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Volumn 47, Issue 47, 2008, Pages 12551-12561

Functional cross-linked hemoglobin bis-tetramers: Geometry and cooperativity

Author keywords

[No Author keywords available]

Indexed keywords

AMINES; BINDING ENERGY; BINDING SITES; BIOCHEMISTRY; CIVIL AVIATION; DICHROISM; HEMOGLOBIN; MATERIALS PROPERTIES; OPTICAL PROPERTIES; OXYGEN; PORPHYRINS;

EID: 56749117870     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801452b     Document Type: Article
Times cited : (40)

References (42)
  • 1
    • 0035465476 scopus 로고    scopus 로고
    • Oxygen Carriers ("Blood Substitutes")- Raison d'Etre, Chemistry, and Some Physiology
    • Riess, J. G. (2001) Oxygen Carriers ("Blood Substitutes")- Raison d'Etre, Chemistry, and Some Physiology. Chem. Rev. 101, 2797-2919.
    • (2001) Chem. Rev , vol.101 , pp. 2797-2919
    • Riess, J.G.1
  • 2
    • 0037885022 scopus 로고    scopus 로고
    • Current status of blood substitute research: Towards a new paradigm
    • Winslow, R. M. (2003) Current status of blood substitute research: towards a new paradigm. J. Intern. Med. 253, 508-517.
    • (2003) J. Intern. Med , vol.253 , pp. 508-517
    • Winslow, R.M.1
  • 3
    • 4844221727 scopus 로고    scopus 로고
    • Toxicities of hemoglobin solutions: In search of in-vitro and in-vivo model systems
    • Buehler, P. W., and Alayash, A. I. (2004) Toxicities of hemoglobin solutions: in search of in-vitro and in-vivo model systems. Transfusion 44, 1516-1530.
    • (2004) Transfusion , vol.44 , pp. 1516-1530
    • Buehler, P.W.1    Alayash, A.I.2
  • 4
    • 0343852124 scopus 로고    scopus 로고
    • Site-specific modifications and toxicity of blood substitutes. The case of diaspirin cross-linked hemoglobin
    • D'Agnillo, F., and Alayash, A. I. (2000) Site-specific modifications and toxicity of blood substitutes. The case of diaspirin cross-linked hemoglobin. Adv. Drug Deliv. Rev. 40, 199-212.
    • (2000) Adv. Drug Deliv. Rev , vol.40 , pp. 199-212
    • D'Agnillo, F.1    Alayash, A.I.2
  • 5
    • 0033022393 scopus 로고    scopus 로고
    • Hemoglobin-based blood substitutes: Oxygen carriers, pressor agents, or oxidants?
    • Alayash, A. I. (1999) Hemoglobin-based blood substitutes: oxygen carriers, pressor agents, or oxidants? Nat. Biotechnol. 17, 545-549.
    • (1999) Nat. Biotechnol , vol.17 , pp. 545-549
    • Alayash, A.I.1
  • 6
    • 44249093233 scopus 로고    scopus 로고
    • Cell-free hemoglobin-based blood substitutes and risk of myocardial infarction and death. A meta-analysis
    • Natanson, C., Kern, S. J., Lurie, P., Banks, S. M., and Wolfe, S. M. (2008) Cell-free hemoglobin-based blood substitutes and risk of myocardial infarction and death. A meta-analysis. J. Am. Med. Assoc. 299, 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
  • 8
    • 0029316370 scopus 로고
    • Contractile effects of diaspirin cross-linked hemoglobin (DCLHb) on isolated porcine blood vessels
    • Freas, W., Llave, R., Jing, M., Hart, J., McQuillan, P., and Muldoon, S. (1995) Contractile effects of diaspirin cross-linked hemoglobin (DCLHb) on isolated porcine blood vessels. J. Lab. Clin. Med. 125, 762-767.
    • (1995) J. Lab. Clin. Med , vol.125 , pp. 762-767
    • Freas, W.1    Llave, R.2    Jing, M.3    Hart, J.4    McQuillan, P.5    Muldoon, S.6
  • 9
    • 0027251288 scopus 로고
    • Systemic and pulmonary hypertension after resuscitation with cell-free hemoglobin
    • Hess, J. R., MacDonald, V. W., and Brinkley, W. W. (1993) Systemic and pulmonary hypertension after resuscitation with cell-free hemoglobin. J. Appl. Physiol. 74, 1769-1778.
