메뉴 건너뛰기




Volumn 1784, Issue 10, 2008, Pages 1365-1377

Ligand reactivity and allosteric regulation of hemoglobin-based oxygen carriers

Author keywords

(propyl PEG2k)6 Hb; (propyl PEG5k)6 Hb; 2,3 diphosphoglicerate; Allosteric properties; bezafibrate; BZF; carbonmonoxy Hb; DPG; HbCO; Hemoglobin; hemoglobin PEGylated with 6 PEG 2000 chains by reductive alkylation chemistry; hemoglobin PEGylated with 6 PEG 5000 chains by reductive alkylation chemistry; IHP; inositol hexaphosphate; Monod, Wyman and Changeux; MWC; nitric oxide; NO; Oxygen binding; oxygen partial pressure; PEG; pO2; polyethylene glycol; Silica gel; Tertiary conformation; Tertiary Two State model; TTS model

Indexed keywords

BEZAFIBRATE; BLOOD SUBSTITUTE; DEOXYHEMOGLOBIN; HEMOGLOBIN; HEMOGLOBIN BASED OXYGEN CARRIER; HEMOGLOBIN GLUTAMER 200; HEMOSPAN; LIPOSOME; MACROGOL; NANOPARTICLE; NITRIC OXIDE; POLYMERIZED HEMOGLOBIN; RECOMBINANT HEMOGLOBIN; UNCLASSIFIED DRUG;

EID: 52349088745     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.04.021     Document Type: Review
Times cited : (23)

References (222)
  • 1
    • 33745926240 scopus 로고    scopus 로고
    • Blood substitutes based on nanobiotechnology
    • Chang T.M. Blood substitutes based on nanobiotechnology. Trends Biotechnol. 24 (2006) 372-377
    • (2006) Trends Biotechnol. , vol.24 , pp. 372-377
    • Chang, T.M.1
  • 3
    • 0001382516 scopus 로고
    • Injection of hemoglobin in man and its relation to blood distribution, with special reference to the anemias
    • Sellards A.W., and Minot G.R. Injection of hemoglobin in man and its relation to blood distribution, with special reference to the anemias. J. Med. Res. 34 (1916) 469-494
    • (1916) J. Med. Res. , vol.34 , pp. 469-494
    • Sellards, A.W.1    Minot, G.R.2
  • 4
    • 0001166627 scopus 로고
    • Clinical experience with hemoglobin-saline solutions
    • Amberson W.R., Jennings J.J., and Rhode C.M. Clinical experience with hemoglobin-saline solutions. J. Appl. Physiol. 1 (1949) 469-489
    • (1949) J. Appl. Physiol. , vol.1 , pp. 469-489
    • Amberson, W.R.1    Jennings, J.J.2    Rhode, C.M.3
  • 6
    • 34248161572 scopus 로고    scopus 로고
    • First-generation blood substitutes: what have we learned? Biochemical and physiological perspectives
    • Alayash A.I., D'Agnillo F., and Buehler P.W. First-generation blood substitutes: what have we learned? Biochemical and physiological perspectives. Expert Opin. Biol. Ther. 7 (2007) 665-675
    • (2007) Expert Opin. Biol. Ther. , vol.7 , pp. 665-675
    • Alayash, A.I.1    D'Agnillo, F.2    Buehler, P.W.3
  • 7
    • 52049122011 scopus 로고    scopus 로고
    • Oxygen delivery via allosteric effectors of hemoglobin, blood substitutes and plasma expanders
    • Abraham D. (Ed), John Wiley and Sons, Inc.
    • Campanini B., Bruno S., Raboni S., and Mozzarelli A. Oxygen delivery via allosteric effectors of hemoglobin, blood substitutes and plasma expanders. In: Abraham D. (Ed). Burger's Medicinal Chemistry. 6th edition vol. 3 (2003), John Wiley and Sons, Inc. 385-442
    • (2003) Burger's Medicinal Chemistry. 6th edition , vol.3 , pp. 385-442
    • Campanini, B.1    Bruno, S.2    Raboni, S.3    Mozzarelli, A.4
  • 8
    • 33748188470 scopus 로고    scopus 로고
    • Microvascular perspective of oxygen-carrying and -noncarrying blood substitutes
    • Intaglietta M., Cabrales P., and Tsai A.G. Microvascular perspective of oxygen-carrying and -noncarrying blood substitutes. Annu. Rev. Biomed. Eng. 8 (2006) 289-321
    • (2006) Annu. Rev. Biomed. Eng. , vol.8 , pp. 289-321
    • Intaglietta, M.1    Cabrales, P.2    Tsai, A.G.3
  • 9
    • 7644222814 scopus 로고    scopus 로고
    • Artificial oxygen carriers for trauma: myth or reality
    • Mackenzie C.F., and Bucci C. Artificial oxygen carriers for trauma: myth or reality. Hosp. Med. 65 (2004) 582-588
    • (2004) Hosp. Med. , vol.65 , pp. 582-588
    • Mackenzie, C.F.1    Bucci, C.2
  • 12
    • 33746462251 scopus 로고    scopus 로고
    • Current status of oxygen carriers ('blood substitutes'): 2006
    • Winslow R.M. Current status of oxygen carriers ('blood substitutes'): 2006. Vox Sang. 91 (2006) 102-110
    • (2006) Vox Sang. , vol.91 , pp. 102-110
    • Winslow, R.M.1
  • 13
    • 0033022393 scopus 로고    scopus 로고
    • Hemoglobin-based blood substitutes: oxygen carriers, pressor agents, or oxidants?
    • Alayash A.I. Hemoglobin-based blood substitutes: oxygen carriers, pressor agents, or oxidants?. Nat. Biotechnol. 17 (1999) 545-549
    • (1999) Nat. Biotechnol. , vol.17 , pp. 545-549
    • Alayash, A.I.1
  • 14
    • 0034633998 scopus 로고    scopus 로고
    • Reaction of hydrogen peroxide with ferrylhemoglobin: superoxide production and heme degradation
    • Nagababu E., and Rifkind J.M. Reaction of hydrogen peroxide with ferrylhemoglobin: superoxide production and heme degradation. Biochemistry 39 (2000) 12503-12511
    • (2000) Biochemistry , vol.39 , pp. 12503-12511
    • Nagababu, E.1    Rifkind, J.M.2
  • 15
    • 0034647775 scopus 로고    scopus 로고
    • Heme degradation during autoxidation of oxyhemoglobin
    • Nagababu E., and Rifkind J.M. Heme degradation during autoxidation of oxyhemoglobin. Biochem. Biophys. Res. Commun. 273 (2000) 839-845
    • (2000) Biochem. Biophys. Res. Commun. , vol.273 , pp. 839-845
    • Nagababu, E.1    Rifkind, J.M.2
  • 16
    • 0014408353 scopus 로고
    • Exchange of heme among hemoglobins and between hemoglobin and albumin
    • Bunn H.F., and Jandl J.H. Exchange of heme among hemoglobins and between hemoglobin and albumin. J. Biol. Chem. 243 (1968) 465-475
    • (1968) J. Biol. Chem. , vol.243 , pp. 465-475
    • Bunn, H.F.1    Jandl, J.H.2
  • 17
    • 37649017715 scopus 로고    scopus 로고
    • Clinical implications of the loss of vasoactive nitric oxide during red blood cell storage
    • Bonaventura J. Clinical implications of the loss of vasoactive nitric oxide during red blood cell storage. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 19165-19166
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 19165-19166
    • Bonaventura, J.1
  • 18
    • 1242353138 scopus 로고    scopus 로고
    • Oxygen therapeutics: can we tame haemoglobin?
