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Volumn 1820, Issue 12, 2012, Pages 2044-2051

Propylbenzmethylation at Val-1(α) markedly increases the tetramer stability of the PEGylated hemoglobin: A comparison with propylation at Val-1(α)

Author keywords

Hemoglobin; Hemoglobin based oxygen carrier; PEGylation; Propylbenzmethylation; Tetramer stability

Indexed keywords

CYSTEINE; DIMER; HEMOGLOBIN A; MALEIMIDE; PEGYLATED HEMOGLOBIN; TETRAMER; UNCLASSIFIED DRUG; VALINE;

EID: 84867237759     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2012.09.013     Document Type: Article
Times cited : (16)

References (47)
  • 1
    • 84857064605 scopus 로고    scopus 로고
    • Hemoglobin-based oxygen carriers for hemorrhagic shock
    • J. Elmer, H.B. Alam, and S.R. Wilcox Hemoglobin-based oxygen carriers for hemorrhagic shock Resuscitation 83 2012 285 292
    • (2012) Resuscitation , vol.83 , pp. 285-292
    • Elmer, J.1    Alam, H.B.2    Wilcox, S.R.3
  • 2
    • 84857081709 scopus 로고    scopus 로고
    • Impact of hemoglobin concentration and affinity for oxygen on tissue oxygenation: The case of hemoglobin-based oxygen carriers
    • M. Samaja, and L. Terraneo Impact of hemoglobin concentration and affinity for oxygen on tissue oxygenation: the case of hemoglobin-based oxygen carriers Artif. Organs 36 2012 210 215
    • (2012) Artif. Organs , vol.36 , pp. 210-215
    • Samaja, M.1    Terraneo, L.2
  • 3
    • 79959954970 scopus 로고    scopus 로고
    • Basic science offers a challenge for developing hemoglobin based oxygen carriers into therapeutic agents
    • E. Bucci Basic science offers a challenge for developing hemoglobin based oxygen carriers into therapeutic agents Artif. Cells Blood Substit. Immobil. Biotechnol. 39 2011 206 213
    • (2011) Artif. Cells Blood Substit. Immobil. Biotechnol. , vol.39 , pp. 206-213
    • Bucci, E.1
  • 4
    • 79955412524 scopus 로고    scopus 로고
    • Hemoglobin-based oxygen carriers for reversing hypotension and shock: NO way, NO how?
    • J.H. Levy Hemoglobin-based oxygen carriers for reversing hypotension and shock: NO way, NO how? Anesthesiology 114 2011 1016 1018
    • (2011) Anesthesiology , vol.114 , pp. 1016-1018
    • Levy, J.H.1
  • 5
    • 52049125961 scopus 로고    scopus 로고
    • Hemoglobin-based oxygen carriers as blood substitutes
    • A. Mozzarelli Hemoglobin-based oxygen carriers as blood substitutes Biochim. Biophys. Acta 1784 2008 1363 1364
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 1363-1364
    • Mozzarelli, A.1
  • 6
    • 84861466881 scopus 로고    scopus 로고
    • Down selection of polymerized bovine hemoglobins for use as oxygen releasing therapeutics in a guinea pig model
    • J.H. Baek, Y. Zhou, D.R. Harris, D.J. Schaer, A.F. Palmer, and P.W. Buehler Down selection of polymerized bovine hemoglobins for use as oxygen releasing therapeutics in a guinea pig model Toxicol. Sci. 127 2012 567 581
    • (2012) Toxicol. Sci. , vol.127 , pp. 567-581
    • Baek, J.H.1    Zhou, Y.2    Harris, D.R.3    Schaer, D.J.4    Palmer, A.F.5    Buehler, P.W.6
  • 7
    • 0036290272 scopus 로고    scopus 로고
    • Preparation of well-defined polyhemoglobin based on dimethyl apidimidate and glutaraldehyde cross-linkage
    • T. Hu, and Z. Su Preparation of well-defined polyhemoglobin based on dimethyl apidimidate and glutaraldehyde cross-linkage Biochem. Biophys. Res. Commun. 293 2002 958 961
    • (2002) Biochem. Biophys. Res. Commun. , vol.293 , pp. 958-961
    • Hu, T.1    Su, Z.2
  • 8
    • 52049089667 scopus 로고    scopus 로고
