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Volumn 12, Issue 1, 2011, Pages

Low affinity PEGylated hemoglobin from Trematomus bernacchii, a model for hemoglobin-based blood substitutes

Author keywords

[No Author keywords available]

Indexed keywords

2 IMINOTHIOLANE; ADENOSINE TRIPHOSPHATE; BLOOD SUBSTITUTE; CYSTEINE; DIOXYGENASE; HEMOGLOBIN DERIVATIVE; MACROGOL; NITRIC OXIDE; PEGYLATED HEMOGLOBIN; PROTEIN P50; PROTON; TETRAMER; UNCLASSIFIED DRUG; FISH PROTEIN; HEMOGLOBIN; MACROGOL DERIVATIVE; OXYGEN;

EID: 83655197887     PISSN: None     EISSN: 14712091     Source Type: Journal    
DOI: 10.1186/1471-2091-12-66     Document Type: Article
Times cited : (9)

References (36)
  • 1
    • 78649781950 scopus 로고    scopus 로고
    • Modulation of expression and polymerization of hemoglobin Polytaur, a potential blood substitute
    • 10.1016/j.abb.2010.09.027 20920461
    • Modulation of expression and polymerization of hemoglobin Polytaur, a potential blood substitute. Faggiano S, Bruno S, Ronda L, Pizzonia P, Pioselli B, Mozzarelli A, Arch Biochem Biophys 2011 505 42 47 10.1016/j.abb.2010.09.027 20920461
    • (2011) Arch Biochem Biophys , vol.505 , pp. 42-47
    • Faggiano, S.1    Bruno, S.2    Ronda, L.3    Pizzonia, P.4    Pioselli, B.5    Mozzarelli, A.6
  • 2
    • 63049083139 scopus 로고    scopus 로고
    • Design of recombinant hemoglobins for use in transfusion fluids
    • 10.1016/j.ccc.2008.12.010 19341913
    • Design of recombinant hemoglobins for use in transfusion fluids. Fronticelli C, Koehler RC, Crit Care Clin 2009 25 357 371 10.1016/j.ccc.2008.12. 010 19341913
    • (2009) Crit Care Clin , vol.25 , pp. 357-371
    • Fronticelli, C.1    Koehler, R.C.2
  • 5
    • 52049094782 scopus 로고    scopus 로고
    • Hb(alphaalpha, betabeta): A novel fusion construct for a dimeric, four-domain hemoglobin
    • 18267132
    • Hb(alphaalpha, betabeta): a novel fusion construct for a dimeric, four-domain hemoglobin. Panetta G, Arcovito A, Morea V, Bellelli A, Miele AE, Biochim Biophys Acta 2008 1784 1462 1470 18267132
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 1462-1470
    • Panetta, G.1    Arcovito, A.2    Morea, V.3    Bellelli, A.4    Miele, A.E.5
  • 6
    • 52349088745 scopus 로고    scopus 로고
    • Ligand reactivity and allosteric regulation of hemoglobin-based oxygen carriers
    • 18502214
    • Ligand reactivity and allosteric regulation of hemoglobin-based oxygen carriers. Ronda L, Bruno S, Abbruzzetti S, Viappiani C, Bettati S, Biochim Biophys Acta 2008 1784 1365 1377 18502214
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 1365-1377
    • Ronda, L.1    Bruno, S.2    Abbruzzetti, S.3    Viappiani, C.4    Bettati, S.5
  • 7
    • 0037390385 scopus 로고    scopus 로고
    • MP4, a new nonvasoactive PEG-Hb conjugate
    • DOI 10.1046/j.1537-2995.2003.00341.x
    • MP4, a new nonvasoactive PEG-Hb conjugate. Vandegriff KD, Malavalli A, Wooldridge J, Lohman J, Winslow RM, Transfusion 2003 43 509 516 10.1046/j.1537-2995.2003.00341.x 12662285 (Pubitemid 36428335)
    • (2003) Transfusion , vol.43 , Issue.4 , pp. 509-516
    • Vandegriff, K.D.1    Malavalli, A.2    Wooldridge, J.3    Lohman, J.4    Winslow, R.M.5
  • 9
    • 52049114134 scopus 로고    scopus 로고
    • Cell-free oxygen carriers: Scientific foundations, clinical development, and new directions
    • 18555029
    • Cell-free oxygen carriers: scientific foundations, clinical development, and new directions. Winslow RM, Biochim Biophys Acta 2008 1784 1382 1386 18555029
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 1382-1386
    • Winslow, R.M.1
  • 10
    • 44249093233 scopus 로고    scopus 로고
    • Cell-free hemoglobin-based blood substitutes and risk of myocardial infarction and death: A meta-analysis