    • Alayash A.I. Oxygen therapeutics: can we tame haemoglobin?. Nat. Rev. Drug Discov. 3 (2004) 152-159
    • (2004) Nat. Rev. Drug Discov. , vol.3 , pp. 152-159
    • Alayash, A.I.1
  • 20
    • 0035465476 scopus 로고    scopus 로고
    • Oxygen carriers ("blood substitutes"): raison d'etre, chemistry and some physiology
    • Reiss J.G. Oxygen carriers ("blood substitutes"): raison d'etre, chemistry and some physiology. Chem. Rev. 101 (2001) 2797-2919
    • (2001) Chem. Rev. , vol.101 , pp. 2797-2919
    • Reiss, J.G.1
  • 21
    • 0037885022 scopus 로고    scopus 로고
    • Current status of blood substitute research: towards a new paradigm
    • Winslow R.M. Current status of blood substitute research: towards a new paradigm. J. Intern. Med. 253 (2003) 508-517
    • (2003) J. Intern. Med. , vol.253 , pp. 508-517
    • Winslow, R.M.1
  • 26
    • 1342346682 scopus 로고    scopus 로고
    • A theoretical model of nitric oxide transport in arterioles: frequency- vs. amplitude-dependent control of cGMP formation
    • Tsoukias N.M., Kavdia M., and Popel A.S. A theoretical model of nitric oxide transport in arterioles: frequency- vs. amplitude-dependent control of cGMP formation. Am. J. Physiol. Heart. Circ. Physiol. 286 (2004) H1043-H1056
    • (2004) Am. J. Physiol. Heart. Circ. Physiol. , vol.286
    • Tsoukias, N.M.1    Kavdia, M.2    Popel, A.S.3
  • 27
    • 33749499778 scopus 로고    scopus 로고
    • Oxygen therapeutics: oxygen delivery without blood
    • Stollings J.L., and Oyen L.J. Oxygen therapeutics: oxygen delivery without blood. Pharmacotherapy 26 (2006) 1453-1464
    • (2006) Pharmacotherapy , vol.26 , pp. 1453-1464
    • Stollings, J.L.1    Oyen, L.J.2
  • 28
    • 0030874733 scopus 로고    scopus 로고
    • Initial evaluation of diaspirin cross-linked hemoglobin (DCLHb) as a vasopressor in critically ill patients
    • Reah G., Bodenham A.R., Mallick A., Daily E.K., and Przybelski R.J. Initial evaluation of diaspirin cross-linked hemoglobin (DCLHb) as a vasopressor in critically ill patients. Crit. Care. Med. 25 (1997) 1480-1488
    • (1997) Crit. Care. Med. , vol.25 , pp. 1480-1488
    • Reah, G.1    Bodenham, A.R.2    Mallick, A.3    Daily, E.K.4    Przybelski, R.J.5
  • 29
    • 0033224584 scopus 로고    scopus 로고
    • Nitric oxide scavengers in the treatment of shock associated with systemic inflammatory response syndrome
    • De Angelo J. Nitric oxide scavengers in the treatment of shock associated with systemic inflammatory response syndrome. Expert Opin. Pharmacother. 1 (1999) 19-29
    • (1999) Expert Opin. Pharmacother. , vol.1 , pp. 19-29
    • De Angelo, J.1
  • 31
    • 33847797129 scopus 로고    scopus 로고
    • Engineering blood cells and proteins as blood substitutes: a short review
    • Kim H.W. Engineering blood cells and proteins as blood substitutes: a short review. Biotechnol. Bioprocess Eng. 12 (2007) 43-47
    • (2007) Biotechnol. Bioprocess Eng. , vol.12 , pp. 43-47
    • Kim, H.W.1
  • 32
    • 0036839090 scopus 로고    scopus 로고
    • Hemoglobin-based oxygen carriers
    • Stowell C.P. Hemoglobin-based oxygen carriers. Curr. Opin. Hematol. 9 (2002) 537-543
    • (2002) Curr. Opin. Hematol. , vol.9 , pp. 537-543
    • Stowell, C.P.1
  • 38
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: a plausible model
    • Monod J., Wyman J., and Changeux J.P. On the nature of allosteric transitions: a plausible model. J. Mol. Biol. 12 (1965) 88-118
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 39
    • 0000610156 scopus 로고
    • Structure of haemoglobin. A three-dimensional fourier synthesis of reduced human haemoglobin at 5.5 Å resolution
    • Muirhead H., and Perutz M.F. Structure of haemoglobin. A three-dimensional fourier synthesis of reduced human haemoglobin at 5.5 Å resolution. Nature 199 (1963) 633-638
    • (1963) Nature , vol.199 , pp. 633-638
    • Muirhead, H.1    Perutz, M.F.2
  • 40
    • 0001372229 scopus 로고
    • Structure of haemoglobin. An X-ray examination of reduced horse haemoglobin
    • Perutz M.F., Bolton W., Diamond R., Muirhead H., and Watson H.C. Structure of haemoglobin. An X-ray examination of reduced horse haemoglobin. Nature 203 (1964) 687-690
    • (1964) Nature , vol.203 , pp. 687-690
    • Perutz, M.F.1    Bolton, W.2    Diamond, R.3    Muirhead, H.4    Watson, H.C.5
  • 41
    • 0000450916 scopus 로고
    • The oxygen equilibrium of hemoglobin and its structural interpretation
    • Pauling L. The oxygen equilibrium of hemoglobin and its structural interpretation. Proc. Natl. Acad. Sci. U. S. A. 21 (1935) 186-191
    • (1935) Proc. Natl. Acad. Sci. U. S. A. , vol.21 , pp. 186-191
    • Pauling, L.1
  • 42
    • 0013863816 scopus 로고
    • Comparison of experimental binding data and theoretical models in proteins containing subunits
    • Koshland Jr. D.E., Nemethy G., and Filmer D. Comparison of experimental binding data and theoretical models in proteins containing subunits. Biochemistry 5 (1966) 365-385
    • (1966) Biochemistry , vol.5 , pp. 365-385
    • Koshland Jr., D.E.1    Nemethy, G.2    Filmer, D.3
  • 43
    • 0025801633 scopus 로고
    • Crystals of hemoglobin with the T-quarternary structure bind oxygen noncooperatively with no Bohr effect
    • Mozzarelli A., Rivetti C., Rossi G.L., Henry E.R., and Eaton W.A. Crystals of hemoglobin with the T-quarternary structure bind oxygen noncooperatively with no Bohr effect. Nature 351 (1991) 416-419
    • (1991) Nature , vol.351 , pp. 416-419
    • Mozzarelli, A.1    Rivetti, C.2    Rossi, G.L.3    Henry, E.R.4    Eaton, W.A.5
  • 46
    • 0029163340 scopus 로고
    • Fixation of the quaternary structures of human adult haemoglobin by encapsulation in transparent porous silica gels
    • Shibayama N., and Saigo S. Fixation of the quaternary structures of human adult haemoglobin by encapsulation in transparent porous silica gels. J. Mol. Biol. 251 (1995) 203-209
    • (1995) J. Mol. Biol. , vol.251 , pp. 203-209
    • Shibayama, N.1    Saigo, S.2
  • 47
    • 0031463937 scopus 로고    scopus 로고
    • T state hemoglobin binds oxygen noncooperatively with allosteric effects of protons, inositol hexaphosphate, and chloride
    • Bettati S., and Mozzarelli A. T state hemoglobin binds oxygen noncooperatively with allosteric effects of protons, inositol hexaphosphate, and chloride. J. Biol. Chem. 272 (1997) 32050-32055
    • (1997) J. Biol. Chem. , vol.272 , pp. 32050-32055
    • Bettati, S.1    Mozzarelli, A.2
  • 48
    • 0031048477 scopus 로고    scopus 로고
    • Allosteric effectors do not alter the oxygen affinity of hemoglobin crystals
    • Mozzarelli A., Rivetti C., Rossi G.L., Eaton W.A., and Henry E.R. Allosteric effectors do not alter the oxygen affinity of hemoglobin crystals. Protein Sci. 6 (1997) 484-489
    • (1997) Protein Sci. , vol.6 , pp. 484-489
    • Mozzarelli, A.1    Rivetti, C.2    Rossi, G.L.3    Eaton, W.A.4    Henry, E.R.5
  • 52
    • 0023426568 scopus 로고
    • Oxygen-organophosphate linkage in hemoglobin A. The double hump effect
    • Kister J., Poyart C., and Edelstein S.J. Oxygen-organophosphate linkage in hemoglobin A. The double hump effect. Biophys. J. 52 (1987) 527-535
    • (1987) Biophys. J. , vol.52 , pp. 527-535
    • Kister, J.1    Poyart, C.2    Edelstein, S.J.3
  • 53
    • 0023257012 scopus 로고
    • An expanded two-state allosteric model for interactions of human hemoglobin A with nonsaturating concentrations of 2,3-diphosphoglycerate
    • Kister J., Poyart C., and Edelstein S.J. An expanded two-state allosteric model for interactions of human hemoglobin A with nonsaturating concentrations of 2,3-diphosphoglycerate. J. Biol. Chem. 262 (1987) 12085-12091
    • (1987) J. Biol. Chem. , vol.262 , pp. 12085-12091
    • Kister, J.1    Poyart, C.2    Edelstein, S.J.3
  • 54
    • 0025343392 scopus 로고
    • Effectors of hemoglobin - separation of allosteric and affinity factors
    • Marden M.C., Bohn B., Kister J., and Poyart C. Effectors of hemoglobin - separation of allosteric and affinity factors. Biophys. J. 57 (1990) 397-403
    • (1990) Biophys. J. , vol.57 , pp. 397-403
    • Marden, M.C.1    Bohn, B.2    Kister, J.3    Poyart, C.4
  • 55
    • 0037072945 scopus 로고    scopus 로고
    • Global allostery model of hemoglobin - modulation of O2 affinity, cooperativity, and Bohr effect by heterotropic allosteric effectors
    • Yonetani T., Park S., Tsuneshige A., Imai K., and Kanaori K. Global allostery model of hemoglobin - modulation of O2 affinity, cooperativity, and Bohr effect by heterotropic allosteric effectors. J. Biol. Chem. 277 (2002) 34508-34520
    • (2002) J. Biol. Chem. , vol.277 , pp. 34508-34520
    • Yonetani, T.1    Park, S.2    Tsuneshige, A.3    Imai, K.4    Kanaori, K.5
  • 56
    • 0037054844 scopus 로고    scopus 로고
    • Heterotropic effectors control the hemoglobin function by interacting with its T and R states - a new view on the principle of allostery
    • Tsuneshige A., Park S., and Yonetani T. Heterotropic effectors control the hemoglobin function by interacting with its T and R states - a new view on the principle of allostery. Biophys. Chem. 98 (2002) 49-63
    • (2002) Biophys. Chem. , vol.98 , pp. 49-63
    • Tsuneshige, A.1    Park, S.2    Yonetani, T.3
  • 57
    • 0037054871 scopus 로고    scopus 로고
    • Description of hemoglobin oxygenation under universal solution conditions by a global allostery model with a single adjustable parameter
    • Imai K., Tsuneshige A., and Yonetani T. Description of hemoglobin oxygenation under universal solution conditions by a global allostery model with a single adjustable parameter. Biophys. Chem. 98 (2002) 79-91
    • (2002) Biophys. Chem. , vol.98 , pp. 79-91
    • Imai, K.1    Tsuneshige, A.2    Yonetani, T.3
  • 58
    • 0141717848 scopus 로고    scopus 로고
    • The global allostery model of hemoglobin: an allosteric mechanism involving homotropic and heterotropic interactions
    • Yonetani T., and Tsuneshige A. The global allostery model of hemoglobin: an allosteric mechanism involving homotropic and heterotropic interactions. C. R. Biol. 326 (2003) 523-532
    • (2003) C. R. Biol. , vol.326 , pp. 523-532
    • Yonetani, T.1    Tsuneshige, A.2
  • 59
