocytes. Blood. 56:667-676.
    • (1980) Blood , vol.56 , pp. 667-676
    • Schrier, S.L.1    Johnson, M.2    Junga, I.3    Krueger, J.4
  • 49
    • 0017588035 scopus 로고
    • Interaction of hemoglobin with red blood cell membranes as shown by a fluorescent chromophore
    • Shaklai, N., J. Yguerabide, and H. M. Ranney. 1977. Interaction of hemoglobin with red blood cell membranes as shown by a fluorescent chromophore. Biochemistry. 16:5585-5592.
    • (1977) Biochemistry , vol.16 , pp. 5585-5592
    • Shaklai, N.1    Yguerabide, J.2    Ranney, H.M.3
  • 50
    • 0021952980 scopus 로고
    • Cell age-dependent changes in deformability and calcium accumulation of human erythrocytes
    • Shiga, T., M. Sekiya, N. Maeda, K. Kon, and M. Okazaki. 1985. Cell age-dependent changes in deformability and calcium accumulation of human erythrocytes. Biochim. Biophys. Acta. 814:289-299.
    • (1985) Biochim. Biophys. Acta , vol.814 , pp. 289-299
    • Shiga, T.1    Sekiya, M.2    Maeda, N.3    Kon, K.4    Okazaki, M.5
  • 52
    • 0019347338 scopus 로고
    • Effects of the calcium-mediated enzymatic cross-linking of membrane proteins on cellular deformability
    • Smith, B. D., P. L. LaCelle, G. E. Siefring, L. Lowe-Krentz, and L. Lorand. 1981. Effects of the calcium-mediated enzymatic cross-linking of membrane proteins on cellular deformability. J. Membr. Biol. 61:75-80.
    • (1981) J. Membr. Biol. , vol.61 , pp. 75-80
    • Smith, B.D.1    LaCelle, P.L.2    Siefring, G.E.3    Lowe-Krentz, L.4    Lorand, L.5
  • 53
    • 0004067948 scopus 로고    scopus 로고
    • Spektrum-Lehrbuch, Heidelberg, Germany
    • Stryer, L. 1996. Biochemie. Spektrum-Lehrbuch, Heidelberg, Germany.
    • (1996) Biochemie
    • Stryer, L.1
  • 56
    • 0026503909 scopus 로고
    • Rheologic properties of senescent erythrocytes: Loss of surface and volume with red blood cell age
    • Waugh, R. E., N. Mohandas, C. W. Jackson, T. J. Mueller, T. Suzuki, and G. L. Dale. 1992. Rheologic properties of senescent erythrocytes: loss of surface and volume with red blood cell age. Blood. 79:1351-1358.
    • (1992) Blood , vol.79 , pp. 1351-1358
    • Waugh, R.E.1    Mohandas, N.2    Jackson, C.W.3    Mueller, T.J.4    Suzuki, T.5    Dale, G.L.6
  • 57
    • 0014506945 scopus 로고
    • Metabolic dependence of red cell deformability
    • Weed, R. I., P. L. LaCelle, and E. W. Merill. 1969. Metabolic dependence of red cell deformability. J. Clin. Imest. 48:795-809.
    • (1969) J. Clin. Imest. , vol.48 , pp. 795-809
    • Weed, R.I.1    LaCelle, P.L.2    Merill, E.W.3
  • 58
    • 0017279642 scopus 로고
    • Scanning electron microscopy of erythrocyte deformation: The influence of a Ca-ionophore A23187
    • White, J. G. 1976. Scanning electron microscopy of erythrocyte deformation: the influence of a Ca-ionophore A23187. Semin. Hematol. 13:121-132.
    • (1976) Semin. Hematol. , vol.13 , pp. 121-132
    • White, J.G.1


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