    • Enhancing stability and expression of recombinant human hemoglobin in E. coli: Progress in the development of a recombinant HBOC source
    • P.E. Graves, D.P. Henderson, M.J. Horstman, B.J. Solomon, and J.S. Olson Enhancing stability and expression of recombinant human hemoglobin in E. coli: progress in the development of a recombinant HBOC source Biochim. Biophys. Acta 1784 2008 1471 1479
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 1471-1479
    • Graves, P.E.1    Henderson, D.P.2    Horstman, M.J.3    Solomon, B.J.4    Olson, J.S.5
  • 9
    • 84934440696 scopus 로고    scopus 로고
    • MP4, a vasodilatory PEGylated hemoglobin
    • R.H. Cole, and K.D. Vandegriff MP4, a vasodilatory PEGylated hemoglobin Adv. Exp. Med. Biol. 701 2011 85 90
    • (2011) Adv. Exp. Med. Biol. , vol.701 , pp. 85-90
    • Cole, R.H.1    Vandegriff, K.D.2
  • 10
    • 79955639505 scopus 로고    scopus 로고
    • Dimer-tetramer association equilibria of human adult hemoglobin and its mutants as observed by analytical ultracentrifugation
    • F. Arisaka, Y. Nagai, and M. Nagai Dimer-tetramer association equilibria of human adult hemoglobin and its mutants as observed by analytical ultracentrifugation Methods 54 2011 175 180
    • (2011) Methods , vol.54 , pp. 175-180
    • Arisaka, F.1    Nagai, Y.2    Nagai, M.3
  • 11
    • 33846969212 scopus 로고    scopus 로고
    • Influence of intramolecular cross-links on the molecular, structural and functional properties of PEGylated hemoglobin
    • T. Hu, B.N. Manjula, D. Li, M. Brenowitz, and A.S. Acharya Influence of intramolecular cross-links on the molecular, structural and functional properties of PEGylated hemoglobin Biochem. J. 402 2007 143 151
    • (2007) Biochem. J. , vol.402 , pp. 143-151
    • Hu, T.1    Manjula, B.N.2    Li, D.3    Brenowitz, M.4    Acharya, A.S.5
  • 14
    • 79952396185 scopus 로고    scopus 로고
    • Increased inter dimeric interaction of oxy hemoglobin is necessary for attenuation of reductive Pegylation promoted dissociation of tetramer
    • T. Hu, D. Li, F. Meng, M. Prabhakaran, and S.A. Acharya Increased inter dimeric interaction of oxy hemoglobin is necessary for attenuation of reductive Pegylation promoted dissociation of tetramer Artif. Cells Blood Substit. Immobil. Biotechnol. 39 2011 69 78
    • (2011) Artif. Cells Blood Substit. Immobil. Biotechnol. , vol.39 , pp. 69-78
    • Hu, T.1    Li, D.2    Meng, F.3    Prabhakaran, M.4    Acharya, S.A.5
  • 15
    • 44249093233 scopus 로고    scopus 로고
    • Cell-free hemoglobin based blood substitutes and risk of myocardial infarction and death: A meta-analysis
    • C. Natanson, S.J. Kern, P. Lurie, S.M. Banks, and S.M. Wolfe Cell-free hemoglobin based blood substitutes and risk of myocardial infarction and death: a meta-analysis J. Am. Med. Assoc. 299 2008 2304 2312
    • (2008) J. Am. Med. Assoc. , vol.299 , pp. 2304-2312
    • Natanson, C.1    Kern, S.J.2    Lurie, P.3    Banks, S.M.4    Wolfe, S.M.5
  • 16
    • 56749117870 scopus 로고    scopus 로고
    • Functional cross-linked hemoglobin bis-tetramers: Geometry and cooperativity
    • D. Hu, and R. Kluger Functional cross-linked hemoglobin bis-tetramers: geometry and cooperativity Biochemistry 47 2008 12551 12561
    • (2008) Biochemistry , vol.47 , pp. 12551-12561
    • Hu, D.1    Kluger, R.2
  • 17
    • 53749092845 scopus 로고    scopus 로고
    • Autoxidation of the site-specifically PEGylated hemoglobin
    • T. Hu, D. Li, B.N. Manjula, and S.A. Acharya Autoxidation of the site-specifically PEGylated hemoglobin Biochemistry 47 2008 10981 10990
    • (2008) Biochemistry , vol.47 , pp. 10981-10990
    • Hu, T.1    Li, D.2    Manjula, B.N.3    Acharya, S.A.4