    • 10344255690 scopus 로고    scopus 로고
    • Semihemoglobins, high oxygen affinity dimeric forms of human hemoglobin respond efficiently to allosteric effectors without forming tetramers
    • Tsuneshige A., Kanaori K., Samuni U., Danstker D., Friedman J.M., Neya S., Giangiacomo L., and Yonetani T. Semihemoglobins, high oxygen affinity dimeric forms of human hemoglobin respond efficiently to allosteric effectors without forming tetramers. J. Biol. Chem. 279 (2004) 48959-48967
    • (2004) J. Biol. Chem. , vol.279 , pp. 48959-48967
    • Tsuneshige, A.1    Kanaori, K.2    Samuni, U.3    Danstker, D.4    Friedman, J.M.5    Neya, S.6    Giangiacomo, L.7    Yonetani, T.8
  • 60
    • 0016157532 scopus 로고
    • Influence of globin structure on the state of the heme. II. Allosteric transitions in methemoglobin
    • Perutz M.F., Fersht A.R., Simon S.R., and Roberts G.C. Influence of globin structure on the state of the heme. II. Allosteric transitions in methemoglobin. Biochemistry 13 (1974) 2174-2186
    • (1974) Biochemistry , vol.13 , pp. 2174-2186
    • Perutz, M.F.1    Fersht, A.R.2    Simon, S.R.3    Roberts, G.C.4
  • 61
    • 0016258287 scopus 로고
    • Influence of globin structure on the state of the heme. I. Human deoxyhemoglobin
    • Perutz M.F., Ladner J.E., Simon S.R., and Ho C. Influence of globin structure on the state of the heme. I. Human deoxyhemoglobin. Biochemistry 13 (1974) 2163-2173
    • (1974) Biochemistry , vol.13 , pp. 2163-2173
    • Perutz, M.F.1    Ladner, J.E.2    Simon, S.R.3    Ho, C.4
  • 62
    • 33746563394 scopus 로고    scopus 로고
    • Circular dichroism spectroscopy of tertiary and quaternary conformations of human hemoglobin entrapped in wet silica gels
    • Ronda L., Bruno S., Viappiani C., Abbruzzetti S., Mozzarelli A., Lowe K.C., and Bettati S. Circular dichroism spectroscopy of tertiary and quaternary conformations of human hemoglobin entrapped in wet silica gels. Protein Sci. 15 (2006) 1961-1967
    • (2006) Protein Sci. , vol.15 , pp. 1961-1967
    • Ronda, L.1    Bruno, S.2    Viappiani, C.3    Abbruzzetti, S.4    Mozzarelli, A.5    Lowe, K.C.6    Bettati, S.7
  • 63
    • 0037064138 scopus 로고    scopus 로고
    • Crystal structure of horse carbonmonoxyhemoglobin-bezafibrate complex at 1.55-angstrom resolution - a novel allosteric binding site in R-state hemoglobin
    • Shibayama N., Miura S., Tame J.R.H., Yonetani T., and Park S.Y. Crystal structure of horse carbonmonoxyhemoglobin-bezafibrate complex at 1.55-angstrom resolution - a novel allosteric binding site in R-state hemoglobin. J. Biol. Chem. 277 (2002) 38791-38796
    • (2002) J. Biol. Chem. , vol.277 , pp. 38791-38796
    • Shibayama, N.1    Miura, S.2    Tame, J.R.H.3    Yonetani, T.4    Park, S.Y.5
  • 64
    • 31344438645 scopus 로고    scopus 로고
    • R-state haemoglobin with low oxygen affinity: crystal structures of deoxy human and carbonmonoxy horse haemoglobin bound to the effector molecule L35
    • Yokoyama T., Neya S., Tsuneshige A., Yonetani T., Park S.Y., and Tame J.R. R-state haemoglobin with low oxygen affinity: crystal structures of deoxy human and carbonmonoxy horse haemoglobin bound to the effector molecule L35. J. Mol. Biol. 356 (2006) 790-801
    • (2006) J. Mol. Biol. , vol.356 , pp. 790-801
    • Yokoyama, T.1    Neya, S.2    Tsuneshige, A.3    Yonetani, T.4    Park, S.Y.5    Tame, J.R.6
  • 65
    • 0022634647 scopus 로고
    • Hemoglobin as a receptor of drugs and peptides: X-ray studies of the stereochemistry of binding
    • Perutz M.F., Fermi G., Abraham D.J., Poyart C., and Bursaux E. Hemoglobin as a receptor of drugs and peptides: X-ray studies of the stereochemistry of binding. J. Am. Chem. Soc. 108 (1986) 1064-1078
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 1064-1078
    • Perutz, M.F.1    Fermi, G.2    Abraham, D.J.3    Poyart, C.4    Bursaux, E.5
  • 66
    • 33745571654 scopus 로고    scopus 로고
    • 1.25 Angstrom resolution crystal structures of human haemoglobin in the oxy, deoxy and carbonmonoxy forms
    • Park S.Y., Yokoyama T., Shibayama N., Shiro Y., and Tame J.R.H. 1.25 Angstrom resolution crystal structures of human haemoglobin in the oxy, deoxy and carbonmonoxy forms. J. Mol. Biol. 360 (2006) 690-701
    • (2006) J. Mol. Biol. , vol.360 , pp. 690-701
    • Park, S.Y.1    Yokoyama, T.2    Shibayama, N.3    Shiro, Y.4    Tame, J.R.H.5
  • 67
    • 1942502768 scopus 로고    scopus 로고
    • Domain-specific effector interactions within the central cavity of human adult hemoglobin in solution and in porous sol-gel matrices: evidence for long-range communication pathways
    • Peterson E.S., Shinder R., Khan I., Juczszak L., Wang J., Manjula B., Acharya S.A., Bonaventura C., and Friedman J.M. Domain-specific effector interactions within the central cavity of human adult hemoglobin in solution and in porous sol-gel matrices: evidence for long-range communication pathways. Biochemistry 43 (2004) 4832-4843
    • (2004) Biochemistry , vol.43 , pp. 4832-4843
    • Peterson, E.S.1    Shinder, R.2    Khan, I.3    Juczszak, L.4    Wang, J.5    Manjula, B.6    Acharya, S.A.7    Bonaventura, C.8    Friedman, J.M.9
  • 69
    • 0026795182 scopus 로고
    • A 3rd quaternary structure of human hemoglobin A at 1.7-Å resolution
    • Silva M.M., Rogers P.H., and Arnone A. A 3rd quaternary structure of human hemoglobin A at 1.7-Å resolution. J. Biol. Chem. 267 (1992) 17248-17256
    • (1992) J. Biol. Chem. , vol.267 , pp. 17248-17256
    • Silva, M.M.1    Rogers, P.H.2    Arnone, A.3
  • 70
    • 0034687668 scopus 로고    scopus 로고
    • Interface sliding as illustrated by the multiple quaternary structures of liganded hemoglobin
    • Mueser T.C., Rogers P.H., and Arnone A. Interface sliding as illustrated by the multiple quaternary structures of liganded hemoglobin. Biochemistry 39 (2000) 15353-15364
    • (2000) Biochemistry , vol.39 , pp. 15353-15364
    • Mueser, T.C.1    Rogers, P.H.2    Arnone, A.3
  • 71
    • 20444417111 scopus 로고    scopus 로고
    • The enigma of the liganded hemoglobin end state: a novel quaternary structure of human carbonmonoxy hemoglobin
    • Safo M.K., and Abraham D.J. The enigma of the liganded hemoglobin end state: a novel quaternary structure of human carbonmonoxy hemoglobin. Biochemistry 44 (2005) 8347-8359
    • (2005) Biochemistry , vol.44 , pp. 8347-8359
    • Safo, M.K.1    Abraham, D.J.2
  • 72
    • 17644375152 scopus 로고    scopus 로고
    • Crystallographic evidence for a new ensemble of ligand-induced allosteric transitions in hemoglobin: the T-to-T-high quaternary transitions
    • Kavanaugh J.S., Rogers P.H., and Arnone A. Crystallographic evidence for a new ensemble of ligand-induced allosteric transitions in hemoglobin: the T-to-T-high quaternary transitions. Biochemistry 44 (2005) 6101-6121
    • (2005) Biochemistry , vol.44 , pp. 6101-6121
    • Kavanaugh, J.S.1    Rogers, P.H.2    Arnone, A.3
  • 73
    • 34548496030 scopus 로고    scopus 로고
    • Insights into the solution structure of human deoxyhemoglobin in the absence and presence of an allosteric effector
    • Sahu S.C., Simplaceanu V., Gong Q., Ho N.T., Tian F., Prestegard J.H., and Ho C. Insights into the solution structure of human deoxyhemoglobin in the absence and presence of an allosteric effector. Biochemistry 46 (2007) 9973-9980
    • (2007) Biochemistry , vol.46 , pp. 9973-9980
    • Sahu, S.C.1    Simplaceanu, V.2    Gong, Q.3    Ho, N.T.4    Tian, F.5    Prestegard, J.H.6    Ho, C.7
  • 74
    • 33645978391 scopus 로고    scopus 로고
    • Quaternary structure of carbonmonoxyhemoglobins in solution: structural changes induced by the allosteric effector inositol hexaphosphate
    • Gong Q.G., Simplaceanu V., Lukin J.A., Giovannelli J.L., Ho N.T., and Ho C. Quaternary structure of carbonmonoxyhemoglobins in solution: structural changes induced by the allosteric effector inositol hexaphosphate. Biochemistry 45 (2006) 5140-5148
    • (2006) Biochemistry , vol.45 , pp. 5140-5148
    • Gong, Q.G.1    Simplaceanu, V.2    Lukin, J.A.3    Giovannelli, J.L.4    Ho, N.T.5    Ho, C.6
  • 75
    • 21244479077 scopus 로고    scopus 로고
    • Liganded hemoglobin structural perturbations by the allosteric effector L35
    • Chen Q., Lalezari I., Nagel R.L., and H.R.E. Liganded hemoglobin structural perturbations by the allosteric effector L35. Biophys. J. 88 (2005) 2057-2067
    • (2005) Biophys. J. , vol.88 , pp. 2057-2067
    • Chen, Q.1    Lalezari, I.2    Nagel, R.L.3
  • 76
    • 0035831056 scopus 로고    scopus 로고
    • Direct observation of two distinct affinity conformations in the T state human deoxyhemoglobin
    • Shibayama N., and Saigo S. Direct observation of two distinct affinity conformations in the T state human deoxyhemoglobin. FEBS Lett. 429 (2001) 50-53
    • (2001) FEBS Lett. , vol.429 , pp. 50-53
    • Shibayama, N.1    Saigo, S.2
  • 77
    • 0018098692 scopus 로고
    • An estimation of the first binding constant of O2 to human hemoglobin A
    • Poyart C.F., Bursaux E., and Bohn B. An estimation of the first binding constant of O2 to human hemoglobin A. Eur. J. Biochem. 87 (1978) 75-83
    • (1978) Eur. J. Biochem. , vol.87 , pp. 75-83
    • Poyart, C.F.1    Bursaux, E.2    Bohn, B.3
  • 78
    • 0018162699 scopus 로고
    • Nanosecond transient Raman spectra of photolysed carboxyhaemoglobin
    • Lyons K.B., Friedman J.M., and Fleury P.A. Nanosecond transient Raman spectra of photolysed carboxyhaemoglobin. Nature 275 (1978) 565-566
    • (1978) Nature , vol.275 , pp. 565-566
    • Lyons, K.B.1    Friedman, J.M.2    Fleury, P.A.3
  • 79
    • 0001700167 scopus 로고
    • Nanosecond absorption spectroscopy of hemoglobin: elementary processes in kinetic cooperativity
    • Hofrichter J., Sommer J.H., Henry E.R., and Eaton W.A. Nanosecond absorption spectroscopy of hemoglobin: elementary processes in kinetic cooperativity. Proc. Natl. Acad. Sci. U. S. A. 80 (1983) 2235-2239
    • (1983) Proc. Natl. Acad. Sci. U. S. A. , vol.80 , pp. 2235-2239
    • Hofrichter, J.1    Sommer, J.H.2    Henry, E.R.3    Eaton, W.A.4
  • 80
    • 0030907624 scopus 로고    scopus 로고
    • Can a two-state MWC allosteric model explain hemoglobin kinetics?
