메뉴 건너뛰기




Volumn 61, Issue 3, 2011, Pages 531-537

Influence of Glucose Concentration on the Membrane Stability of Human Erythrocytes

Author keywords

Erythrocytes; Glucose; Hypotonic lysis; Membrane stability; Osmolytes

Indexed keywords

GLUCOSE; SODIUM CHLORIDE;

EID: 81155131168     PISSN: 10859195     EISSN: None     Source Type: Journal    
DOI: 10.1007/s12013-011-9235-z     Document Type: Article
Times cited : (21)

References (44)
  • 1
    • 0015966621 scopus 로고
    • The salt relations of marine and halophilic species of the intracellular green alga Dunaliella: The role of glycerol as a compatible solute
    • Borowitza, L. J., & Brown, A. D. (1974). The salt relations of marine and halophilic species of the intracellular green alga Dunaliella: The role of glycerol as a compatible solute. Archives of Microbiology, 96, 37-52.
    • (1974) Archives of Microbiology , vol.96 , pp. 37-52
    • Borowitza, L.J.1    Brown, A.D.2
  • 2
    • 0018474573 scopus 로고
    • Solute compatibility with enzyme function and structure: Rationales for the selection of osmotic and end-products of anaerobic metabolism in marine invertebrates
    • Bowlus, R. D., & Somero, G. N. (1979). Solute compatibility with enzyme function and structure: Rationales for the selection of osmotic and end-products of anaerobic metabolism in marine invertebrates. Journal of Experimental Zoology, 208, 137-151.
    • (1979) Journal of Experimental Zoology , vol.208 , pp. 137-151
    • Bowlus, R.D.1    Somero, G.N.2
  • 3
    • 0042404530 scopus 로고
    • Enzyme activities in concentrated solution of glycinebetaine and other solutes
    • Pollard, A., & Wyn-Jones, R. G. (1979). Enzyme activities in concentrated solution of glycinebetaine and other solutes. Planta, 144, 291-298.
    • (1979) Planta , vol.144 , pp. 291-298
    • Pollard, A.1    Wyn-Jones, R.G.2
  • 4
    • 0001784001 scopus 로고
    • Organic osmotic effectors in cartilaginous fishes
    • R. Gilles and M. Gilles-Ballien (Eds.), Berlin: Springer-Verlag
    • Yancey, P. H. (1985). Organic osmotic effectors in cartilaginous fishes. In R. Gilles & M. Gilles-Ballien (Eds.), Transport processes, iono- and osmoregulation (pp. 424-436). Berlin: Springer-Verlag.
    • (1985) Transport Processes, Iono- and Osmoregulation , pp. 424-436
    • Yancey, P.H.1
  • 5
    • 0026631716 scopus 로고
    • Increase thermal stability of proteins in the presence of naturally occurring osmolytes
    • Santoro, M. M., Liu, Y., Khan, S. M. A., Hou, L. X., & Bolen, D. W. (1992). Increase thermal stability of proteins in the presence of naturally occurring osmolytes. Biochemistry, 31, 5278-5283.
    • (1992) Biochemistry , vol.31 , pp. 5278-5283
    • Santoro, M.M.1    Liu, Y.2    Khan, S.M.A.3    Hou, L.X.4    Bolen, D.W.5
  • 6
    • 23044529588 scopus 로고    scopus 로고
    • Water stress, osmolytes and proteins
    • Yancey, P. H. (2001). Water stress, osmolytes and proteins. American Zoologist, 41, 699-709.
    • (2001) American Zoologist , vol.41 , pp. 699-709
    • Yancey, P.H.1
  • 9
    • 0019872622 scopus 로고
    • Mechanism of proteins stabilization by glycerol-preferential hydration in glycerol-water mixtures
    • Gekko, K., & Timasheff, S. N. (1981). Mechanism of proteins stabilization by glycerol-preferential hydration in glycerol-water mixtures. Biochemistry, 20, 4667-4676.
    • (1981) Biochemistry , vol.20 , pp. 4667-4676
    • Gekko, K.1    Timasheff, S.N.2
