메뉴 건너뛰기




Volumn 25, Issue 6, 2009, Pages 1803-1809

The quaternary structure of tetrameric hemoglobin regulates the oxygen affinity of polymerized hemoglobin

Author keywords

Blood substitute; Cross link; Glutaraldehyde; Hemoglobin; Oxygen carrier; Polymerization; Polymerized hemoglobin; Quaternary structure

Indexed keywords

CROSS-LINK; GLUTARALDEHYDES; OXYGEN CARRIER; POLYMERIZED HEMOGLOBIN; QUATERNARY STRUCTURE;

EID: 73249136130     PISSN: 87567938     EISSN: None     Source Type: Journal    
DOI: 10.1002/btpr.265     Document Type: Article
Times cited : (18)

References (35)
  • 1
    • 73249133205 scopus 로고    scopus 로고
    • Oxidation of hemoglobin: Mechanisms of control in vitro and in vivo
    • Buehler JH, Alayash AI. Oxidation of hemoglobin: mechanisms of control in vitro and in vivo. Transfus Altern Transfus Med. 2007;9:204-212.
    • (2007) Transfus Altern Transfus Med , vol.9 , pp. 204-212
    • Buehler, J.H.1    Alayash, A.I.2
  • 2
    • 0035465476 scopus 로고    scopus 로고
    • Oxygen carriers (''blood substitutes'')-raison d'etre, chemistry, and some physiology
    • Riess JG. Oxygen carriers (''blood substitutes'')-raison d'etre, chemistry, and some physiology. Chem Rev. 2001;101:2797-2920.
    • (2001) Chem Rev , vol.101 , pp. 2797-2920
    • Riess, J.G.1
  • 3
    • 0001166627 scopus 로고
    • Clinical experience with hemoglobin-saline solutions
    • Amberson WR, Jennings JJ, Rhode CM. Clinical experience with hemoglobin-saline solutions. J Appl Physiol. 1949;1:469-489.
    • (1949) J Appl Physiol , vol.1 , pp. 469-489
    • Amberson, W.R.1    Jennings, J.J.2    Rhode, C.M.3
  • 4
    • 52049095278 scopus 로고    scopus 로고
    • Peroxidase activity of hemoglobin towards ascor-bate and urate: A synergistic protective strategy against toxicity of hemoglobin-based oxygen carriers (HBOC)
    • Cooper CE, Silaghi-Dumitrescu R, Rukengwa M, Alayash AI, Buehler PW. Peroxidase activity of hemoglobin towards ascor-bate and urate: a synergistic protective strategy against toxicity of hemoglobin-based oxygen carriers (HBOC). Biochim Biophys Acta. 2008;1784:1415-1420.
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 1415-1420
    • Cooper, C.E.1    Silaghi-Dumitrescu, R.2    Rukengwa, M.3    Alayash, A.I.4    Buehler, P.W.5
  • 6
    • 0028797258 scopus 로고
    • Effects of intra- and intermolecular crosslinking on the free radical reactions of bovine hemoglobins
    • Alayash AI. Effects of intra- and intermolecular crosslinking on the free radical reactions of bovine hemoglobins. Free Radic Biol Med. 1995;18:295-301.
    • (1995) Free Radic Biol Med , vol.18 , pp. 295-301
    • Alayash, A.I.1
  • 7
    • 33751171092 scopus 로고    scopus 로고
    • Molecular volume and HBOC-induced vasoconstriction
    • Palmer AF. Molecular volume and HBOC-induced vasoconstriction. Blood. 2006;108:3231-3232.
    • (2006) Blood , vol.108 , pp. 3231-3232
    • Palmer, A.F.1
  • 8
    • 0037885022 scopus 로고    scopus 로고
    • Current status of blood substitute research: Towards a new paradigm
    • Winslow RM. Current status of blood substitute research: towards a new paradigm. J Intern Med. 2003;253:508-517.
    • (2003) J Intern Med , vol.253 , pp. 508-517
    • Winslow, R.M.1
  • 10