    • Henry E.R., Jones C.M., Hofrichter J., and Eaton W.A. Can a two-state MWC allosteric model explain hemoglobin kinetics?. Biochemistry 36 (1997) 6511-6528
    • (1997) Biochemistry , vol.36 , pp. 6511-6528
    • Henry, E.R.1    Jones, C.M.2    Hofrichter, J.3    Eaton, W.A.4
  • 81
    • 0015945113 scopus 로고
    • A general approach to co-operativity and its application to the oxygen equilibrium of hemoglobin and its effectors
    • Herzfeld J., and Stanley H.E. A general approach to co-operativity and its application to the oxygen equilibrium of hemoglobin and its effectors. J. Mol. Biol. 82 (1974) 231-265
    • (1974) J. Mol. Biol. , vol.82 , pp. 231-265
    • Herzfeld, J.1    Stanley, H.E.2
  • 83
    • 0033585545 scopus 로고    scopus 로고
    • Kinetics of the allosteric transition in hemoglobin within silicate sol-gels
    • Shibayama N., and Saigo S. Kinetics of the allosteric transition in hemoglobin within silicate sol-gels. J. Am. Chem. Soc. 121 (1999) 444-445
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 444-445
    • Shibayama, N.1    Saigo, S.2
  • 84
    • 0032605985 scopus 로고    scopus 로고
    • Temperature dependent quaternary state relaxation in sol-gel encapsulated hemoglobin
    • Das T.K., Khan I., Rousseau D.L., and Friedman J.M. Temperature dependent quaternary state relaxation in sol-gel encapsulated hemoglobin. Biospectroscopy 5 (1999) S64-S70
    • (1999) Biospectroscopy , vol.5
    • Das, T.K.1    Khan, I.2    Rousseau, D.L.3    Friedman, J.M.4
  • 85
    • 0032746488 scopus 로고    scopus 로고
    • UV resonance Raman spectra of ligand binding intermediates of sol-gel encapsulated hemoglobin
    • Juszczak L.J., and Friedman J.M. UV resonance Raman spectra of ligand binding intermediates of sol-gel encapsulated hemoglobin. J. Biol. Chem. 274 (1999) 30357-30360
    • (1999) J. Biol. Chem. , vol.274 , pp. 30357-30360
    • Juszczak, L.J.1    Friedman, J.M.2
  • 87
    • 35348847304 scopus 로고    scopus 로고
    • Quaternary relaxations in sol-gel encapsulated hemoglobin studied via NIR and UV spectroscopy
    • Schiro G., and Cupane A. Quaternary relaxations in sol-gel encapsulated hemoglobin studied via NIR and UV spectroscopy. Biochemistry 46 (2007) 11568-11576
    • (2007) Biochemistry , vol.46 , pp. 11568-11576
    • Schiro, G.1    Cupane, A.2
  • 88
    • 0022531124 scopus 로고
    • A cooperative model for ligand binding to biological macromolecules as applied to oxygen carriers
    • Brunori M., Coletta M., and Di Cera E. A cooperative model for ligand binding to biological macromolecules as applied to oxygen carriers. Biophys. Chem. 23 (1986) 215-222
    • (1986) Biophys. Chem. , vol.23 , pp. 215-222
    • Brunori, M.1    Coletta, M.2    Di Cera, E.3
  • 89
    • 0022800418 scopus 로고
    • Cooperative free energies for nested allosteric models as applied to human hemoglobin
    • Gill S.J., Robert C.H., Coletta M., Di Cera E., and Brunori M. Cooperative free energies for nested allosteric models as applied to human hemoglobin. Biophys. J. 50 (1986) 747-752
    • (1986) Biophys. J. , vol.50 , pp. 747-752
    • Gill, S.J.1    Robert, C.H.2    Coletta, M.3    Di Cera, E.4    Brunori, M.5
  • 90
    • 0015506515 scopus 로고
    • A mathematical model for structure-function relations in hemoglobin
    • Szabo A., and Karplus M. A mathematical model for structure-function relations in hemoglobin. J. Mol. Biol. 72 (1972) 163-197
    • (1972) J. Mol. Biol. , vol.72 , pp. 163-197
    • Szabo, A.1    Karplus, M.2
  • 91
    • 0014958182 scopus 로고
    • Stereochemistry of cooperative effects in haemoglobin
    • Perutz M.F. Stereochemistry of cooperative effects in haemoglobin. Nature 228 (1970) 726-739
    • (1970) Nature , vol.228 , pp. 726-739
    • Perutz, M.F.1
  • 92
    • 0023850148 scopus 로고
    • Analysis of proton release in oxygen binding by hemoglobin: implications for the cooperative mechanism
    • Lee A.W., Karplus M., Poyart C., and Bursaux E. Analysis of proton release in oxygen binding by hemoglobin: implications for the cooperative mechanism. Biochemistry 27 (1988) 1285-1301
    • (1988) Biochemistry , vol.27 , pp. 1285-1301
    • Lee, A.W.1    Karplus, M.2    Poyart, C.3    Bursaux, E.4
  • 93
    • 0021818674 scopus 로고
    • Structure, dynamics, and reactivity in hemoglobin
    • Friedman J.M. Structure, dynamics, and reactivity in hemoglobin. Science 228 (1985) 1273-1280
    • (1985) Science , vol.228 , pp. 1273-1280
    • Friedman, J.M.1
  • 94
    • 0022363398 scopus 로고
    • Localized control of ligand binding in hemoglobin: effect of tertiary structure on picosecond geminate recombination
    • Friedman J.M., Scott T.W., Fisanick G.J., Simon S.R., Findsen E.W., Ondrias M.R., and Macdonald V.W. Localized control of ligand binding in hemoglobin: effect of tertiary structure on picosecond geminate recombination. Science 229 (1985) 187-190
    • (1985) Science , vol.229 , pp. 187-190
    • Friedman, J.M.1    Scott, T.W.2    Fisanick, G.J.3    Simon, S.R.4    Findsen, E.W.5    Ondrias, M.R.6    Macdonald, V.W.7
  • 95
    • 0022412308 scopus 로고
    • Picosecond time-resolved resonance Raman studies of hemoglobin: implications for reactivity
    • Findsen E.W., Friedman J.M., Ondrias M.R., and Simon S.R. Picosecond time-resolved resonance Raman studies of hemoglobin: implications for reactivity. Science 229 (1985) 661-665
    • (1985) Science , vol.229 , pp. 661-665
    • Findsen, E.W.1    Friedman, J.M.2    Ondrias, M.R.3    Simon, S.R.4
  • 96
    • 0021486088 scopus 로고
    • Tertiary-structure relaxation in hemoglobin: a transient Raman study
    • Scott T.W., and Friedman J.M. Tertiary-structure relaxation in hemoglobin: a transient Raman study. J. Am. Chem. Soc. 106 (1984) 5677-5687
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 5677-5687
    • Scott, T.W.1    Friedman, J.M.2
  • 97
    • 0032584325 scopus 로고    scopus 로고
    • A possible allosteric communication pathway identified through a resonance Raman study of four beta37 mutants of human hemoglobin A
    • Peterson E.S., and Friedman J.M. A possible allosteric communication pathway identified through a resonance Raman study of four beta37 mutants of human hemoglobin A. Biochemistry 37 (1998) 4346-4357
    • (1998) Biochemistry , vol.37 , pp. 4346-4357
    • Peterson, E.S.1    Friedman, J.M.2
  • 98
    • 7244239027 scopus 로고    scopus 로고
    • Spectroscopic and functional characterization of T state hemoglobin conformations encapsulated in silica gels
    • Samuni U., Dantsker D., Juszczak L.J., Bettati S., Ronda L., Mozzarelli A., and Friedman J.M. Spectroscopic and functional characterization of T state hemoglobin conformations encapsulated in silica gels. Biochemistry 43 (2004) 13674-13682
    • (2004) Biochemistry , vol.43 , pp. 13674-13682
    • Samuni, U.1    Dantsker, D.2    Juszczak, L.J.3    Bettati, S.4    Ronda, L.5    Mozzarelli, A.6    Friedman, J.M.7
  • 99
    • 33644680949 scopus 로고    scopus 로고
    • Modulation of reactivity and conformation within the T-quaternary state of human hemoglobin: the combined use of mutagenesis and sol-gel encapsulation
    • Samuni U., Roche C.J., Dantsker D., Juszczak L.J., and Friedman J.M. Modulation of reactivity and conformation within the T-quaternary state of human hemoglobin: the combined use of mutagenesis and sol-gel encapsulation. Biochemistry 45 (2006) 2820-2835
    • (2006) Biochemistry , vol.45 , pp. 2820-2835
    • Samuni, U.1    Roche, C.J.2    Dantsker, D.3    Juszczak, L.J.4    Friedman, J.M.5
  • 101
    • 35548949877 scopus 로고    scopus 로고
    • Conformational dependence of hemoglobin reactivity under high viscosity conditions: the role of solvent slaved dynamics
    • Samuni U., Roche C.J., Dantsker D., and Friedman J.M. Conformational dependence of hemoglobin reactivity under high viscosity conditions: the role of solvent slaved dynamics. J. Am. Chem. Soc. 129 (2007) 12756-12764
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 12756-12764
    • Samuni, U.1    Roche, C.J.2    Dantsker, D.3    Friedman, J.M.4
  • 102
    • 1342328188 scopus 로고    scopus 로고
    • The biochemistry of nitric oxide, nitrite, and hemoglobin: role in blood flow regulation
    • Gladwin M.T., Crawford J.H., and Patel R.P. The biochemistry of nitric oxide, nitrite, and hemoglobin: role in blood flow regulation. Free Radic. Biol. Med. 36 (2004) 707-717