    • (1993) J. Appl. Physiol , vol.74 , pp. 1769-1778
    • Hess, J.R.1    MacDonald, V.W.2    Brinkley, W.W.3
  • 11
    • 0036785040 scopus 로고    scopus 로고
    • Vascular response to infusions of a nonextravasating hemoglobin polymer
    • Matheson, B., Kwansa, H. E., Bucci, E., Rebel, A., and Koehler, R. C. (2002) Vascular response to infusions of a nonextravasating hemoglobin polymer. J. Appl. Physiol. 93, 1479-1486.
    • (2002) J. Appl. Physiol , vol.93 , pp. 1479-1486
    • Matheson, B.1    Kwansa, H.E.2    Bucci, E.3    Rebel, A.4    Koehler, R.C.5
  • 12
    • 34249317587 scopus 로고    scopus 로고
    • Toxicity and hemodynamic effects after single dose administration of MalPEG-hemoglobin (MP4) in rhesus monkeys
    • Young, M. A., Malavalli, A., Winslow, N., Vandegriff, K. D., and Winslow, R. M. (2007) Toxicity and hemodynamic effects after single dose administration of MalPEG-hemoglobin (MP4) in rhesus monkeys. Transl. Res. 149, 333-342.
    • (2007) Transl. Res. 149 , pp. 333-342
    • Young, M.A.1    Malavalli, A.2    Winslow, N.3    Vandegriff, K.D.4    Winslow, R.M.5
  • 13
    • 0036785040 scopus 로고    scopus 로고
    • Vascular response to infusions of a nonextravasating hemoglobin polymer
    • Matheson, B., Kwansa, H. E., Bucci, E., Rebel, A., and Koehler, R. C. (2002) Vascular response to infusions of a nonextravasating hemoglobin polymer. J. Appl. Physiol. 93, 1479-1486.
    • (2002) J. Appl. Physiol , vol.93 , pp. 1479-1486
    • Matheson, B.1    Kwansa, H.E.2    Bucci, E.3    Rebel, A.4    Koehler, R.C.5
  • 14
    • 20444385158 scopus 로고    scopus 로고
    • Structural and functional characterization of glutaraldehyde-polymerized bovine hemoglobin and its isolated fractions
    • Buehler, P. W., Boykins, R. A., Jia, Y., Norris, S., Freedberg, D. I., and Alayash, A. I. (2005) Structural and functional characterization of glutaraldehyde-polymerized bovine hemoglobin and its isolated fractions. Anal. Chem. 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
  • 15
    • 18844444557 scopus 로고    scopus 로고
    • O-raffinose crosslinked hemoglobin lacks site-specific chemistry in the central cavity: Structural and functional consequences of b93Cys modification. Proteins: Struct., Funct
    • Boykins, R. A., Buehler, P. W., Jia, Y., Venable, R., and Alayash, A. I. (2005) O-raffinose crosslinked hemoglobin lacks site-specific chemistry in the central cavity: Structural and functional consequences of b93Cys modification. Proteins: Struct., Funct., Bioinformatics 59, 840-855.
    • (2005) Bioinformatics , vol.59 , pp. 840-855
    • Boykins, R.A.1    Buehler, P.W.2    Jia, Y.3    Venable, R.4    Alayash, A.I.5
  • 16
    • 4344592222 scopus 로고    scopus 로고
    • MP4, a new nonvasoactive polyethylene glycol-hemoglobin conjugate
    • Winslow, R. M. (2004) MP4, a new nonvasoactive polyethylene glycol-hemoglobin conjugate. Artif. Organs 28, 800-806.
    • (2004) Artif. Organs , vol.28 , pp. 800-806
    • Winslow, R.M.1
  • 17
    • 0028533182 scopus 로고
    • 1994 Syntex Award Lecture. Anionic electrophiles, protein modification, and artificial blood
    • Kluger, R. (1994) 1994 Syntex Award Lecture. Anionic electrophiles, protein modification, and artificial blood. Can. J. Chem. 72, 2193-2197.