  • 18
    • 0142166336 scopus 로고    scopus 로고
    • Purification and molecular analysis of hemoglobin by high-performance liquid chromatography
    • B.N. Manjula, and A.S. Acharya Purification and molecular analysis of hemoglobin by high-performance liquid chromatography Methods Mol. Med. 82 2003 31 47
    • (2003) Methods Mol. Med. , vol.82 , pp. 31-47
    • Manjula, B.N.1    Acharya, A.S.2
  • 19
    • 83655163715 scopus 로고    scopus 로고
    • Preparation, characterization and in vitro bioactivity of N-terminally PEGylated staphylokinase dimers
    • R. Liu, D. Li, J. Wang, R. Qiu, Q. Lin, G. Zhang, G. Ma, Z. Su, and T. Hu Preparation, characterization and in vitro bioactivity of N-terminally PEGylated staphylokinase dimers Process. Biochem. 47 2012 41 46
    • (2012) Process. Biochem. , vol.47 , pp. 41-46
    • Liu, R.1    Li, D.2    Wang, J.3    Qiu, R.4    Lin, Q.5    Zhang, G.6    Ma, G.7    Su, Z.8    Hu, T.9
  • 20
    • 79952450902 scopus 로고    scopus 로고
    • Kinetic and stoichiometric analysis of the modification process for N-terminal PEGylation of staphylokinase
    • J. Wang, T. Hu, Y. Liu, G. Zhang, G. Ma, and Z. Su Kinetic and stoichiometric analysis of the modification process for N-terminal PEGylation of staphylokinase Anal. Biochem. 412 2011 114 116
    • (2011) Anal. Biochem. , vol.412 , pp. 114-116
    • Wang, J.1    Hu, T.2    Liu, Y.3    Zhang, G.4    Ma, G.5    Su, Z.6
  • 21
    • 77958454555 scopus 로고    scopus 로고
    • Electrophoretic analysis of PEGylated hemoglobin-based blood substitutes
    • L. Ronda, B. Pioselli, S. Bruno, S. Faggiano, and A. Mozzarelli Electrophoretic analysis of PEGylated hemoglobin-based blood substitutes Anal. Biochem. 408 2011 118 123
    • (2011) Anal. Biochem. , vol.408 , pp. 118-123
    • Ronda, L.1    Pioselli, B.2    Bruno, S.3    Faggiano, S.4    Mozzarelli, A.5
  • 22
    • 0014679374 scopus 로고
    • Determination of the reactive SH groups in heme protein with 4,4′-dipyridine disulfide
    • R.S. Ampulski, V.E. Ayers, and S.A. Morell Determination of the reactive SH groups in heme protein with 4,4′-dipyridine disulfide Anal. Biochem. 32 1969 136 169
    • (1969) Anal. Biochem. , vol.32 , pp. 136-169
    • Ampulski, R.S.1    Ayers, V.E.2    Morell, S.A.3
  • 23
    • 0031572829 scopus 로고    scopus 로고
    • Mapping of recombinant hemoglobin using immobilized trypsin cartridges
    • J. Lippincott, E. Hess, and I. Apostol Mapping of recombinant hemoglobin using immobilized trypsin cartridges Anal. Biochem. 252 1997 314 325
    • (1997) Anal. Biochem. , vol.252 , pp. 314-325
    • Lippincott, J.1    Hess, E.2    Apostol, I.3
  • 24
    • 0033593343 scopus 로고    scopus 로고
    • Glutaraldehyde modification of recombinant human hemoglobin alters its hemodynamic properties
    • M.P. Doyle, I. Apostol, and B.A. Kerwin Glutaraldehyde modification of recombinant human hemoglobin alters its hemodynamic properties J. Biol. Chem. 274 1999 2583 2591
    • (1999) J. Biol. Chem. , vol.274 , pp. 2583-2591
    • Doyle, M.P.1    Apostol, I.2    Kerwin, B.A.3
  • 25
    • 29644434820 scopus 로고    scopus 로고
    • Influence of the chemistry of conjugation of poly(ethylene glycol) to Hb on the oxygen-binding and solution properties of the PEG-Hb conjugate
    • T. Hu, M. Prabhakaran, S.A. Acharya, and B.N. Manjula Influence of the chemistry of conjugation of poly(ethylene glycol) to Hb on the oxygen-binding and solution properties of the PEG-Hb conjugate Biochem. J. 392 2005 555 564
    • (2005) Biochem. J. , vol.392 , pp. 555-564
    • Hu, T.1    Prabhakaran, M.2    Acharya, S.A.3    Manjula, B.N.4