    • (2004) Free Radic. Biol. Med. , vol.36 , pp. 707-717
    • Gladwin, M.T.1    Crawford, J.H.2    Patel, R.P.3
  • 103
    • 0019726454 scopus 로고
    • Oxidation of nitrogen oxides by bound dioxygen in hemoproteins
    • Doyle M.P., and Hoekstra J.W. Oxidation of nitrogen oxides by bound dioxygen in hemoproteins. J. Inorg. Biochem. 14 (1981) 351-358
    • (1981) J. Inorg. Biochem. , vol.14 , pp. 351-358
    • Doyle, M.P.1    Hoekstra, J.W.2
  • 105
    • 0032951905 scopus 로고    scopus 로고
    • Nitric oxide and iron proteins
    • Cooper C.E. Nitric oxide and iron proteins. Biochim. Biophys. Acta 1411 (1999) 290-309
    • (1999) Biochim. Biophys. Acta , vol.1411 , pp. 290-309
    • Cooper, C.E.1
  • 106
    • 0018742687 scopus 로고
    • The rate of oxygen uptake by human red blood cells
    • Coin J.T., and Olson J.S. The rate of oxygen uptake by human red blood cells. J. Biol. Chem. 254 (1979) 1178-1190
    • (1979) J. Biol. Chem. , vol.254 , pp. 1178-1190
    • Coin, J.T.1    Olson, J.S.2
  • 108
    • 0032538124 scopus 로고    scopus 로고
    • Diffusion of nitric oxide and scavenging by blood in the vasculature
    • Butler A.R., Megson I.L., and Wright P.G. Diffusion of nitric oxide and scavenging by blood in the vasculature. Biochim. Biophys. Acta 1425 (1998) 168-176
    • (1998) Biochim. Biophys. Acta , vol.1425 , pp. 168-176
    • Butler, A.R.1    Megson, I.L.2    Wright, P.G.3
  • 109
    • 33750814148 scopus 로고    scopus 로고
    • Effective diffusion distance of nitric oxide in the microcirculation
    • Vaughn M.W., Kuo L., and Liao J.C. Effective diffusion distance of nitric oxide in the microcirculation. Am. J. Physiol. 274 (1998) H1705-H1714
    • (1998) Am. J. Physiol. , vol.274
    • Vaughn, M.W.1    Kuo, L.2    Liao, J.C.3
  • 111
    • 0034723187 scopus 로고    scopus 로고
    • Erythrocytes possess an intrinsic barrier to nitric oxide consumption
    • Vaughn M.W., Huang K.T., Kuo L., and Liao J.C. Erythrocytes possess an intrinsic barrier to nitric oxide consumption. J. Biol. Chem. 275 (2000) 2342-2348
    • (2000) J. Biol. Chem. , vol.275 , pp. 2342-2348
    • Vaughn, M.W.1    Huang, K.T.2    Kuo, L.3    Liao, J.C.4
  • 114
    • 0038578668 scopus 로고    scopus 로고
    • Nitric oxides reactions with hemoglobin: a view through the SNO-storm
    • Gladwin M.T., Lancaster J.R., Freeman B.A., and Schechter A.N. Nitric oxides reactions with hemoglobin: a view through the SNO-storm. Nature Med. 9 (2003) 496-500
    • (2003) Nature Med. , vol.9 , pp. 496-500
    • Gladwin, M.T.1    Lancaster, J.R.2    Freeman, B.A.3    Schechter, A.N.4
  • 115
    • 0032495529 scopus 로고    scopus 로고
    • Reactions between nitric oxide and haemoglobin under physiological conditions
    • Gow A.J., and Stamler J.S. Reactions between nitric oxide and haemoglobin under physiological conditions. Nature 391 (1998) 169-173
    • (1998) Nature , vol.391 , pp. 169-173
    • Gow, A.J.1    Stamler, J.S.2
  • 116
    • 0029875840 scopus 로고    scopus 로고
    • S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control
    • Jia L., Bonaventura C., Bonaventura J., and Stamler J.S. S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control. Nature 380 (1996) 221-226
    • (1996) Nature , vol.380 , pp. 221-226
    • Jia, L.1    Bonaventura, C.2    Bonaventura, J.3    Stamler, J.S.4
  • 117
    • 0035252076 scopus 로고    scopus 로고
    • Export by red blood cells of nitric oxide bioactivity
    • Pawloski J.R., Hess D.T., and Stamler J.S. Export by red blood cells of nitric oxide bioactivity. Nature 409 (2001) 622-626
    • (2001) Nature , vol.409 , pp. 622-626
    • Pawloski, J.R.1    Hess, D.T.2    Stamler, J.S.3
  • 120
    • 0032493731 scopus 로고    scopus 로고
    • Electron paramagnetic resonance and oxygen binding studies of S-nitrosyl hemoglobin. A novel oxygen carrier having NO-assisted allosteric functions
    • Yonetani T., Tsuneshige A., Zhou Y., and Chen X. Electron paramagnetic resonance and oxygen binding studies of S-nitrosyl hemoglobin. A novel oxygen carrier having NO-assisted allosteric functions. J. Biol. Chem. 273 (1998) 20323-20333
    • (1998) J. Biol. Chem. , vol.273 , pp. 20323-20333
    • Yonetani, T.1    Tsuneshige, A.2    Zhou, Y.3    Chen, X.4
  • 121
    • 0141494483 scopus 로고    scopus 로고
    • Interaction of nitrogen monoxide with hemoglobin and the artefactual production of S-nitroso-hemoglobin
    • Herold S. Interaction of nitrogen monoxide with hemoglobin and the artefactual production of S-nitroso-hemoglobin. C. R. Biol. 326 (2003) 533-541
    • (2003) C. R. Biol. , vol.326 , pp. 533-541
    • Herold, S.1
  • 122
    • 0345306150 scopus 로고    scopus 로고
    • Oxidation and nitrosylation of oxyhemoglobin by S-nitrosoglutathione via nitroxyl anion
    • Spencer N.Y., Patel N.K., Keszler A., and Hogg N. Oxidation and nitrosylation of oxyhemoglobin by S-nitrosoglutathione via nitroxyl anion. Free. Radic. Biol. Med. 35 (2003) 1515-1526
    • (2003) Free. Radic. Biol. Med. , vol.35 , pp. 1515-1526
    • Spencer, N.Y.1    Patel, N.K.2    Keszler, A.3    Hogg, N.4
  • 123
    • 1642588213 scopus 로고    scopus 로고
    • S-nitrosohemoglobin: a biochemical perspective
    • Zhang Y., and Hogg N. S-nitrosohemoglobin: a biochemical perspective. Free Radic. Biol. Med. 36 (2004) 947-958
    • (2004) Free Radic. Biol. Med. , vol.36 , pp. 947-958
    • Zhang, Y.1    Hogg, N.2
  • 124
    • 0000192486 scopus 로고
    • Sickle cell anemia a molecular disease
    • Pauling L., Itano H.A., et al. Sickle cell anemia a molecular disease. Science 110 (1949) 543-548
    • (1949) Science , vol.110 , pp. 543-548
    • Pauling, L.1    Itano, H.A.2
  • 127
    • 2442687968 scopus 로고    scopus 로고
    • Recording human globin gene variation
    • Patrinos G.P., and Wajcman H. Recording human globin gene variation. Hemoglobin 28 (2004) v-vii
    • (2004) Hemoglobin , vol.28
    • Patrinos, G.P.1    Wajcman, H.2
  • 128
    • 33645127489 scopus 로고    scopus 로고
    • The allosteric properties of hemoglobin: insights from natural and site directed mutants
    • Bellelli A., Brunori M., Miele A.E., Panetta G., and Vallone B. The allosteric properties of hemoglobin: insights from natural and site directed mutants. Curr. Protein Pept. Sci. 7 (2006) 17-45
    • (2006) Curr. Protein Pept. Sci. , vol.7 , pp. 17-45
    • Bellelli, A.1    Brunori, M.2    Miele, A.E.3    Panetta, G.4    Vallone, B.5
  • 129
    • 0021051045 scopus 로고
    • Hemoglobin tertiary structural change on ligand binding. Its role in the co-operative mechanism
    • Gelin B.R., Lee A.W., and Karplus M. Hemoglobin tertiary structural change on ligand binding. Its role in the co-operative mechanism. J. Mol. Bio.l 171 (1983) 489-559
    • (1983) J. Mol. Bio.l , vol.171 , pp. 489-559
    • Gelin, B.R.1    Lee, A.W.2    Karplus, M.3
  • 130
    • 0018642588 scopus 로고
    • The linkage between oxygenation and subunit association in human hemoglobin Kansas. Concentration dependence of the oxygen binding equilibria
    • Atha D.H., Johnson M.L., and Riggs A.F. The linkage between oxygenation and subunit association in human hemoglobin Kansas. Concentration dependence of the oxygen binding equilibria. J. Biol. Chem. 254 (1979) 12390-12398
    • (1979) J. Biol. Chem. , vol.254 , pp. 12390-12398
    • Atha, D.H.1    Johnson, M.L.2    Riggs, A.F.3
  • 131
    • 0018198707 scopus 로고
    • Hemoglobin Presbyterian: beta108 (G10) asparagine leads to lysine, a hemoglobin variant with low oxygen affinity
    • Moo-Penn W.F., Wolff J.A., Simon G., Vacek M., Jue D.L., and Johnson M.H. Hemoglobin Presbyterian: beta108 (G10) asparagine leads to lysine, a hemoglobin variant with low oxygen affinity. FEBS Lett. 92 (1978) 53-56
    • (1978) FEBS Lett. , vol.92 , pp. 53-56
    • Moo-Penn, W.F.1    Wolff, J.A.2    Simon, G.3    Vacek, M.4    Jue, D.L.5    Johnson, M.H.6
  • 132
    • 33847048655 scopus 로고    scopus 로고
    • Mutations of the betaN102 residue of HbA not only inhibit the ligand-linked T to Re state transition, but also profoundly affect the properties of the T state itself
    • Kwiatkowski L.D., Hui H.L., Karasik E., Colby J.E., and Noble R.W. Mutations of the betaN102 residue of HbA not only inhibit the ligand-linked T to Re state transition, but also profoundly affect the properties of the T state itself. Biochemistry 46 (2007) 2037-2049
    • (2007) Biochemistry , vol.46 , pp. 2037-2049