    • (1994) Can. J. Chem. 72 , pp. 2193-2197
    • Kluger, R.1
  • 18
    • 0036213559 scopus 로고    scopus 로고
    • 2001 Lemieux award lecture. Organic chemistry and hemoglobin: Benefits from controlled alteration
    • Kluger, R. (2002) 2001 Lemieux award lecture. Organic chemistry and hemoglobin: benefits from controlled alteration. Can. J. Chem. 80, 217-221.
    • (2002) Can. J. Chem. 80 , pp. 217-221
    • Kluger, R.1
  • 19
    • 8644282069 scopus 로고    scopus 로고
    • Chemical cross-linking and protein-protein interactions-a review with illustrative protocols
    • Kluger, R., and Alagic, A. (2004) Chemical cross-linking and protein-protein interactions-a review with illustrative protocols. Bioorg. Chem. 32, 451-472.
    • (2004) Bioorg. Chem , vol.32 , pp. 451-472
    • Kluger, R.1    Alagic, A.2
  • 20
    • 0033612730 scopus 로고    scopus 로고
    • Connecting proteins by design. Cross-linked bis-hemoglobin
    • Kluger, R., Lock-O'Brien, J., and Teytelboym, A. (1999) Connecting proteins by design. Cross-linked bis-hemoglobin. J. Am. Chem. Soc. 121, 6780-6785.
    • (1999) J. Am. Chem. Soc , vol.121 , pp. 6780-6785
    • Kluger, R.1    Lock-O'Brien, J.2    Teytelboym, A.3
  • 21
    • 0033972378 scopus 로고    scopus 로고
    • Mechanism of site-directed protein cross-linking. Protein-directed selectivity in reactions of hemoglobin with aryl trimesates
    • Kluger, R., and De Stefano, V. (2000) Mechanism of site-directed protein cross-linking. Protein-directed selectivity in reactions of hemoglobin with aryl trimesates. J. Org. Chem. 65, 214-219.
    • (2000) J. Org. Chem , vol.65 , pp. 214-219
    • Kluger, R.1    De Stefano, V.2
  • 22
    • 37149039501 scopus 로고    scopus 로고
    • Efficient generation of dendritic arrays of cross-linked hemoglobin: Symmetry and redundancy
    • Hu, D., and Kluger, R. (2008) Efficient generation of dendritic arrays of cross-linked hemoglobin: symmetry and redundancy. Org. Biomol. Chem. 6, 151-156.
    • (2008) Org. Biomol. Chem , vol.6 , pp. 151-156
    • Hu, D.1    Kluger, R.2
  • 23
    • 0043236018 scopus 로고    scopus 로고
    • Crosslinked bis-hemoglobins: Connections and oxygen binding
    • Gourianov, N., and Kluger, R. (2003) Crosslinked bis-hemoglobins: connections and oxygen binding. J. Am. Chem. Soc. 125, 10885-10892.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 10885-10892
    • Gourianov, N.1    Kluger, R.2
  • 24
    • 27744479440 scopus 로고    scopus 로고
    • Conjoined hemoglobins. Loss of cooperativity and protein-protein interactions
    • Gourianov, N., and Kluger, R. (2005) Conjoined hemoglobins. Loss of cooperativity and protein-protein interactions. Biochemistry 44, 14989-14999.
    • (2005) Biochemistry , vol.44 , pp. 14989-14999
    • Gourianov, N.1    Kluger, R.2
  • 25
    • 34247621783 scopus 로고    scopus 로고
    • A quantitative framework for the design of acellular hemoglobins as blood substitutes: Implications of dynamic flow conditions
    • Cole, R. H., Vandegriff, K. D., Szeri, A. J., Savas, O., Baker, D. A., and Winslow, R. M. (2007) A quantitative framework for the design of acellular hemoglobins as blood substitutes: Implications of dynamic flow conditions. Biophys. Chem. 128, 63-74.