  • 27
    • 0015223254 scopus 로고
    • Dissociation of hemoglobin into subunits: Ligand-linked dissociation at neutral pH
    • G.L. Kellett Dissociation of hemoglobin into subunits: ligand-linked dissociation at neutral pH J. Mol. Biol. 59 1971 401 424
    • (1971) J. Mol. Biol. , vol.59 , pp. 401-424
    • Kellett, G.L.1
  • 28
    • 18844427853 scopus 로고    scopus 로고
    • Structural and biophysical characterization of the 40 kDa PEG-interferon-α2a and its individual positional isomers
    • C. Dhalluin, A. Ross, L.A. Leuthold, S. Foser, B. Gsell, F. Muller, and H. Senn Structural and biophysical characterization of the 40 kDa PEG-interferon-α2a and its individual positional isomers Bioconjug. Chem. 16 2005 504 517
    • (2005) Bioconjug. Chem. , vol.16 , pp. 504-517
    • Dhalluin, C.1    Ross, A.2    Leuthold, L.A.3    Foser, S.4    Gsell, B.5    Muller, F.6    Senn, H.7
  • 29
    • 0345169971 scopus 로고    scopus 로고
    • Preparation and characterization dimeric bovine hemoglobin tetramers
    • T. Hu, D. Li, and Z. Su Preparation and characterization dimeric bovine hemoglobin tetramers J. Protein Chem. 22 2003 411 416
    • (2003) J. Protein Chem. , vol.22 , pp. 411-416
    • Hu, T.1    Li, D.2    Su, Z.3
  • 30
    • 0037434443 scopus 로고    scopus 로고
    • A solid phase adsorption method for preparation of bovine serum albumin-bovine hemoglobin conjugate
    • T. Hu, and Z. Su A solid phase adsorption method for preparation of bovine serum albumin-bovine hemoglobin conjugate J. Biotechnol. 100 2003 267 275
    • (2003) J. Biotechnol. , vol.100 , pp. 267-275
    • Hu, T.1    Su, Z.2
  • 31
    • 0025122955 scopus 로고
    • The stability of the hemoglobin linkage in some normal, mutant, and chemically modified hemoglobins
    • R.E. Benesch, and S. Kwong The stability of the hemoglobin linkage in some normal, mutant, and chemically modified hemoglobins J. Biol. Chem. 265 1990 14881 14885
    • (1990) J. Biol. Chem. , vol.265 , pp. 14881-14885
    • Benesch, R.E.1    Kwong, S.2
  • 32
    • 0028286276 scopus 로고
    • The stability of the heme-globin linkage: Measurement of heme exchange
    • R.E. Benesch The stability of the heme-globin linkage: measurement of heme exchange Methods Enzymol. 231 1994 496 502
    • (1994) Methods Enzymol. , vol.231 , pp. 496-502
    • Benesch, R.E.1
  • 33
    • 0016665257 scopus 로고
    • Alteration of functional properties associated with the change in quaternary structure in unliganded haemoglobin
    • J.V. Kilmartin, J.A. Hewitt, and J.F. Wootton Alteration of functional properties associated with the change in quaternary structure in unliganded haemoglobin J. Mol. Biol. 93 1975 203 218
    • (1975) J. Mol. Biol. , vol.93 , pp. 203-218
    • Kilmartin, J.V.1    Hewitt, J.A.2    Wootton, J.F.3
  • 34
    • 0142228326 scopus 로고    scopus 로고
    • Hemoglobin fluorescence
    • R.E. Hirsch Hemoglobin fluorescence Methods Mol. Med. 82 2003 133 154
    • (2003) Methods Mol. Med. , vol.82 , pp. 133-154
    • Hirsch, R.E.1
  • 35
    • 0014408353 scopus 로고
    • The renal handling of hemoglobin
    • H.F. Bunn, and J.H. Jandl The renal handling of hemoglobin J. Biol. Chem. 243 1968 465 475
    • (1968) J. Biol. Chem. , vol.243 , pp. 465-475
    • Bunn, H.F.1    Jandl, J.H.2
  • 36
    • 52049110550 scopus 로고    scopus 로고
    • Effect of cross-linker length on the stability of hemoglobin
    • K.M. Bobofchak, E. Tarasov, and K.W. Olsen Effect of cross-linker length on the stability of hemoglobin Biochim. Biophys. Acta 1784 2008 1410 1414
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 1410-1414