    • Kwiatkowski, L.D.1    Hui, H.L.2    Karasik, E.3    Colby, J.E.4    Noble, R.W.5
  • 136
    • 0015924336 scopus 로고
    • Ligand binding kinetics of des arginine haemoglobin
    • Hewitt J.A., and Gibson Q.H. Ligand binding kinetics of des arginine haemoglobin. J. Mol. Biol. 74 (1973) 489-498
    • (1973) J. Mol. Biol. , vol.74 , pp. 489-498
    • Hewitt, J.A.1    Gibson, Q.H.2
  • 137
    • 0016665257 scopus 로고
    • Alteration of functional properties associated with the change in quaternary structure in unliganded haemoglobin
    • Kilmartin J.V., Hewitt J.A., and Wootton J.F. 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
  • 138
    • 0015901066 scopus 로고
    • The ligand-binding properties of desHis (146beta) hemoglobin
    • Moffat K., Olson J.S., Gibson Q.H., and Kilmartin J.V. The ligand-binding properties of desHis (146beta) hemoglobin. J. Biol. Chem. 48 (1973) 6387-6393
    • (1973) J. Biol. Chem. , vol.48 , pp. 6387-6393
    • Moffat, K.1    Olson, J.S.2    Gibson, Q.H.3    Kilmartin, J.V.4
  • 139
    • 0036786309 scopus 로고    scopus 로고
    • Ligand binding properties and structural studies of recombinant and chemically modified hemoglobins altered at beta 93 cysteine
    • Cheng Y., Shen T.J., Simplaceanu V., and Ho C. Ligand binding properties and structural studies of recombinant and chemically modified hemoglobins altered at beta 93 cysteine. Biochemistry 41 (2002) 11901-11913
    • (2002) Biochemistry , vol.41 , pp. 11901-11913
    • Cheng, Y.1    Shen, T.J.2    Simplaceanu, V.3    Ho, C.4
  • 140
    • 0032607505 scopus 로고    scopus 로고
    • Cysteines beta93 and beta112 as probes of conformational and functional events at the human hemoglobin subunit interfaces
    • Vasquez G.B., Karavitis M., Ji X., Pechik I., Brinigar W.S., Gilliland G.L., and Fronticelli C. Cysteines beta93 and beta112 as probes of conformational and functional events at the human hemoglobin subunit interfaces. Biophys. J. 76 (1999) 88-97
    • (1999) Biophys. J. , vol.76 , pp. 88-97
    • Vasquez, G.B.1    Karavitis, M.2    Ji, X.3    Pechik, I.4    Brinigar, W.S.5    Gilliland, G.L.6    Fronticelli, C.7
  • 143
    • 0016340828 scopus 로고
    • Hemoglobin Chesapeake (92 alpha, arginine-leucine). Precise measurements and analyses of oxygen equilibrium
    • Imai K. Hemoglobin Chesapeake (92 alpha, arginine-leucine). Precise measurements and analyses of oxygen equilibrium. J. Biol. Chem. 249 (1974) 7607-7612
    • (1974) J. Biol. Chem. , vol.249 , pp. 7607-7612
    • Imai, K.1
  • 144
    • 0014030460 scopus 로고
    • Haemoglobin Koln (beta-98 valine-methionine): an unstable protein causing inclusion-body anaemia
    • Carrell R.W., Lehmann H., and Hutchison H.E. Haemoglobin Koln (beta-98 valine-methionine): an unstable protein causing inclusion-body anaemia. Nature 210 (1966) 915-916
    • (1966) Nature , vol.210 , pp. 915-916
    • Carrell, R.W.1    Lehmann, H.2    Hutchison, H.E.3
  • 145
    • 0013809189 scopus 로고
    • Hemoglobin Koln disease: familial hypochromic hemolytic anemia with hemoglobin anomaly
    • Pribilla W., Klesse P., Betke K., Lehmann H., and Beale D. Hemoglobin Koln disease: familial hypochromic hemolytic anemia with hemoglobin anomaly. Klin. Wochenschr. 43 (1965) 1049-1053
    • (1965) Klin. Wochenschr. , vol.43 , pp. 1049-1053
    • Pribilla, W.1    Klesse, P.2    Betke, K.3    Lehmann, H.4    Beale, D.5
  • 146
    • 0025037279 scopus 로고
    • Unstable hemoglobins
    • Ohba Y. Unstable hemoglobins. Hemoglobin 14 (1990) 353-388
    • (1990) Hemoglobin , vol.14 , pp. 353-388
    • Ohba, Y.1
  • 149
    • 0033939355 scopus 로고    scopus 로고
    • Genetically crosslinked hemoglobin: a structural study
    • Brucker E.A. Genetically crosslinked hemoglobin: a structural study. Acta Crystallogr. D Biol. Crystallogr. 56 (2000) 812-816
    • (2000) Acta Crystallogr. D Biol. Crystallogr. , vol.56 , pp. 812-816
    • Brucker, E.A.1
  • 150
    • 0031568811 scopus 로고    scopus 로고
    • Structures of a hemoglobin-based blood substitute: insights into the function of allosteric proteins
    • Kroeger K.S., and Kundrot C.E. Structures of a hemoglobin-based blood substitute: insights into the function of allosteric proteins. Structure 5 (1997) 227-237
    • (1997) Structure , vol.5 , pp. 227-237
    • Kroeger, K.S.1    Kundrot, C.E.2
  • 152
    • 0036087535 scopus 로고    scopus 로고
    • Correlation of protein functional properties in the crystal and in solution: the case study of T-state hemoglobin
    • Noble R.W., Kwiatkowski L.D., Hui H.L., Bruno S., Bettati S., and Mozzarelli A. Correlation of protein functional properties in the crystal and in solution: the case study of T-state hemoglobin. Protein Sci. 11 (2002) 1845-1849
    • (2002) Protein Sci. , vol.11 , pp. 1845-1849
    • Noble, R.W.1    Kwiatkowski, L.D.2    Hui, H.L.3    Bruno, S.4    Bettati, S.5    Mozzarelli, A.6
  • 153
    • 0032834006 scopus 로고    scopus 로고
    • Recombinant hemoglobin(alpha 29leucine → phenylalanine, alpha 96valine → tryptophan, beta 108asparagine → lysine) exhibits low oxygen affinity and high cooperativity combined with resistance to autoxidation
    • Jeong S.T., Ho N.T., Hendrich M.P., and Ho C. Recombinant hemoglobin(alpha 29leucine → phenylalanine, alpha 96valine → tryptophan, beta 108asparagine → lysine) exhibits low oxygen affinity and high cooperativity combined with resistance to autoxidation. Biochemistry 38 (1999) 13433-13442
    • (1999) Biochemistry , vol.38 , pp. 13433-13442
    • Jeong, S.T.1    Ho, N.T.2    Hendrich, M.P.3    Ho, C.4
  • 154
    • 0029024086 scopus 로고
    • A novel low oxygen affinity recombinant hemoglobin (alpha96Val → Trp): switching quaternary structure without changing the ligation state
    • Kim H.W., Shen T.J., Sun D.P., Ho N.T., Madrid M., and Ho C. A novel low oxygen affinity recombinant hemoglobin (alpha96Val → Trp): switching quaternary structure without changing the ligation state. J. Mol. Biol. 248 (1995) 867-882
    • (1995) J. Mol. Biol. , vol.248 , pp. 867-882
    • Kim, H.W.1    Shen, T.J.2    Sun, D.P.3    Ho, N.T.4    Madrid, M.5    Ho, C.6
  • 156
    • 0037378305 scopus 로고    scopus 로고
    • Stable octameric structure of recombinant hemoglobin alpha(2)beta(2)83 Gly → Cys
    • Fablet C., Marden M.C., Green B.N., Ho C., Pagnier J., and Baudin-Creuza V. Stable octameric structure of recombinant hemoglobin alpha(2)beta(2)83 Gly → Cys. Protein Sci. 12 (2003) 690-695
    • (2003) Protein Sci. , vol.12 , pp. 690-695
    • Fablet, C.1    Marden, M.C.2    Green, B.N.3    Ho, C.4    Pagnier, J.5    Baudin-Creuza, V.6
  • 159
    • 0035882543 scopus 로고    scopus 로고
    • Molecular engineering of a polymer of tetrameric hemoglobins
    • Fronticelli C., Arosio D., Bobofchak K.M., and Vasquez G.B. Molecular engineering of a polymer of tetrameric hemoglobins. Proteins 44 (2001) 212-222
    • (2001) Proteins , vol.44 , pp. 212-222
    • Fronticelli, C.1    Arosio, D.2    Bobofchak, K.M.3    Vasquez, G.B.4
  • 161
    • 0032545463 scopus 로고    scopus 로고
    • Reduced nitric oxide reactivity of a new recombinant human hemoglobin attenuates gastric dysmotility
    • Hartman J.C., Argoudelis G., Doherty D., Lemon D., and Gorczynski R. Reduced nitric oxide reactivity of a new recombinant human hemoglobin attenuates gastric dysmotility. Eur. J. Pharmacol. 363 (1998) 175-178
    • (1998) Eur. J. Pharmacol. , vol.363 , pp. 175-178
    • Hartman, J.C.1    Argoudelis, G.2    Doherty, D.3    Lemon, D.4    Gorczynski, R.5
  • 163
    • 0014414239 scopus 로고
    • Glutaraldehyde as a protein cross-linkage reagent
    • Richards F.M., and Knowles J.R. Glutaraldehyde as a protein cross-linkage reagent. J. Mol. Biol. 37 (1968) 231-233
    • (1968) J. Mol. Biol. , vol.37 , pp. 231-233
    • Richards, F.M.1    Knowles, J.R.2
  • 164
    • 0018714227 scopus 로고
    • Diaspirins that cross-link beta chains of hemoglobin: bis(3,5-dibromosalicyl) succinate and bis(3,5-dibromosalicyl) fumarate
    • Walder J.A., Zaugg R.H., Walder R.Y., Steele J.M., and Klotz I.M. Diaspirins that cross-link beta chains of hemoglobin: bis(3,5-dibromosalicyl) succinate and bis(3,5-dibromosalicyl) fumarate. Biochemistry 18 (1979) 4265-4270
    • (1979) Biochemistry , vol.18 , pp. 4265-4270
    • Walder, J.A.1    Zaugg, R.H.2    Walder, R.Y.3    Steele, J.M.4    Klotz, I.M.5
  • 165
    • 0023024415 scopus 로고