  • 10
    • 0019872612 scopus 로고
    • Thermodynamic and kinetic examination of proteins stabilization by glycerol
    • Gekko, K., & Timasheff, S. N. (1981). Thermodynamic and kinetic examination of proteins stabilization by glycerol. Biochemistry, 20, 4677-4686.
    • (1981) Biochemistry , vol.20 , pp. 4677-4686
    • Gekko, K.1    Timasheff, S.N.2
  • 13
    • 0027157062 scopus 로고
    • Characterization of organic osmolytes in avian renal medulla-A nonurea osmotic gradient system
    • Lien, Y. H. H., Pacelli, M. M., & Braun, E. J. (1993). Characterization of organic osmolytes in avian renal medulla-A nonurea osmotic gradient system. American Journal of Physiology, 264, R1045-R1049.
    • (1993) American Journal of Physiology , vol.264
    • Lien, Y.H.H.1    Pacelli, M.M.2    Braun, E.J.3
  • 14
    • 0027310845 scopus 로고
    • The control of proteins stability and association by weak-interactions with water-how do solvents affect these processes
    • Timasheff, S. N. (1993). The control of proteins stability and association by weak-interactions with water-how do solvents affect these processes. Annual Review of Biophysics and Biomolecular Structure, 22, 67-97.
    • (1993) Annual Review of Biophysics and Biomolecular Structure , vol.22 , pp. 67-97
    • Timasheff, S.N.1
  • 15
    • 0028862864 scopus 로고
    • The peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes
    • Liu, Y., & Bolen, D. W. (1995). The peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes. Biochemistry, 34, 12884-12891.
    • (1995) Biochemistry , vol.34 , pp. 12884-12891
    • Liu, Y.1    Bolen, D.W.2
  • 17
    • 0030762556 scopus 로고    scopus 로고
    • A naturally occurring protective system in urea-rich cells: Mechanism of osmolyte protection of proteins against urea denaturation
    • Wang, A., & Bolen, D. W. (1997). A naturally occurring protective system in urea-rich cells: Mechanism of osmolyte protection of proteins against urea denaturation. Biochemistry, 36, 9101-9108.
    • (1997) Biochemistry , vol.36 , pp. 9101-9108
    • Wang, A.1    Bolen, D.W.2
  • 18
    • 0031778590 scopus 로고    scopus 로고
    • Control of protein stability and reactions by weakly interacting cosolvents: The simplicity of the complicated
    • Timasheff, S. N. (1998). Control of protein stability and reactions by weakly interacting cosolvents: The simplicity of the complicated. Advances in Protein Chemistry, 51, 355-432.
    • (1998) Advances in Protein Chemistry , vol.51 , pp. 355-432
    • Timasheff, S.N.1
  • 19
    • 0037162456 scopus 로고    scopus 로고
    • Protein-solvent preferential interactions, protein hydration, and the modulation of biochemical reactions by solvent components
    • Timasheff, S. N. (2002). Protein-solvent preferential interactions, protein hydration, and the modulation of biochemical reactions by solvent components. Proceedings of the National Academy of Sciences of the United States of America, 99, 9721-9726.
    • (2002) Proceedings of the National Academy of Sciences of the United States of America , vol.99 , pp. 9721-9726
    • Timasheff, S.N.1
  • 20
    • 0021173565 scopus 로고
    • Comparison of the cryoprotection of red blood cells by 1,2-propanediol and glycerol
    • Boutron, P., & Arnaud, F. (1984). Comparison of the cryoprotection of red blood cells by 1, 2-propanediol and glycerol. Cryobiology, 21, 348-358.
    • (1984) Cryobiology , vol.21 , pp. 348-358
