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Volumn 16, Issue 1, 2003, Pages 19-28

Saturation transfer in human red blood cells with normal and unstable hemoglobin

Author keywords

Aggregation of hemoglobin; Human red blood cells; Hydration; Methemoglobin; Saturation transfer

Indexed keywords

AGGLOMERATION; BLOOD; MAGNETIZATION; PROTEINS; PROTON IRRADIATION;

EID: 0037292139     PISSN: 09523480     EISSN: None     Source Type: Journal    
DOI: 10.1002/nbm.808     Document Type: Article
Times cited : (6)

References (51)
  • 1
    • 0025139884 scopus 로고
    • Oxidative denaturation in hemolytic anemia
    • Winterbourn CC. Oxidative denaturation in hemolytic anemia. Semin. Hematol. 1990; 27: 41-50.
    • (1990) Semin. Hematol. , vol.27 , pp. 41-50
    • Winterbourn, C.C.1
  • 4
    • 0028025706 scopus 로고
    • Causal role of dense microspherocytes in the anemia of hereditary spherocytosis: Clinical importance of filterability measurements through 3-μm pores
    • Hasegawa S, Nomura T, Iino M, Shio H, Schecter AN, Uyesaka N. Causal role of dense microspherocytes in the anemia of hereditary spherocytosis: Clinical importance of filterability measurements through 3-μm pores. Clin. Hemorheol. 1994; 14: 571-584.
    • (1994) Clin. Hemorheol. , vol.14 , pp. 571-584
    • Hasegawa, S.1    Nomura, T.2    Iino, M.3    Shio, H.4    Schecter, A.N.5    Uyesaka, N.6
  • 5
    • 0028145749 scopus 로고
    • Rheologic and pathophysiologic significance of red cell passage through narrow pores
    • Nakamura T, Hasegawa S, Shio H, Uyesaka N. Rheologic and pathophysiologic significance of red cell passage through narrow pores. Blood Cells 1994; 20: 151-165.
    • (1994) Blood Cells , vol.20 , pp. 151-165
    • Nakamura, T.1    Hasegawa, S.2    Shio, H.3    Uyesaka, N.4
  • 6
    • 0029016063 scopus 로고
    • Contribution of sickle hemoglobin polymer and cell membranes to impaired filterability
    • (Heart Circ. Physiol. 37)
    • Hiruma H, Noguchi CT, Uyesaka N, Schechter AN, Rodgers GP. Contribution of sickle hemoglobin polymer and cell membranes to impaired filterability. Am. J. Physiol. 1995; 268 (Heart Circ. Physiol. 37): H2003-H2008.
    • (1995) Am. J. Physiol. , vol.268
    • Hiruma, H.1    Noguchi, C.T.2    Uyesaka, N.3    Schechter, A.N.4    Rodgers, G.P.5
  • 7
    • 0031408172 scopus 로고    scopus 로고
    • 2+ influx and c-AMP-mediated signaling pathway
    • (Cell Physiol. 42)
    • 2+ influx and c-AMP-mediated signaling pathway. Am. J. Physiol. 1997; 273 (Cell Physiol. 42): C1828-C1834.
    • (1997) Am. J. Physiol. , vol.273
    • Oonishi, T.1    Sakashita, K.2    Uyesaka, N.3
  • 8
    • 0001818023 scopus 로고
    • Longitudinal relaxation of protons under cross saturation
    • Akasaka K. Longitudinal relaxation of protons under cross saturation. J. Magn. Reson. 1981; 45: 337-343.
    • (1981) J. Magn. Reson. , vol.45 , pp. 337-343
    • Akasaka, K.1
  • 9
    • 0002316964 scopus 로고
    • Spin diffusion and dynamic structure of protein
    • Akasaka K. Spin diffusion and dynamic structure of protein. J. Magn. Reson. 1983; 51: 14-25.
    • (1983) J. Magn. Reson. , vol.51 , pp. 14-25
    • Akasaka, K.1
  • 10
    • 0001133187 scopus 로고
    • Proton spin relaxation in biopolymer system
    • Akasaka K, Ishima R, Shibata S. Proton spin relaxation in biopolymer system. Physica B 1990; 164: 163-179.
    • (1990) Physica B , vol.164 , pp. 163-179
    • Akasaka, K.1    Ishima, R.2    Shibata, S.3
  • 20
    • 0024573913 scopus 로고
    • Magnetization transfer contrast (MTC) and tissue water proton relaxation in vivo
    • Wolff SD, Balaban RS. Magnetization transfer contrast (MTC) and tissue water proton relaxation in vivo. Magn. Reson. Med. 1989; 10: 135-144.
    • (1989) Magn. Reson. Med. , vol.10 , pp. 135-144