    • Isolation and characterization of a new hemoglobin derivative cross-linked between the alpha chains (lysine 99 alpha 1-lysine 99 alpha 2)
    • Chatterjee R., Welty E.V., Walder R.Y., Pruitt S.L., Rogers P.H., Arnone A., and Walder J.A. Isolation and characterization of a new hemoglobin derivative cross-linked between the alpha chains (lysine 99 alpha 1-lysine 99 alpha 2). J. Biol. Chem. 261 (1986) 9929-9937
    • (1986) J. Biol. Chem. , vol.261 , pp. 9929-9937
    • Chatterjee, R.1    Welty, E.V.2    Walder, R.Y.3    Pruitt, S.L.4    Rogers, P.H.5    Arnone, A.6    Walder, J.A.7
  • 166
    • 34247251297 scopus 로고    scopus 로고
    • Combining the influence of two low O2 affinity-inducing chemical modifications of the central cavity of hemoglobin
    • Nacharaju P., Friedman J.M., Prabhakaran M., Acharya S.A., and Manjula B.N. Combining the influence of two low O2 affinity-inducing chemical modifications of the central cavity of hemoglobin. Biochemistry 46 (2007) 4554-4564
    • (2007) Biochemistry , vol.46 , pp. 4554-4564
    • Nacharaju, P.1    Friedman, J.M.2    Prabhakaran, M.3    Acharya, S.A.4    Manjula, B.N.5
  • 168
    • 0030047619 scopus 로고    scopus 로고
    • Stabilization of the tetrameric structure of human and bovine hemoglobins by pseudocrosslinking with muconic acid
    • Razynska A., Matheson-Urbaitis B., Fronticelli C., Collins J.H., and Bucci E. Stabilization of the tetrameric structure of human and bovine hemoglobins by pseudocrosslinking with muconic acid. Arch. Biochem. Biophys. 326 (1996) 119-125
    • (1996) Arch. Biochem. Biophys. , vol.326 , pp. 119-125
    • Razynska, A.1    Matheson-Urbaitis, B.2    Fronticelli, C.3    Collins, J.H.4    Bucci, E.5
  • 169
    • 0034192555 scopus 로고    scopus 로고
    • Adipyl crosslinked bovine hemoglobins as new models of allosteric systems
    • Kwansa H.E., Young A.D., Arosio D., Razynska A., and Bucci E. Adipyl crosslinked bovine hemoglobins as new models of allosteric systems. Proteins 39 (2000) 166-169
    • (2000) Proteins , vol.39 , pp. 166-169
    • Kwansa, H.E.1    Young, A.D.2    Arosio, D.3    Razynska, A.4    Bucci, E.5
  • 171
    • 0032519439 scopus 로고    scopus 로고
    • Conformation of the sebacyl beta1Lys82-beta2Lys82 crosslink in T-state human hemoglobin
    • Ji X., Braxenthaler M., Moult J., Fronticelli C., Bucci E., and Gilliland G.L. Conformation of the sebacyl beta1Lys82-beta2Lys82 crosslink in T-state human hemoglobin. Proteins 30 (1998) 309-320
    • (1998) Proteins , vol.30 , pp. 309-320
    • Ji, X.1    Braxenthaler, M.2    Moult, J.3    Fronticelli, C.4    Bucci, E.5    Gilliland, G.L.6
  • 172
    • 0034628672 scopus 로고    scopus 로고
    • Crystal structure of Lysbeta(1)82-Lysbeta(2)82 crosslinked hemoglobin: a possible allosteric intermediate
    • Fernandez E.J., Abad-Zapatero C., and Olsen K.W. Crystal structure of Lysbeta(1)82-Lysbeta(2)82 crosslinked hemoglobin: a possible allosteric intermediate. J. Mol. Biol. 296 (2000) 1245-1256
    • (2000) J. Mol. Biol. , vol.296 , pp. 1245-1256
    • Fernandez, E.J.1    Abad-Zapatero, C.2    Olsen, K.W.3
  • 173
    • 0027429840 scopus 로고
    • Cross-linked hemoglobin-superoxide dismutase-catalase scavenges oxygen-derived free radicals and prevents methemoglobin formation and iron release
    • D'Agnillo F., and Chang T.M. Cross-linked hemoglobin-superoxide dismutase-catalase scavenges oxygen-derived free radicals and prevents methemoglobin formation and iron release. Biomater. Artif. Cell Immobil. Biotechnol. 21 (1993) 609-621
    • (1993) Biomater. Artif. Cell Immobil. Biotechnol. , vol.21 , pp. 609-621
    • D'Agnillo, F.1    Chang, T.M.2
  • 174
    • 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. Structural and functional characterization of glutaraldehyde-polymerized bovine hemoglobin and its isolated fractions. Anal. Chem. 77 (2005) 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
  • 175
    • 8544279614 scopus 로고    scopus 로고
    • Ethical considerations concerning South Africa's approval of a blood substitute
    • Schutte A.E. Ethical considerations concerning South Africa's approval of a blood substitute. Ethics Med. 18 (2002) 55-62
    • (2002) Ethics Med. , vol.18 , pp. 55-62
    • Schutte, A.E.1
  • 176
    • 4043084061 scopus 로고    scopus 로고
    • Effect of glutaraldehyde concentration on the physical properties of polymerized hemoglobin-based oxygen carriers
    • Eike J.H., and Palmer A.F. Effect of glutaraldehyde concentration on the physical properties of polymerized hemoglobin-based oxygen carriers. Biotechnol. Prog. 20 (2004) 1225-1232
    • (2004) Biotechnol. Prog. , vol.20 , pp. 1225-1232
    • Eike, J.H.1    Palmer, A.F.2
  • 177
    • 3142750045 scopus 로고    scopus 로고
    • PolyHeme. Northfield Laboratories
    • Jahr J.S., and Varma N. PolyHeme. Northfield Laboratories. IDrugs 7 (2004) 478-482
    • (2004) IDrugs , vol.7 , pp. 478-482
    • Jahr, J.S.1    Varma, N.2
  • 178
    • 0031858604 scopus 로고    scopus 로고
    • The first randomized trial of human polymerized hemoglobin as a blood substitute in acute trauma and emergent surgery
    • discussion 120-122
    • Gould S.A., Moore E.E., Hoyt D.B., Burch J.M., Haenel J.B., Garcia J., DeWoskin R., and Moss G.S. The first randomized trial of human polymerized hemoglobin as a blood substitute in acute trauma and emergent surgery. J. Am. Coll. Surgeons 187 (1998) 113-120 discussion 120-122
    • (1998) J. Am. Coll. Surgeons , vol.187 , pp. 113-120
    • Gould, S.A.1    Moore, E.E.2    Hoyt, D.B.3    Burch, J.M.4    Haenel, J.B.5    Garcia, J.6
  • 180
    • 0021257844 scopus 로고
    • Polymerized pyridoxylated hemoglobin: a red cell substitute with normal oxygen capacity
    • Sehgal L.R., Gould S.A., Rosen A.L., Sehgal H.L., and Moss G.S. Polymerized pyridoxylated hemoglobin: a red cell substitute with normal oxygen capacity. Surgery 95 (1984) 433-438
    • (1984) Surgery , vol.95 , pp. 433-438
    • Sehgal, L.R.1    Gould, S.A.2    Rosen, A.L.3    Sehgal, H.L.4    Moss, G.S.5
  • 181
    • 18844444557 scopus 로고    scopus 로고
    • O-raffinose crosslinked hemoglobin lacks site-specific chemistry in the central cavity: structural and functional consequences of beta93Cys modification
    • Boykins R.A., Buehler P.W., Jia Y., Venable R., and Alayash A.I. O-raffinose crosslinked hemoglobin lacks site-specific chemistry in the central cavity: structural and functional consequences of beta93Cys modification. Proteins 59 (2005) 840-855
    • (2005) Proteins , vol.59 , pp. 840-855
    • Boykins, R.A.1    Buehler, P.W.2    Jia, Y.3    Venable, R.4    Alayash, A.I.5
  • 182
    • 2942722660 scopus 로고    scopus 로고
    • Oxidized mono-, di-, tri-, and polysaccharides as potential hemoglobin cross-linking reagents for the synthesis of high oxygen affinity artificial blood substitutes
    • Eike J.H., and Palmer A.F. Oxidized mono-, di-, tri-, and polysaccharides as potential hemoglobin cross-linking reagents for the synthesis of high oxygen affinity artificial blood substitutes. Biotechnol. Prog. 20 (2004) 953-962
    • (2004) Biotechnol. Prog. , vol.20 , pp. 953-962
    • Eike, J.H.1    Palmer, A.F.2
  • 183
    • 25844443775 scopus 로고    scopus 로고
    • Synthesis and characterization of a novel DTPA polymerized hemoglobin based oxygen carrier
    • Haney C.R., Buehler P.W., and Gulati A. Synthesis and characterization of a novel DTPA polymerized hemoglobin based oxygen carrier. Biochim. Biophys. Acta 1725 (2005) 358-369
    • (2005) Biochim. Biophys. Acta , vol.1725 , pp. 358-369
    • Haney, C.R.1    Buehler, P.W.2    Gulati, A.3
  • 184
    • 37149039501 scopus 로고    scopus 로고
    • Efficient generation of dendritic arrays of cross-linked hemoglobin: symmetry and redundancy
    • Hu D., and Kluger R. Efficient generation of dendritic arrays of cross-linked hemoglobin: symmetry and redundancy. Org. Biomol. Chem. 6 (2008) 151-156
    • (2008) Org. Biomol. Chem. , vol.6 , pp. 151-156
    • Hu, D.1    Kluger, R.2
  • 187
    • 0031876095 scopus 로고    scopus 로고
    • Polyhemoglobin-superoxide dismutase-catalase as a blood substitute with antioxidant properties
    • D'Agnillo F., and Chang T.M. Polyhemoglobin-superoxide dismutase-catalase as a blood substitute with antioxidant properties. Nature Biotechnol. 16 (1998) 667-671
    • (1998) Nature Biotechnol. , vol.16 , pp. 667-671
    • D'Agnillo, F.1    Chang, T.M.2
  • 188
    • 33847308140 scopus 로고    scopus 로고