    • DOI 10.1001/jama.299.19.jrv80007
    • Cell-free hemoglobin-based blood substitutes and risk of myocardial infarction and death: a meta-analysis. Natanson C, Kern SJ, Lurie P, Banks SM, Wolfe SM, Jama 2008 299 2304 2312 10.1001/jama.299.19.jrv80007 18443023 (Pubitemid 351724397)
    • (2008) JAMA - Journal of the American Medical Association , vol.299 , Issue.19 , pp. 2304-2312
    • Natanson, C.1    Kern, S.J.2    Lurie, P.3    Banks, S.M.4    Wolfe, S.M.5
  • 14
    • 71249139373 scopus 로고    scopus 로고
    • Extension arm facilitated pegylation of alphaalpha-hemoglobin with modifications targeted exclusively to amino groups: Functional and structural advantages of free Cys-93(beta) in the PEG-Hb adduct
    • 10.1021/bc900170e 19842622
    • Extension arm facilitated pegylation of alphaalpha-hemoglobin with modifications targeted exclusively to amino groups: functional and structural advantages of free Cys-93(beta) in the PEG-Hb adduct. Li D, Hu T, Manjula BN, Acharya SA, Bioconjug Chem 2009 20 2062 2070 10.1021/bc900170e 19842622
    • (2009) Bioconjug Chem , vol.20 , pp. 2062-2070
    • Li, D.1    Hu, T.2    Manjula, B.N.3    Acharya, S.A.4
  • 15
    • 33847259712 scopus 로고    scopus 로고
    • Molecular aspects of the high oxygen afinity of non-hypertensive hexa pegylated hemoglobin, [(SP-PEG5K)6-Hb]
    • DOI 10.1080/10731190600974376, PII 770970752
    • Molecular aspects of the high oxygen affinity of non-hypertensive hexa pegylated hemoglobin, [(SP-PEG5K)(6)-Hb]. Li D, Manjula BN, Ho NT, Simplaceanu V, Ho C, Acharya AS, Artif Cells Blood Substit Immobil Biotechnol 2007 35 19 29 10.1080/10731190600974376 17364468 (Pubitemid 46324169)
    • (2007) Artificial Cells, Blood Substitutes, and Biotechnology , vol.35 , Issue.1 , pp. 19-29
    • Li, D.1    Manjula, B.N.2    Ho, N.T.3    Simplaceanu, V.4    Ho, C.5    Acharya, A.S.6
  • 16
    • 34547396502 scopus 로고    scopus 로고
    • 2 affinity and tissue oxygenation
    • DOI 10.1042/BJ20070238
    • Non-hypertensive tetraPEGylated canine haemoglobin: correlation between PEGylation, O2 affinity and tissue oxygenation. Acharya SA, Acharya VN, Kanika ND, Tsai AG, Intaglietta M, Manjula BN, Biochem J 2007 405 503 511 10.1042/BJ20070238 17425516 (Pubitemid 47172048)
    • (2007) Biochemical Journal , vol.405 , Issue.3 , pp. 503-511
    • Acharya, S.A.1    Acharya, V.N.2    Kanika, N.D.3    Tsai, A.G.4    Intaglietta, M.5    Manjula, B.N.6
  • 18
    • 34447504390 scopus 로고    scopus 로고
    • Biogeography and adaptation of Notothenioid fish: Hemoglobin function and globin-gene evolution
    • DOI 10.1016/j.gene.2007.02.047, PII S0378111907002144
    • Biogeography and adaptation of Notothenioid fish: hemoglobin function and globin-gene evolution. di Prisco G, Eastman JT, Giordano D, Parisi E, Verde C, Gene 2007 398 143 155 10.1016/j.gene.2007.02.047 17553637 (Pubitemid 47068898)
    • (2007) Gene , vol.398 , Issue.SPEC. ISS.1-2 , pp. 143-155
    • Di Prisco, G.1    Eastman, J.T.2    Giordano, D.3    Parisi, E.4    Verde, C.5
  • 19
    • 0035852972 scopus 로고    scopus 로고
    • Hemoglobin of the antarctic fishes Trematomus bernacchii and Trematomus newnesi: Structural basis for the increased stability of the liganded tetramer relative to human hemoglobin
    • DOI 10.1021/bi002297j
    • Hemoglobin of the Antarctic fishes Trematomus bernacchii and Trematomus newnesi: structural basis for the increased stability of the liganded tetramer relative to human hemoglobin. Giangiacomo L, D'Avino R, di Prisco G, Chiancone E, Biochemistry 2001 40 3062 3068 10.1021/bi002297j 11258920 (Pubitemid 32205349)
    • (2001) Biochemistry , vol.40 , Issue.10 , pp. 3062-3068
    • Giangiacomo, L.1    D'Avino, R.2    Di Prisco, G.3    Chiancone, E.4