    • (2007) Biophys. Chem , vol.128 , pp. 63-74
    • Cole, R.H.1    Vandegriff, K.D.2    Szeri, A.J.3    Savas, O.4    Baker, D.A.5    Winslow, R.M.6
  • 27
    • 0009813746 scopus 로고
    • Extinction coefficient of human hemiglobincyanide
    • Salvati, A. M., Tentori, L., and Vivaldi, G. (1965) Extinction coefficient of human hemiglobincyanide. Clin. Chim. Acta 11, 477-479.
    • (1965) Clin. Chim. Acta , vol.11 , pp. 477-479
    • Salvati, A.M.1    Tentori, L.2    Vivaldi, G.3
  • 28
    • 0028306493 scopus 로고
    • Structural characterization of modified hemoglobins
    • Jones, R. T. (1994) Structural characterization of modified hemoglobins. Methods Enzymol. 231, 322-343.
    • (1994) Methods Enzymol , vol.231 , pp. 322-343
    • Jones, R.T.1
  • 29
    • 0021360601 scopus 로고
    • Alternative diaspirins for modification of hemoglobin and sickle hemoglobin
    • Delaney, E. J., Massil, S. E., Shi, G. Y., and Klotz, I. M. (1984) Alternative diaspirins for modification of hemoglobin and sickle hemoglobin. Arch. Biochem. Biophys. 228, 627-638.
    • (1984) Arch. Biochem. Biophys , vol.228 , pp. 627-638
    • Delaney, E.J.1    Massil, S.E.2    Shi, G.Y.3    Klotz, I.M.4
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T-4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T-4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 31
    • 0019167803 scopus 로고
    • Reverse-phase high-performance liquid chromatography of proteins: The separation of hemoglobin chain variants
    • Petrides, P. E., Jones, R. T., and Boehlen, P. (1980) Reverse-phase high-performance liquid chromatography of proteins: the separation of hemoglobin chain variants. Anal. Biochem. 105, 383-388.
    • (1980) Anal. Biochem , vol.105 , pp. 383-388
    • Petrides, P.E.1    Jones, R.T.2    Boehlen, P.3
  • 32
    • 0021286911 scopus 로고
    • High performance liquid chromatographic separation of globin chains on a large-pore C4 column
    • Shelton, J. B., Shelton, J. R., and Schroeder, W. A. (1969) (1984) High performance liquid chromatographic separation of globin chains on a large-pore C4 column. J. Liq. Chromatogr. 7 1977.
    • (1969) J. Liq. Chromatogr , vol.7 , pp. 1977
    • Shelton, J.B.1    Shelton, J.R.2    Schroeder, W.A.3
  • 33
    • 0032126013 scopus 로고    scopus 로고
    • Renal response to hemodilution with albumin or crosslinked bovine hemoglobin: Role of nitric oxide
    • Matheson, B., Razynska, A., O'Hearne, M., and Bucci, E. (1998) Renal response to hemodilution with albumin or crosslinked bovine hemoglobin: role of nitric oxide. J. Lab. Clin. Med. 132, 47-53.
    • (1998) J. Lab. Clin. Med , vol.132 , pp. 47-53
    • Matheson, B.1    Razynska, A.2    O'Hearne, M.3    Bucci, E.4
  • 34
    • 0027505550 scopus 로고
    • Modification of human hemoglobin with methyl acyl phosphates derived from dicarboxylic acids. Systematic relationships between cross-linked structure and oxygen-binding properties
    • Jones, R. T., Head, C. G., Fujita, T. S., Shih, D. T. B., Wodzinska, J., and Kluger, R. (1993) Modification of human hemoglobin with methyl acyl phosphates derived from dicarboxylic acids. Systematic relationships between cross-linked structure and oxygen-binding properties. Biochemistry 32, 215-223.
    • (1993) Biochemistry , vol.32 , pp. 215-223
    • Jones, R.T.1    Head, C.G.2    Fujita, T.S.3    Shih, D.T.B.4    Wodzinska, J.5    Kluger, R.6
  • 35
    • 0014958182 scopus 로고
    • Stereochemistry of cooperative effects in haemoglobin
    • Perutz, M. F. (1970) Stereochemistry of cooperative effects in haemoglobin. Nature 228, 726-739.