    • Wolff, S.D.1    Balaban, R.S.2
  • 21
    • 0025925024 scopus 로고
    • Quantitative 1H magnetization transfer imaging in vivo
    • Eng J, Ceckler TL, Balaban RS. Quantitative 1H magnetization transfer imaging in vivo. Magn. Reson. Med. 1991; 17: 304-314.
    • (1991) Magn. Reson. Med. , vol.17 , pp. 304-314
    • Eng, J.1    Ceckler, T.L.2    Balaban, R.S.3
  • 22
    • 0026877440 scopus 로고
    • Magnetization transfer contrast in magnetic resonance imaging
    • Balaban RS, Ceckler TL. Magnetization transfer contrast in magnetic resonance imaging. Magn. Reson. Q. 1992; 8: 116-137.
    • (1992) Magn. Reson. Q. , vol.8 , pp. 116-137
    • Balaban, R.S.1    Ceckler, T.L.2
  • 23
    • 0000949403 scopus 로고
    • Rotating frame and magnetization transfer
    • Stark DD, Bradley WG (eds). Mosby-Yearbook: St Louis, MO
    • Sepponen RE. Rotating frame and magnetization transfer. In Magnetic Resonance Imaging, Stark DD, Bradley WG (eds). Mosby-Yearbook: St Louis, MO, 1992; 204-218.
    • (1992) Magnetic Resonance Imaging , pp. 204-218
    • Sepponen, R.E.1
  • 25
    • 0034769163 scopus 로고    scopus 로고
    • Basic studies on the equivalent cross-relaxation rate imaging (equivalent CRI) - Phantom studies
    • Sogami M, Era S, Kinosada Y, Matsushima S, Kato K, Tomida M, Hirabayashi T. Basic studies on the equivalent cross-relaxation rate imaging (equivalent CRI) - phantom studies. NMR Biomed. 2001; 14: 367-375.
    • (2001) NMR Biomed. , vol.14 , pp. 367-375
    • Sogami, M.1    Era, S.2    Kinosada, Y.3    Matsushima, S.4    Kato, K.5    Tomida, M.6    Hirabayashi, T.7
  • 26
    • 0034544023 scopus 로고    scopus 로고
    • Saturation transfer ratio in magnetic resonance imaging. A novel physical parameter for evaluation of the hydrophobicity of synthetic copolymer gels
    • Matsushima M, Takasu A, Inai Y, Hirabayashi T, Era S, Sogami M, Kinosada Y. Saturation transfer ratio in magnetic resonance imaging. A novel physical parameter for evaluation of the hydrophobicity of synthetic copolymer gels. Polym. J. 2000; 32: 828-833.
    • (2000) Polym. J. , vol.32 , pp. 828-833
    • Matsushima, M.1    Takasu, A.2    Inai, Y.3    Hirabayashi, T.4    Era, S.5    Sogami, M.6    Kinosada, Y.7
  • 27
    • 0035025870 scopus 로고    scopus 로고
    • Equivalent cross-relaxation rate in magnetic resonance imaging. A novel physical parameter for evaluation of conditions of water in synthetic copolymer gels
    • Matsushima S, Takasu A, Inai Y, Hirabayashi T, Era S, Sogami M, Kinosada Y. Equivalent cross-relaxation rate in magnetic resonance imaging. A novel physical parameter for evaluation of conditions of water in synthetic copolymer gels. Polym. J. 2001; 33: 236-241.
    • (2001) Polym. J. , vol.33 , pp. 236-241
    • Matsushima, S.1    Takasu, A.2    Inai, Y.3    Hirabayashi, T.4    Era, S.5    Sogami, M.6    Kinosada, Y.7
  • 28
    • 0023698083 scopus 로고
    • Human erythrocyte cross-linked with glutaraldehyde - General properties and significance as a blood substitute
    • Bellelli A, Bendetti PL, Coletta M, Ippoliti R, Brunori M. Human erythrocyte cross-linked with glutaraldehyde - general properties and significance as a blood substitute. Biochem. Biophys. Res. Commun. 1988; 156: 970-977.
    • (1988) Biochem. Biophys. Res. Commun. , vol.156 , pp. 970-977
    • Bellelli, A.1    Bendetti, P.L.2    Coletta, M.3    Ippoliti, R.4    Brunori, M.5
  • 29
    • 0028783566 scopus 로고
    • Superoxide dismutase and catalase cross-linked to polyhemoglobin reduces to methemoglobin formation in vitro
    • Quebec EA, Chang TMS. Superoxide dismutase and catalase cross-linked to polyhemoglobin reduces to methemoglobin formation in vitro. Artif. Cells, Blood Subs. Immob. Biotech. 1995; 23: 693-705.
    • (1995) Artif. Cells, Blood Subs. Immob. Biotech. , vol.23 , pp. 693-705