  • 20
    • 33748996221 scopus 로고    scopus 로고
    • High resolution crystal structure of deoxy hemoglobin from Trematomus bernacchii at different pH values: The role of histidine residues in modulating the strength of the root effect
    • DOI 10.1002/prot.21114
    • High resolution crystal structure of deoxy hemoglobin from Trematomus bernacchii at different pH values: the role of histidine residues in modulating the strength of the root effect. Mazzarella L, Vergara A, Vitagliano L, Merlino A, Bonomi G, Scala S, Verde C, di Prisco G, Proteins 2006 65 490 498 10.1002/prot.21114 16909420 (Pubitemid 44454119)
    • (2006) Proteins: Structure, Function and Genetics , vol.65 , Issue.2 , pp. 490-498
    • Mazzarella, L.1    Vergara, A.2    Vitagliano, L.3    Merlino, A.4    Bonomi, G.5    Scala, S.6    Verde, C.7    Di Prisco, G.8
  • 21
    • 0015790339 scopus 로고
    • An enzymic reduction system for metmyoglobin and methemoglobin, and its application to functional studies of oxygen carriers
    • 4146292
    • An enzymic reduction system for metmyoglobin and methemoglobin, and its application to functional studies of oxygen carriers. Hayashi A, Suzuki T, Shin M, Biochim Biophys Acta 1973 310 309 316 4146292
    • (1973) Biochim Biophys Acta , vol.310 , pp. 309-316
    • Hayashi, A.1    Suzuki, T.2    Shin, M.3
  • 22
    • 0001620821 scopus 로고
    • Antarctic fish hemoglobin: An outline of the molecular structure and oxygen binding properties - I. Molecular structure
    • 10.1016/0305-0491(88)90298-2
    • Antarctic fish hemoglobin: an outline of the molecular structure and oxygen binding properties - I. Molecular structure. D'Avino R, Di Prisco G, Comp Biochem Physiol, B 1988 90 579 584 10.1016/0305-0491(88)90298-2
    • (1988) Comp Biochem Physiol, B , vol.90 , pp. 579-584
    • D'Avino, R.1    Di Prisco, G.2
  • 23
    • 0026545367 scopus 로고
    • Haemoglobin of the antarctic fish Pagothenia bernacchii. Amino acid sequence, oxygen equilibria and crystal structure of its carbonmonoxy derivative
    • 10.1016/0022-2836(92)91007-C 1560461
    • Haemoglobin of the antarctic fish Pagothenia bernacchii. Amino acid sequence, oxygen equilibria and crystal structure of its carbonmonoxy derivative. Camardella L, Caruso C, D'Avino R, di Prisco G, Rutigliano B, Tamburrini M, Fermi G, Perutz MF, J Mol Biol 1992 224 449 460 10.1016/0022-2836(92)91007-C 1560461
    • (1992) J Mol Biol , vol.224 , pp. 449-460
    • Camardella, L.1    Caruso, C.2    D'Avino, R.3    Di Prisco, G.4    Rutigliano, B.5    Tamburrini, M.6    Fermi, G.7    Perutz, M.F.8
  • 24
    • 47049094619 scopus 로고    scopus 로고
    • Oxygen binding to heme proteins in solution, encapsulated in silica gels, and in the crystalline state
    • 18433635
    • Oxygen binding to heme proteins in solution, encapsulated in silica gels, and in the crystalline state. Ronda L, Bruno S, Faggiano S, Bettati S, Mozzarelli A, Methods Enzymol 2008 437 311 328 18433635
    • (2008) Methods Enzymol , vol.437 , pp. 311-328
    • Ronda, L.1    Bruno, S.2    Faggiano, S.3    Bettati, S.4    Mozzarelli, A.5
  • 25
    • 0015952857 scopus 로고
    • A study of the properties of two porphyringlobin species formed in the reaction of protoporphyrin IX with human globin
    • 4824214
    • A study of the properties of two porphyringlobin species formed in the reaction of protoporphyrin IX with human globin. Ainsworth S, Treffry A, Biochem J 1974 137 331 337 4824214
    • (1974) Biochem J , vol.137 , pp. 331-337
    • Ainsworth, S.1    Treffry, A.2
  • 26
    • 4344592222 scopus 로고    scopus 로고
    • MP4, a new nonvasoactive polyethylene glycol-hemoglobin conjugate
    • DOI 10.1111/j.1525-1594.2004.07392.x