    • Bobofchak, K.M.1    Tarasov, E.2    Olsen, K.W.3
  • 38
    • 0035822702 scopus 로고    scopus 로고
    • Monomer-dimer equilibrium and oxygen binding properties of ferrous Vitreoscilla hemoglobin
    • L. Giangiacomo, R. D'Avino, G. di Prisco, and E. Chiancone Monomer-dimer equilibrium and oxygen binding properties of ferrous Vitreoscilla hemoglobin Biochemistry 40 2001 3062 3068
    • (2001) Biochemistry , vol.40 , pp. 3062-3068
    • Giangiacomo, L.1    D'Avino, R.2    Di Prisco, G.3    Chiancone, E.4
  • 39
    • 0024953088 scopus 로고
    • Mechanisms of cooperativity and allosteric regulation in proteins
    • M.F. Perutz Mechanisms of cooperativity and allosteric regulation in proteins Q. Rev. Biophys. 22 1989 139 237
    • (1989) Q. Rev. Biophys. , vol.22 , pp. 139-237
    • Perutz, M.F.1
  • 40
    • 49449115443 scopus 로고    scopus 로고
    • CO-MP4, a polyethylene glycol-conjugated haemoglobin derivative and carbon monoxide carrier that reduces myocardial infarct size in rats
    • K.D. Vandegriff, M.A. Young, J. Lohman, A. Bellelli, M. Samaja, A. Malavalli, and R.M. Winslow CO-MP4, a polyethylene glycol-conjugated haemoglobin derivative and carbon monoxide carrier that reduces myocardial infarct size in rats Br. J. Pharmacol. 154 2008 1649 1661
    • (2008) Br. J. Pharmacol. , vol.154 , pp. 1649-1661
    • Vandegriff, K.D.1    Young, M.A.2    Lohman, J.3    Bellelli, A.4    Samaja, M.5    Malavalli, A.6    Winslow, R.M.7
  • 41
    • 0001023291 scopus 로고    scopus 로고
    • The molecular mechanism of autoxidation for myoglobin and hemoglobin: A venerable puzzle
    • K. Shikama The molecular mechanism of autoxidation for myoglobin and hemoglobin: a venerable puzzle Chem. Rev. 98 1998 1357 1373
    • (1998) Chem. Rev. , vol.98 , pp. 1357-1373
    • Shikama, K.1
  • 42
    • 0025145949 scopus 로고
    • Oxidative reactions of hemoglobin
    • C.C. Winterbourn Oxidative reactions of hemoglobin Methods Enzymol. 186 1990 265 272
    • (1990) Methods Enzymol. , vol.186 , pp. 265-272
    • Winterbourn, C.C.1
  • 43
    • 0027358877 scopus 로고
    • Endothelial cell heme uptake from heme proteins: Induction of sensitization and desensitization to oxidant damage
    • J. Balla, H.S. Jacob, G. Balla, K. Nath, J.W. Eaton, and G.M. Vercellotti Endothelial cell heme uptake from heme proteins: induction of sensitization and desensitization to oxidant damage Proc. Natl. Acad. Sci. U. S. A. 90 1993 9285 9289
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 9285-9289
    • Balla, J.1    Jacob, H.S.2    Balla, G.3    Nath, K.4    Eaton, J.W.5    Vercellotti, G.M.6
  • 46
    • 44249093233 scopus 로고    scopus 로고
    • Cell-free hemoglobin based blood substitutes and risk of myocardial infarction and death: A meta-analysis
    • C. Natanson, S.J. Kern, P. Lurie, S.M. Banks, and S.M. Wolfe Cell-free hemoglobin based blood substitutes and risk of myocardial infarction and death: a meta-analysis JAMA 299 2008 2304 2312
    • (2008) JAMA , vol.299 , pp. 2304-2312
    • Natanson, C.1    Kern, S.J.2    Lurie, P.3    Banks, S.M.4    Wolfe, S.M.5
  • 47
    • 78049404205 scopus 로고    scopus 로고
    • Haemoglobin-based oxygen carriers: Research and reality towards an alternative to blood transfusions
    • A. Mozzarelli, L. Ronda, S. Faggiano, S. Bettati, and S. Bruno Haemoglobin-based oxygen carriers: research and reality towards an alternative to blood transfusions Blood Transfus. 8 2010 s59 s68
    • (2010) Blood Transfus. , vol.8
    • Mozzarelli, A.1    Ronda, L.2    Faggiano, S.3    Bettati, S.4    Bruno, S.5


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