    • 0014310023 scopus 로고
    • Reaction of proteins with glutaraldehyde
    • Habeeb AJ, Hiramoto R. Reaction of proteins with glutaraldehyde. Arch Biochem Biophys. 1968;126:16-26.
    • (1968) Arch Biochem Biophys , vol.126 , pp. 16-26
    • Habeeb, A.J.1    Hiramoto, R.2
  • 11
    • 0007763432 scopus 로고    scopus 로고
    • Hemorrhagic disorders after administration of glutaraldehydepolymerized hemoglobin
    • In: Vandegriff K, Intaglietta RWM, editors., Boston: Birkhauser
    • Bleeker W, Agterberg J, Hey EL, Rigter G, Zappeij L, Bakker J. Hemorrhagic disorders after administration of glutaraldehydepolymerized hemoglobin. In: Vandegriff K, Intaglietta RWM, editors. Blood Substitutes: New Challenges. Boston: Birkhauser; 1996:112-123.
    • (1996) Blood Substitutes: New Challenges , pp. 112-123
    • Bleeker, W.1    Agterberg, J.2    Hey, E.L.3    Rigter, G.4    Zappeij, L.5    Bakker, J.6
  • 12
    • 20444385158 scopus 로고    scopus 로고
    • Structural and functional characterization of glutaraldehyde-polymerized bovine hemoglobin and its isolated fractions
    • Buehler PW, Boykins RA, Jia Y, Norris S, Freedberg DI, Alayash AI. Structural and functional characterization of glutaraldehyde-polymerized bovine hemoglobin and its isolated fractions. Anal Chem. 2005;77:3466-3478.
    • (2005) Anal Chem , vol.77 , pp. 3466-3478
    • Buehler, P.W.1    Boykins, R.A.2    Jia, Y.3    Norris, S.4    Freedberg, D.I.5    Alayash, A.I.6
  • 13
    • 52949142206 scopus 로고    scopus 로고
    • HBOC-201, hemoglobin glutamer-250 (bovine), hemopure (Biopure Corporation)
    • Jahr JS, Moallempour M, Lim JC. HBOC-201, hemoglobin glutamer-250 (bovine), hemopure (Biopure Corporation). Expert Opin Biol Ther. 2008;8:1425-1433.
    • (2008) Expert Opin Biol Ther , vol.8 , pp. 1425-1433
    • Jahr, J.S.1    Moallempour, M.2    Lim, J.C.3
  • 15
    • 33947420123 scopus 로고    scopus 로고
    • Bovine hemoglobin (glutamer-250, Hemopure)-specific immunoglobulin G antibody cross-reacts with human hemoglobin but does not lyse red blood cells in vitro
    • Hamilton RG, Kickler TS. Bovine hemoglobin (glutamer-250, Hemopure)-specific immunoglobulin G antibody cross-reacts with human hemoglobin but does not lyse red blood cells in vitro. Transfusion. 2007;47:723-728.
    • (2007) Transfusion , vol.47 , pp. 723-728
    • Hamilton, R.G.1    Kickler, T.S.2
  • 16
    • 34347406960 scopus 로고    scopus 로고
    • Hemopure transfusion in a child with severe anemia
    • Stefan DC, Uys R, Wessels G. Hemopure transfusion in a child with severe anemia. Pediatr Hematol Oncol. 2007;24:269-273.
    • (2007) Pediatr Hematol Oncol , vol.24 , pp. 269-273
    • Stefan, D.C.1    Uys, R.2    Wessels, G.3
  • 17
    • 33750477989 scopus 로고    scopus 로고
    • Blood substitutes: From chemistry to clinic
    • Lowe KC. Blood substitutes: from chemistry to clinic. J Mater Chem. 2006;16:4189-4196.
    • (2006) J Mater Chem , vol.16 , pp. 4189-4196
    • Lowe, K.C.1
  • 18
    • 34548140080 scopus 로고    scopus 로고
    • Purification of bovine hemoglobin via fast performance liquid chromatography
    • Dimino ML, Palmer AF. Purification of bovine hemoglobin via fast performance liquid chromatography. J Chromatogr B Analyt Technol Biomed Life Sci. 2007;856:353-357.