    • Boutron, P.1    Arnaud, F.2
  • 21
    • 0031229704 scopus 로고    scopus 로고
    • In vitro study of the effect of trehalose and dextran during freezing of human red blood cells in liquid nitrogen
    • Pellerin-Mendes, C., Million, L., Marchand-Arvier, M., Labrude, P., & Vigneron, C. (1997). In vitro study of the effect of trehalose and dextran during freezing of human red blood cells in liquid nitrogen. Cryobiology, 35, 173-186.
    • (1997) Cryobiology , vol.35 , pp. 173-186
    • Pellerin-Mendes, C.1    Million, L.2    Marchand-Arvier, M.3    Labrude, P.4    Vigneron, C.5
  • 22
    • 0036822978 scopus 로고    scopus 로고
    • Biochemical stabilization enhances red blood cell recovery and stability following cryopreservation
    • Wagner, C. T., Martowicz, M. L., Livesey, S. A., & Connor, J. (2002). Biochemical stabilization enhances red blood cell recovery and stability following cryopreservation. Cryobiology, 45, 153-166.
    • (2002) Cryobiology , vol.45 , pp. 153-166
    • Wagner, C.T.1    Martowicz, M.L.2    Livesey, S.A.3    Connor, J.4
  • 23
    • 17444392867 scopus 로고    scopus 로고
    • Biopreservation of red blood cells: Past, present, and future
    • Scott, K. L., Lecak, J., & Acker, J. P. (2005). Biopreservation of red blood cells: Past, present, and future. Transfusion Medicine Reviews, 19, 127-142.
    • (2005) Transfusion Medicine Reviews , vol.19 , pp. 127-142
    • Scott, K.L.1    Lecak, J.2    Acker, J.P.3
  • 24
    • 37249055045 scopus 로고    scopus 로고
    • Influence of aqueous crude extracts of medicinal plants on the osmotic stability of human erythrocytes
    • de Freitas, M. V., Netto, R. C. M., Huss, J. C. C., de Souza, T. M. T., Costa, J. O., Firmino, C. B., et al. (2008). Influence of aqueous crude extracts of medicinal plants on the osmotic stability of human erythrocytes. Toxicology in Vitro, 22, 219-224.
    • (2008) Toxicology in Vitro , vol.22 , pp. 219-224
    • de Freitas, M.V.1    Netto, R.C.M.2    Huss, J.C.C.3    de Souza, T.M.T.4    Costa, J.O.5    Firmino, C.B.6
  • 30
    • 77954309206 scopus 로고    scopus 로고
    • The approximate entropy of the electromyographic signals of tremor correlates with the osmotic fragility of human erythrocytes
    • Mansur, P. H. G., Cury, L. K. P., Leite, J. O. B., Pereira, A. A., Penha-Silva, N., & Andrade, A. O. (2010). The approximate entropy of the electromyographic signals of tremor correlates with the osmotic fragility of human erythrocytes. BioMedical Engineering OnLine, 9, 29.
    • (2010) BioMedical Engineering OnLine , vol.9 , pp. 29
    • Mansur, P.H.G.1    Cury, L.K.P.2    Leite, J.O.B.3    Pereira, A.A.4    Penha-Silva, N.5    Andrade, A.O.6
  • 33
    • 33745117269 scopus 로고    scopus 로고
    • Effects of the solvent composition on the stability of proteins in aqueous solutions
    • Fonseca, L. C., Correa, N. C. R., Garrote, M. D., Cunha, C. C., & Penha-Silva, N. (2006). Effects of the solvent composition on the stability of proteins in aqueous solutions. Química Nova, 29, 543-548.
    • (2006) Química Nova , vol.29 , pp. 543-548
    • Fonseca, L.C.1    Correa, N.C.R.2    Garrote, M.D.3    Cunha, C.C.4    Penha-Silva, N.5
  • 34
    • 0035958656 scopus 로고    scopus 로고
    • The osmophobic effect: Natural selection of a thermodynamic force in protein folding
    • Bolen, D. W., & Baskakov, I. V. (2001). The osmophobic effect: Natural selection of a thermodynamic force in protein folding. Journal of Molecular Biology, 310, 955-963.