    • Quebec, E.A.1    Chang, T.M.S.2
  • 31
    • 0030332443 scopus 로고    scopus 로고
    • Orientation of glutaraldehyde-fixed erythrocytes in strong static magnetic fields
    • Higashi T, Segawa S, Ashida N, Takeuchi T. Orientation of glutaraldehyde-fixed erythrocytes in strong static magnetic fields. Bioelectromagnetics 1996; 17: 335-338.
    • (1996) Bioelectromagnetics , vol.17 , pp. 335-338
    • Higashi, T.1    Segawa, S.2    Ashida, N.3    Takeuchi, T.4
  • 32
    • 0031190905 scopus 로고    scopus 로고
    • Orientation of blood cells in static magnetic field
    • Higashi T, Ashida N, Takeuchi T. Orientation of blood cells in static magnetic field. Physica B 1997; 237-238: 616-620.
    • (1997) Physica B , vol.237-238 , pp. 616-620
    • Higashi, T.1    Ashida, N.2    Takeuchi, T.3
  • 33
    • 0021359076 scopus 로고
    • Acute intravascular hemolysis due to accidental formalin intoxication during hemodialysis
    • Pun KK, Yeung CK, Chan TK. Acute intravascular hemolysis due to accidental formalin intoxication during hemodialysis. Clin. Nephrol. 1984; 21: 188-190.
    • (1984) Clin. Nephrol. , vol.21 , pp. 188-190
    • Pun, K.K.1    Yeung, C.K.2    Chan, T.K.3
  • 34
    • 0021144921 scopus 로고
    • Reaction of phenylhydrazine with erythrocyte - Cross-linking of spectrin by disulfide exchange with oxidized hemoglobin
    • Vilsen B, Nielsen H. Reaction of phenylhydrazine with erythrocyte - Cross-linking of spectrin by disulfide exchange with oxidized hemoglobin. Biochem. Pharmac. 1984; 33: 2739-2748.
    • (1984) Biochem. Pharmac. , vol.33 , pp. 2739-2748
    • Vilsen, B.1    Nielsen, H.2
  • 35
    • 0012202373 scopus 로고
    • Quantitative relationship between Heinz body formation and red blood cell deformability
    • Reinhart WH, Sung LA, Chien S. Quantitative relationship between Heinz body formation and red blood cell deformability. Blood 1986; 33: 2739-2748.
    • (1986) Blood , vol.33 , pp. 2739-2748
    • Reinhart, W.H.1    Sung, L.A.2    Chien, S.3
  • 36
    • 0026680709 scopus 로고
    • Iron release and membrane damage in erythrocytes exposed to oxidizing agents, phenylhydrazine, divicine and isouramil
    • Ferrali M, Signorini C, Ciccoli L, Comporiti M. Iron release and membrane damage in erythrocytes exposed to oxidizing agents, phenylhydrazine, divicine and isouramil. Biochem. J. 1992; 285: 295-301.
    • (1992) Biochem. J. , vol.285 , pp. 295-301
    • Ferrali, M.1    Signorini, C.2    Ciccoli, L.3    Comporiti, M.4
  • 37
    • 0027990920 scopus 로고
    • Iron release, lipid peroxidation, and morphological alterations of erythrocytes exposed to acrolein and phenylhydrazine
    • Ciccoli L, Signorini C, Alesandrini C, Ferrali M, Comporti M. Iron release, lipid peroxidation, and morphological alterations of erythrocytes exposed to acrolein and phenylhydrazine. Exp. Mol. Pathol. 1994; 60: 108-118.
    • (1994) Exp. Mol. Pathol. , vol.60 , pp. 108-118
    • Ciccoli, L.1    Signorini, C.2    Alesandrini, C.3    Ferrali, M.4    Comporti, M.5
  • 38
  • 39
    • 0012201248 scopus 로고
    • Identical substitution in Hb Ube-1 and Hb Koeln
    • Ohba Y, Miyaji T, Shibata S. Identical substitution in Hb Ube-1 and Hb Koeln. Nature [New Biol.] 1966; 243: 205-207.
    • (1966) Nature [New Biol.] , vol.243 , pp. 205-207
    • Ohba, Y.1    Miyaji, T.2    Shibata, S.3
  • 40
    • 0018074909 scopus 로고
    • Selective spin diffusion. A novel method for studying motional properties of biopolymer in solution
    • Akasaka K, Konrad M, Goody RS. Selective spin diffusion. A novel method for studying motional properties of biopolymer in solution. FEBS Lett. 1978; 96: 287-290.
    • (1978) FEBS Lett. , vol.96 , pp. 287-290
    • Akasaka, K.1    Konrad, M.2    Goody, R.S.3
  • 41