    • (1970) Nature , vol.228 , pp. 726-739
    • Perutz, M.F.1
  • 36
    • 0028111599 scopus 로고
    • Properties of a recombinant human hemoglobin double mutant: Sickle hemoglobin with Leu-88(b) at the primary aggregation site substituted by Ala
    • De Lano, J. J. M., and Manning, J. M. (1994) Properties of a recombinant human hemoglobin double mutant: sickle hemoglobin with Leu-88(b) at the primary aggregation site substituted by Ala. Protein Sci. 3, 1206-1212.
    • (1994) Protein Sci , vol.3 , pp. 1206-1212
    • De Lano, J.J.M.1    Manning, J.M.2
  • 37
    • 0006662187 scopus 로고
    • Methyl acetyl phosphate. A small anionic acetylating agent
    • Kluger, R., and Tsui, W.-G (1980) Methyl acetyl phosphate. A small anionic acetylating agent. J. Org. Chem. 45, 2723-2724.
    • (1980) J. Org. Chem , vol.45 , pp. 2723-2724
    • Kluger, R.1    Tsui, W.-G.2
  • 38
    • 0001553768 scopus 로고
    • Dicarboxylic acid bis(methyl phosphates): Anionic biomimetic crosslinking reagents
    • Kluger, R., Grant, A. S., Bearne, S. L., and Trachsel, M. R. (1990) Dicarboxylic acid bis(methyl phosphates): anionic biomimetic crosslinking reagents. J. Org. Chem. 55, 2864-2868.
    • (1990) J. Org. Chem , vol.55 , pp. 2864-2868
    • Kluger, R.1    Grant, A.S.2    Bearne, S.L.3    Trachsel, M.R.4
  • 39
    • 0001633397 scopus 로고
    • Trimesoyltris(3,5-dibromosalicylate): Specificity of reactions of a trifunctional acylating agent with hemoglobin
    • Kluger, R., Song, Y., Wodzinska, J., Head, C., Fujita, T. S., and Jones, R. T. (1992) Trimesoyltris(3,5-dibromosalicylate): specificity of reactions of a trifunctional acylating agent with hemoglobin. J. Am. Chem. Soc. 114, 9275-9279.
    • (1992) J. Am. Chem. Soc , vol.114 , pp. 9275-9279
    • Kluger, R.1    Song, Y.2    Wodzinska, J.3    Head, C.4    Fujita, T.S.5    Jones, R.T.6
  • 40
    • 0029813464 scopus 로고    scopus 로고
    • Systematically cross-linked human hemoglobin: Functional effects of 10 Å spans between beta subunits at lysine-82
    • Kluger, R., Shen, L., Xiao, H., and Jones, R. T. (1996) Systematically cross-linked human hemoglobin: Functional effects of 10 Å spans between beta subunits at lysine-82. J. Am. Chem. Soc. 118, 8782-8786.
    • (1996) J. Am. Chem. Soc , vol.118 , pp. 8782-8786
    • Kluger, R.1    Shen, L.2    Xiao, H.3    Jones, R.T.4
  • 41
    • 34247621783 scopus 로고    scopus 로고
    • A quantitative framework for the design of acellular hemoglobins as blood substitutes: Implications of dynamic flow conditions
    • Cole, R. H., Vandegriff, K. D., Szeri, A. J., Savas, O., Baker, D. A., and Winslow, R. M. (2007) A quantitative framework for the design of acellular hemoglobins as blood substitutes: Implications of dynamic flow conditions. Biophys. Chem. 128, 63-74.
    • (2007) Biophys. Chem , vol.128 , pp. 63-74
    • Cole, R.H.1    Vandegriff, K.D.2    Szeri, A.J.3    Savas, O.4    Baker, D.A.5    Winslow, R.M.6
  • 42
    • 0032921026 scopus 로고    scopus 로고
    • Is cooperative oxygen binding by hemoglobin really understood?
    • Eaton, W. A., Henry, E. R., Hofrichter, J., and Mozzarelli, A. (1999) Is cooperative oxygen binding by hemoglobin really understood? Nat. Struct. Biol. 6, 351-358.
    • (1999) Nat. Struct. Biol , vol.6 , pp. 351-358
    • Eaton, W.A.1    Henry, E.R.2    Hofrichter, J.3    Mozzarelli, A.4


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