    • MP4, a new nonvasoactive polyethylene glycol-hemoglobin conjugate. Winslow RM, Artif Organs 2004 28 800 806 10.1111/j.1525-1594.2004.07392.x 15320943 (Pubitemid 39159152)
    • (2004) Artificial Organs , vol.28 , Issue.9 , pp. 800-806
    • Winslow, R.M.1
  • 27
    • 77958454555 scopus 로고    scopus 로고
    • Electrophoretic analysis of PEGylated hemoglobin-based blood substitutes
    • 10.1016/j.ab.2010.08.043 20816741
    • Electrophoretic analysis of PEGylated hemoglobin-based blood substitutes. Ronda L, Pioselli B, Bruno S, Faggiano S, Mozzarelli A, Anal Biochem 2011 408 118 123 10.1016/j.ab.2010.08.043 20816741
    • (2011) Anal Biochem , vol.408 , pp. 118-123
    • Ronda, L.1    Pioselli, B.2    Bruno, S.3    Faggiano, S.4    Mozzarelli, A.5
  • 28
    • 33845216141 scopus 로고    scopus 로고
    • Time-resolved methods in biophysics. 2. Monitoring haem proteins at work with nanosecond laser flash photolysis
    • DOI 10.1039/b610236k
    • Time-resolved methods in Biophysics. 2. Monitoring haem proteins at work with nanosecond laser flash photolysis. Abbruzzetti S, Bruno S, Faggiano S, Grandi E, Mozzarelli A, Viappiani C, Photochem Photobiol Sci 2006 5 1109 1120 10.1039/b610236k 17136275 (Pubitemid 44853763)
    • (2006) Photochemical and Photobiological Sciences , vol.5 , Issue.12 , pp. 1109-1120
    • Abbruzzetti, S.1    Bruno, S.2    Faggiano, S.3    Grandi, E.4    Mozzarelli, A.5    Viappiani, C.6
  • 30
    • 0031466768 scopus 로고    scopus 로고
    • Colloid osmotic properties of modified hemoglobins: Chemically cross-linked versus polyethylene glycol surface-conjugated
    • DOI 10.1016/S0301-4622(97)00079-3, PII S0301462297000793
    • Colloid osmotic properties of modified hemoglobins: chemically cross-linked versus polyethylene glycol surface-conjugated. Vandegriff KD, McCarthy M, Rohlfs RJ, Winslow RM, Biophys Chem 1997 69 23 30 10.1016/S0301-4622(97)00079-3 9440206 (Pubitemid 28010759)
    • (1997) Biophysical Chemistry , vol.69 , Issue.1 , pp. 23-30
    • Vandegriff, K.D.1    McCarthy, M.2    Rohlfs, R.J.3    Winslow, R.M.4
  • 31
    • 0030907624 scopus 로고    scopus 로고
    • Can a two-state MWC allosteric model explain hemoglobin kinetics?
    • DOI 10.1021/bi9619177
    • Can a two-state MWC allosteric model explain hemoglobin kinetics? Henry ER, Jones CM, Hofrichter J, Eaton WA, Biochemistry 1997 36 6511 6528 10.1021/bi9619177 9174369 (Pubitemid 27231410)
    • (1997) Biochemistry , vol.36 , Issue.21 , pp. 6511-6528
    • Henry, E.R.1    Jones, C.M.2    Hofrichter, J.3    Eaton, W.A.4
  • 32
    • 0029899611 scopus 로고    scopus 로고
    • Allosteric intermediates in hemoglobin. 2. Kinetic modeling of HbCO photolysis
    • DOI 10.1021/bi952248k
    • Allosteric intermediates in hemoglobin. 2. Kinetic modeling of HbCO photolysis. Goldbeck RA, Paquette SJ, Bjorling SC, Kliger DS, Biochemistry 1996 35 8628 8639 10.1021/bi952248k 8679625 (Pubitemid 26240198)
    • (1996) Biochemistry , vol.35 , Issue.26 , pp. 8628-8639
    • Goldbeck, R.A.1    Paquette, S.J.2    Bjorling, S.C.3    Kliger, D.S.4
  • 33
    • 0031856673 scopus 로고    scopus 로고
    • Rate of reaction with nitric oxide determines the hypertensive effect of cell-free hemoglobin
    • DOI 10.1038/nbt0798-672
    • Rate of reaction with nitric oxide determines the hypertensive effect of cell-free hemoglobin. Doherty DH, Doyle MP, Curry SR, Vali RJ, Fattor TJ, Olson JS, Lemon DD, Nat Biotechnol 1998 16 672 676 10.1038/nbt0798-672 9661203 (Pubitemid 28334327)
    • (1998) Nature Biotechnology , vol.16 , Issue.7 , pp. 672-676
    • Doherty, D.H.1    Doyle, M.P.2    Curry, S.R.3    Vali, R.J.4    Fattor, T.J.5    Olson, J.S.6    Lemon, D.D.7


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