    • 0003739602 scopus 로고
    • Unstable hemoglobin variants - Congenital Heinz body hemolytic anemia
    • W. B. Saunders: Philadelphia, PA
    • Bunn HF, Forget BG. Unstable hemoglobin variants - congenital Heinz body hemolytic anemia. In Hemoglobin: Molecular, Genetic and Clinical Aspect. W. B. Saunders: Philadelphia, PA, 1986; 565-594.
    • (1986) Hemoglobin: Molecular, Genetic and Clinical Aspect , pp. 565-594
    • Bunn, H.F.1    Forget, B.G.2
  • 42
    • 0028848145 scopus 로고
    • Spin-lattice relaxation times of water in polarized and depolarized rabbit vagus nerves
    • Kuwata K, Ueki S, Era S, Sogami M, Watari H. Spin-lattice relaxation times of water in polarized and depolarized rabbit vagus nerves. Biochem. Biophys. Res. Commun. 1995; 215: 459-466.
    • (1995) Biochem. Biophys. Res. Commun. , vol.215 , pp. 459-466
    • Kuwata, K.1    Ueki, S.2    Era, S.3    Sogami, M.4    Watari, H.5
  • 43
    • 0000769635 scopus 로고
    • Intermolecular spin diffusion as a method for studying macromolecule-ligand interactions
    • Akasaka K. Intermolecular spin diffusion as a method for studying macromolecule-ligand interactions. J. Magn. Reson. 1979; 36: 135-140.
    • (1979) J. Magn. Reson. , vol.36 , pp. 135-140
    • Akasaka, K.1
  • 44
    • 49349118272 scopus 로고
    • The measurement of cross-relaxation effects in the proton NMR spin-lattice relaxation of water in biological system: Hydrated collagen and muscle
    • Edzes HT, Samulski ET. The measurement of cross-relaxation effects in the proton NMR spin-lattice relaxation of water in biological system: hydrated collagen and muscle. J. Magn. Reson. 1978; 31: 207-229.
    • (1978) J. Magn. Reson. , vol.31 , pp. 207-229
    • Edzes, H.T.1    Samulski, E.T.2
  • 45
    • 0006021462 scopus 로고
    • The reaction of formaldehyde with protein. V. Cross-linking between amino and primary amide or guanydyl groups
    • Fraenkel-Conrat H, Olcott HS. The reaction of formaldehyde with protein. V. Cross-linking between amino and primary amide or guanydyl groups. J. Am. Chem. Soc. 1948; 70: 2673-2684.
    • (1948) J. Am. Chem. Soc. , vol.70 , pp. 2673-2684
    • Fraenkel-Conrat, H.1    Olcott, H.S.2
  • 46
    • 0003981338 scopus 로고
    • Histological Techniques
    • Blackith RB, Kovoor A. (transl.). Masson and Springer: New York
    • Gabe M. Histological Techniques, Blackith RB, Kovoor A. (transl.). Masson and Springer: New York, 1976; 30-65.
    • (1976) , pp. 30-65
    • Gabe, M.1
  • 47
    • 0014414239 scopus 로고
    • Glutaraldehyde as a protein cross-linking reagent
    • Richard FM, Knowles JR. Glutaraldehyde as a protein cross-linking reagent. J. Mol. Biol. 1968; 37: 231-233.
    • (1968) J. Mol. Biol. , vol.37 , pp. 231-233
    • Richard, F.M.1    Knowles, J.R.2
  • 48
    • 0014977399 scopus 로고
    • Quantitation of human red blood cell fixation by glutaraldehyde
    • Morel FM, Baker RF, Wayland H. Quantitation of human red blood cell fixation by glutaraldehyde. J. Cell Biol. 1971; 48: 91-100.
    • (1971) J. Cell Biol. , vol.48 , pp. 91-100
    • Morel, F.M.1    Baker, R.F.2    Wayland, H.3
  • 51
    • 0000202632 scopus 로고    scopus 로고
    • Multinuclear relaxation dispersion studies of protein hydration
    • Structure Computation and Dynamics in Protein NMR, Krishner NR, Berliner LJ (eds). Kluwer Academic/Plenum: New York
    • Halle B, Denisov VP, Venu K. Multinuclear relaxation dispersion studies of protein hydration. In Biological Magnetic Resonance. Structure Computation and Dynamics in Protein NMR, Krishner NR, Berliner LJ (eds). Kluwer Academic/Plenum: New York, 1999; 17: 419-484.
    • (1999) Biological Magnetic Resonance , vol.17 , pp. 419-484
    • Halle, B.1    Denisov, V.P.2    Venu, K.3


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