    • (2007) J Chromatogr B Analyt Technol Biomed Life Sci , vol.856 , pp. 353-357
    • Dimino, M.L.1    Palmer, A.F.2
  • 19
    • 64549100352 scopus 로고    scopus 로고
    • Tangential flow filtration of hemoglobin
    • Palmer AF, Sun G, Harris DR. Tangential flow filtration of hemoglobin. Biotechnol Prog. 2009;25:189-199.
    • (2009) Biotechnol Prog , vol.25 , pp. 189-199
    • Palmer, A.F.1    Sun, G.2    Harris, D.R.3
  • 20
    • 42749087930 scopus 로고    scopus 로고
    • Preparation of ultrapure bovine and human hemoglobin by anion exchange chromatography
    • Sun G, Palmer AF. Preparation of ultrapure bovine and human hemoglobin by anion exchange chromatography. J Chromatogr B. 2008;867:1-7.
    • (2008) J Chromatogr B , vol.867 , pp. 1-7
    • Sun, G.1    Palmer, A.F.2
  • 21
    • 70350157023 scopus 로고    scopus 로고
    • Purification of hemoglobin by tangential flow filtration with diafiltration
    • In press
    • Elmer J, Harris DR, Sun G, Palmer AF. Purification of hemoglobin by tangential flow filtration with diafiltration. Biotechnol Prog. In press.
    • Biotechnol Prog
    • Elmer, J.1    Harris, D.R.2    Sun, G.3    Palmer, A.F.4
  • 22
    • 0347413685 scopus 로고    scopus 로고
    • Determination of size distribution and encapsulation efficiency of liposome-encapsulated hemoglobin blood substitutes using asymmetric flow field-flow fractionation coupled with multi-angle static light scattering
    • Arifin DR, Palmer AF. Determination of size distribution and encapsulation efficiency of liposome-encapsulated hemoglobin blood substitutes using asymmetric flow field-flow fractionation coupled with multi-angle static light scattering. Biotechnol Prog. 2003;19:1798-1811.
    • (2003) Biotechnol Prog , vol.19 , pp. 1798-1811
    • Arifin, D.R.1    Palmer, A.F.2
  • 23
    • 34249815569 scopus 로고
    • Blood analysis
    • 14th ed. New York: Blakiston Division
    • Hawk PB. Blood analysis. In: Hawk's Physiological Chemistry, 14th ed. New York: Blakiston Division; 1965:1090-1099.
    • (1965) Hawk's Physiological Chemistry , pp. 1090-1099
    • Hawk, P.B.1
  • 25
    • 0017186962 scopus 로고
    • Tetramer-dimer dissociation in hemoglobin and the Bohr effect
    • Atha DH, Riggs A. Tetramer-dimer dissociation in hemoglobin and the Bohr effect. J Biol Chem. 1976;251:5537-5543.
    • (1976) J Biol Chem , vol.251 , pp. 5537-5543
    • Atha, D.H.1    Riggs, A.2
  • 26
    • 0030056719 scopus 로고    scopus 로고
    • Functional studies and polymerization of recombinant hemoglobin Glu-alpha2beta26(A3) --> Val/Glu-7(A4) --> Ala
    • Lesecq S, Baudin V, Kister J, Marden MC, Poyart C, Pagnier J. Functional studies and polymerization of recombinant hemoglobin Glu-alpha2beta26(A3) --> Val/Glu-7(A4) --> Ala. J Biol Chem. 1996;271:17211-17214.
    • (1996) J Biol Chem , vol.271 , pp. 17211-17214
    • Lesecq, S.1    Baudin, V.2    Kister, J.3    Marden, M.C.4    Poyart, C.5    Pagnier, J.6
  • 27
    • 4043084061 scopus 로고    scopus 로고
    • Effect of glutaraldehyde concentration on the physical properties of polymerized hemoglobin-based oxygen carriers
    • Eike JH, Palmer AF. Effect of glutaraldehyde concentration on the physical properties of polymerized hemoglobin-based oxygen carriers. Biotechnol Prog. 2004;20:1225-1232.