    • (2001) Journal of Molecular Biology , vol.310 , pp. 955-963
    • Bolen, D.W.1    Baskakov, I.V.2
  • 35
    • 0028787409 scopus 로고
    • Effects of a naturally-occurring compatible osmolyte on the internal dynamics of ribonuclease-A
    • Wang, A., Robertson, A. D., & Bolen, D. W. (1995). Effects of a naturally-occurring compatible osmolyte on the internal dynamics of ribonuclease-A. Biochemistry, 34, 15096-15104.
    • (1995) Biochemistry , vol.34 , pp. 15096-15104
    • Wang, A.1    Robertson, A.D.2    Bolen, D.W.3
  • 38
    • 0029970223 scopus 로고    scopus 로고
    • Effects of alkanols, alkanediols and glycerol on red blood cell shape and hemolysis
    • Bakaltcheva, I. B., Odeyale, C. O., & Spargo, B. J. (1996). Effects of alkanols, alkanediols and glycerol on red blood cell shape and hemolysis. Biochimica et Biophysica Acta, 1280, 73-80.
    • (1996) Biochimica Et Biophysica Acta , vol.1280 , pp. 73-80
    • Bakaltcheva, I.B.1    Odeyale, C.O.2    Spargo, B.J.3
  • 39
    • 0027620010 scopus 로고
    • Osmotic effects of dilution on erythrocytes after freezing and thawing in glycerol-containing buffer
    • De Loecker, R., Gossens, W., van Duppen, V., Verwilghen, R., & De Loecker, W. (1993). Osmotic effects of dilution on erythrocytes after freezing and thawing in glycerol-containing buffer. Cryobiology, 30, 279-285.
    • (1993) Cryobiology , vol.30 , pp. 279-285
    • de Loecker, R.1    Gossens, W.2    van Duppen, V.3    Verwilghen, R.4    de Loecker, W.5
  • 41
    • 33846065565 scopus 로고    scopus 로고
    • Correlation between erythrocytes deformability and size: A study using a microchannel based cell analyzer
    • Bransky, A., Korin, N., Nemirovski, Y., & Dinnar, U. (2007). Correlation between erythrocytes deformability and size: A study using a microchannel based cell analyzer. Microvascular Research, 73, 7-13.
    • (2007) Microvascular Research , vol.73 , pp. 7-13
    • Bransky, A.1    Korin, N.2    Nemirovski, Y.3    Dinnar, U.4
  • 42
    • 0034973280 scopus 로고    scopus 로고
    • Protein function at thermal extremes: Balancing stability and flexibility
    • Fields, P. A. (2001). Protein function at thermal extremes: Balancing stability and flexibility. Comparative Biochemistry and Physiology Part A, 129, 417-431.
    • (2001) Comparative Biochemistry and Physiology Part A , vol.129 , pp. 417-431
    • Fields, P.A.1
  • 43
    • 0030462212 scopus 로고    scopus 로고
    • Effects of lost surface area on red blood cells and red blood cell survival in mice
    • Waugh, R. E., & Sarelius, I. H. (1996). Effects of lost surface area on red blood cells and red blood cell survival in mice. American Journal of Physiology, 271, C1847-C1852.
    • (1996) American Journal of Physiology , vol.271
    • Waugh, R.E.1    Sarelius, I.H.2
  • 44
    • 0026503909 scopus 로고
    • Rheologic properties of senescent erythrocytes: Loss of surface area and volume with red blood cell age
    • Waugh, R. E., Narla, M., Jackson, C. W., Mueller, T. J., Suzuki, T., & Dale, G. L. (1992). Rheologic properties of senescent erythrocytes: Loss of surface area and volume with red blood cell age. Blood, 79, 1351-1358.
    • (1992) Blood , vol.79 , pp. 1351-1358
    • Waugh, R.E.1    Narla, M.2    Jackson, C.W.3    Mueller, T.J.4    Suzuki, T.5    Dale, G.L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.