    • (2004) Biotechnol Prog , vol.20 , pp. 1225-1232
    • Eike, J.H.1    Palmer, A.F.2
  • 28
    • 2942700266 scopus 로고    scopus 로고
    • 4 concentration and reaction time on physical properties of glutaraldehyde-polymerized hemoglobin
    • Eike JH. Palmer AF. Effect of NaBH4 concentration and reaction time on physical properties of glutaraldehyde-polymerized hemoglobin. Biotechnol Prog. 2004;20:946-952.
    • (2004) Biotechnol Prog , vol.20 , pp. 946-952
    • Eike, J.H.1    Palmer, A.F.2
  • 29
    • 0023048809 scopus 로고
    • Effect of glutaraldehyde on haemoglobin: Oxidation-reduction potentials and stability
    • Guillochon D, Esclade L, Thomas D. Effect of glutaraldehyde on haemoglobin: oxidation-reduction potentials and stability. Biochem Pharmacol. 1986;35:317-323.
    • (1986) Biochem Pharmacol , vol.35 , pp. 317-323
    • Guillochon, D.1    Esclade, L.2    Thomas, D.3
  • 30
    • 0016258287 scopus 로고
    • Influence of globin structure on the state of the heme. I. Human deoxyhemoglobin
    • Perutz MF, Ladner JE, Simon SR, Ho C. Influence of globin structure on the state of the heme. I. Human deoxyhemoglobin. Biochemistry. 1974;13:2163-2173.
    • (1974) Biochemistry , vol.13 , pp. 2163-2173
    • Perutz, M.F.1    Ladner, J.E.2    Simon, S.R.3    Ho, C.4
  • 31
    • 5444226407 scopus 로고    scopus 로고
    • + on the oxygen binding properties of glutaraldehyde-polymerized bovine hemoglobin-based blood substitutes
    • + on the oxygen binding properties of glutaraldehyde-polymerized bovine hemoglobin-based blood substitutes. Biotechnol Prog. 2004;20:1543-1549.
    • (2004) Biotechnol Prog , vol.20 , pp. 1543-1549
    • Eike, J.H.1    Palmer, A.F.2
  • 32
    • 33645004307 scopus 로고    scopus 로고
    • Polyhemoglobin with different percentage of tetrameric hemoglobin and effects on vasoactivity and electrocardiogram
    • Yu B, Liu Z, Chang TM. Polyhemoglobin with different percentage of tetrameric hemoglobin and effects on vasoactivity and electrocardiogram. Artif Cells Blood Substit Immobil Biotechnol. 2006;34:159-173.
    • (2006) Artif Cells Blood Substit Immobil Biotechnol , vol.34 , pp. 159-173
    • Yu, B.1    Liu, Z.2    Chang, T.M.3
  • 33
    • 58749115252 scopus 로고    scopus 로고
    • Prevention of the pulmonary vasoconstrictor effects of HBOC-201 in awake lambs by continuously breathing nitric oxide
    • Yu B, Volpato GP, Chang K, Bloch KD, Zapol WM. Prevention of the pulmonary vasoconstrictor effects of HBOC-201 in awake lambs by continuously breathing nitric oxide. Anesthesiology. 2009;110:113-122.
    • (2009) Anesthesiology , vol.110 , pp. 113-122
    • Yu, B.1    Volpato, G.P.2    Chang, K.3    Bloch, K.D.4    Zapol, W.M.5
  • 34
    • 42149185537 scopus 로고    scopus 로고
    • Inhaled nitric oxide enables artificial blood transfusion without hypertension
    • Yu B, Raher MJ, Volpato GP, Bloch KD, Ichinose F, Zapol WM. Inhaled nitric oxide enables artificial blood transfusion without hypertension. Circulation. 2008;117:1982-1990.
    • (2008) Circulation , vol.117 , pp. 1982-1990
    • Yu, B.1    Raher, M.J.2    Volpato, G.P.3    Bloch, K.D.4    Ichinose, F.5    Zapol, W.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.