    • Synthesis of a hemoglobin polymer containing antioxidant enzymes using complementary chemistry of maleimides and sulfhydryls
    • Tarasov E., Blaszak M.M., LaMarre J.M., and Olsen K.W. Synthesis of a hemoglobin polymer containing antioxidant enzymes using complementary chemistry of maleimides and sulfhydryls. Artif. Cells Blood Substit. Immobil. Biotechnol. 35 (2007) 31-43
    • (2007) Artif. Cells Blood Substit. Immobil. Biotechnol. , vol.35 , pp. 31-43
    • Tarasov, E.1    Blaszak, M.M.2    LaMarre, J.M.3    Olsen, K.W.4
  • 189
    • 0000335121 scopus 로고
    • Soluble dextran-hemoglobin complex as a potential blood substitute
    • Tam S.C., Blumenstein J., and Wong J.T. Soluble dextran-hemoglobin complex as a potential blood substitute. Proc. Natl. Acad. Sci. U. S. A. 73 (1976) 2128-2131
    • (1976) Proc. Natl. Acad. Sci. U. S. A. , vol.73 , pp. 2128-2131
    • Tam, S.C.1    Blumenstein, J.2    Wong, J.T.3
  • 190
    • 0025241983 scopus 로고
    • Covalent fixation of hemoglobin to dextran phosphates decreases its oxygen affinity
    • Sacco D., Klett-Zygmunt D., Vigneron C., and Dellacherie E. Covalent fixation of hemoglobin to dextran phosphates decreases its oxygen affinity. Biochim. Biophys. Acta 1041 (1990) 279-284
    • (1990) Biochim. Biophys. Acta , vol.1041 , pp. 279-284
    • Sacco, D.1    Klett-Zygmunt, D.2    Vigneron, C.3    Dellacherie, E.4
  • 191
    • 0029738132 scopus 로고    scopus 로고
    • Hemoglobin-dialdehyde dextran conjugates: improvement of their oxygen-binding properties with anionic groups
    • Bonneaux F., Dellacherie E., Labrude P., and Vigneron C. Hemoglobin-dialdehyde dextran conjugates: improvement of their oxygen-binding properties with anionic groups. J. Protein Chem. 15 (1996) 461-465
    • (1996) J. Protein Chem. , vol.15 , pp. 461-465
    • Bonneaux, F.1    Dellacherie, E.2    Labrude, P.3    Vigneron, C.4
  • 192
    • 0027338983 scopus 로고
    • Low oxygen affinity derivatives of human hemoglobin by fixation of polycarboxylic dextran to the oxyform
    • Prouchayret F., and Dellacherie E. Low oxygen affinity derivatives of human hemoglobin by fixation of polycarboxylic dextran to the oxyform. Biopolymers 33 (1993) 1803-1809
    • (1993) Biopolymers , vol.33 , pp. 1803-1809
    • Prouchayret, F.1    Dellacherie, E.2
  • 193
    • 0032211606 scopus 로고    scopus 로고
    • Polyethylene glycol-conjugated pharmaceutical proteins
    • Bailon P., and Berthold W. Polyethylene glycol-conjugated pharmaceutical proteins. Pharmaceut. Sci. Tech. Today 1 (1998) 352-356
    • (1998) Pharmaceut. Sci. Tech. Today , vol.1 , pp. 352-356
    • Bailon, P.1    Berthold, W.2
  • 194
    • 30144435054 scopus 로고    scopus 로고
    • CD163 is the macrophage scavenger receptor for native and chemically modified hemoglobins in the absence of haptoglobin
    • Schaer D.J., Schaer C.A., Buehler P.W., Boykins R.A., Schoedon G., Alayash A.I., and Schaffner A. CD163 is the macrophage scavenger receptor for native and chemically modified hemoglobins in the absence of haptoglobin. Blood 107 (2006) 373-380
    • (2006) Blood , vol.107 , pp. 373-380
    • Schaer, D.J.1    Schaer, C.A.2    Buehler, P.W.3    Boykins, R.A.4    Schoedon, G.5    Alayash, A.I.6    Schaffner, A.7
  • 195
    • 0022969334 scopus 로고
    • Preparation and evaluation of hemoglobin-polyethylene glycol conjugate (pyridoxalated polyethylene glycol hemoglobin) as an oxygen-carrying resuscitation fluid
    • Iwasaki K., and Iwashita Y. Preparation and evaluation of hemoglobin-polyethylene glycol conjugate (pyridoxalated polyethylene glycol hemoglobin) as an oxygen-carrying resuscitation fluid. Artif. Organs 10 (1986) 411-416
    • (1986) Artif. Organs , vol.10 , pp. 411-416
    • Iwasaki, K.1    Iwashita, Y.2
  • 196
    • 0028100475 scopus 로고
    • PEG-hemoglobin: an efficient oxygen-delivery system in the rat exchange transfusion and hypovolemic shock models
    • Nho K., Linberg R., Johnson M., Gilbert C., and Shorr R. PEG-hemoglobin: an efficient oxygen-delivery system in the rat exchange transfusion and hypovolemic shock models. Artif. Cells Blood Substit. Immobil. Biotechnol. 22 (1994) 795-803
    • (1994) Artif. Cells Blood Substit. Immobil. Biotechnol. , vol.22 , pp. 795-803
    • Nho, K.1    Linberg, R.2    Johnson, M.3    Gilbert, C.4    Shorr, R.5
  • 198
    • 4344592222 scopus 로고    scopus 로고
    • MP4, a new nonvasoactive polyethylene glycol-hemoglobin conjugate
    • Winslow R.M. MP4, a new nonvasoactive polyethylene glycol-hemoglobin conjugate. Artif. Organs 28 (2004) 800-806
    • (2004) Artif. Organs , vol.28 , pp. 800-806
    • Winslow, R.M.1
  • 200
    • 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
    • Hu T., Prabhakaran M., Acharya S.A., and Manjula B.N. 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
  • 201
    • 0021111673 scopus 로고
    • Schiff base adducts of glyceraldehyde with hemoglobin. Differences in the Amadori rearrangement at the alpha-amino groups
    • Acharya A.S., Sussman L.G., and Manning J.M. Schiff base adducts of glyceraldehyde with hemoglobin. Differences in the Amadori rearrangement at the alpha-amino groups. J. Biol. Chem. 258 (1983) 2296-2302
    • (1983) J. Biol. Chem. , vol.258 , pp. 2296-2302
    • Acharya, A.S.1    Sussman, L.G.2    Manning, J.M.3
  • 203
    • 37748998773 scopus 로고    scopus 로고
    • Solution structure of poly(ethylene) glycol-conjugated hemoglobin revealed by small-angle X-ray scattering: implications for a new oxygen therapeutic
    • Svergun D.I., Ekstrom F., Vandegriff K.D., Malavalli A., Baker D.A., Nilsson C., and Winslow R.M. Solution structure of poly(ethylene) glycol-conjugated hemoglobin revealed by small-angle X-ray scattering: implications for a new oxygen therapeutic. Biophys. J. 94 (2007) 173-181
    • (2007) Biophys. J. , vol.94 , pp. 173-181
    • Svergun, D.I.1    Ekstrom, F.2    Vandegriff, K.D.3    Malavalli, A.4    Baker, D.A.5    Nilsson, C.6    Winslow, R.M.7
  • 204
    • 33847314129 scopus 로고    scopus 로고
    • Trapping hemoglobin in rigid matrices: fine tuning of oxygen binding properties by modulation of encapsulation protocols
    • Bruno S., Ronda L., Bettati S., and Mozzarelli A. Trapping hemoglobin in rigid matrices: fine tuning of oxygen binding properties by modulation of encapsulation protocols. Artif. Cells Blood Substit. Immobil. Biotechnol. 35 (2007) 69-79
    • (2007) Artif. Cells Blood Substit. Immobil. Biotechnol. , vol.35 , pp. 69-79
    • Bruno, S.1    Ronda, L.2    Bettati, S.3    Mozzarelli, A.4
  • 205
    • 0034773128 scopus 로고    scopus 로고
    • Bio-doped nanocomposite polymers: sol-gel bioencapsulates
    • Gill I. Bio-doped nanocomposite polymers: sol-gel bioencapsulates. Chem. Mater. 13 (2001) 3404-3421
    • (2001) Chem. Mater. , vol.13 , pp. 3404-3421
    • Gill, I.1
  • 207
    • 0027128133 scopus 로고
    • Encapsulation of proteins in transparent porous silicate glasses prepared by the sol-gel method
    • Ellerby L., Nishida C.R., Nishida F., Yamanaka S.A., Dunn B., Valentine J.S., and Zink J.I. Encapsulation of proteins in transparent porous silicate glasses prepared by the sol-gel method. Science 255 (1992) 1113-1115
    • (1992) Science , vol.255 , pp. 1113-1115
    • Ellerby, L.1    Nishida, C.R.2    Nishida, F.3    Yamanaka, S.A.4    Dunn, B.5    Valentine, J.S.6    Zink, J.I.7
  • 208
    • 0034237721 scopus 로고    scopus 로고
    • Bioencapsulation within synthetic polymers (Part 1): sol-gel encapsulated biologicals
    • Gill I., and Ballesteros A. Bioencapsulation within synthetic polymers (Part 1): sol-gel encapsulated biologicals. Trends Biotechnol. 18 (2000) 282-296
    • (2000) Trends Biotechnol. , vol.18 , pp. 282-296
    • Gill, I.1    Ballesteros, A.2
  • 209
  • 210
    • 0023804160 scopus 로고
    • Red blood cell substitutes: microencapsulated hemoglobin and cross-linked hemoglobin including pyridoxylated polyhemoglobin & conjugated hemoglobin
    • Chang T.M. Red blood cell substitutes: microencapsulated hemoglobin and cross-linked hemoglobin including pyridoxylated polyhemoglobin & conjugated hemoglobin. Biomater. Artif. Cell Immobil. Biotechnol. 16 (1988) 11-29
    • (1988) Biomater. Artif. Cell Immobil. Biotechnol. , vol.16 , pp. 11-29
    • Chang, T.M.1
  • 211
    • 0024232476 scopus 로고
    • Artificial cells with ultrathin lipid-polymer or lipid-protein membranes
    • Chang T.M. Artificial cells with ultrathin lipid-polymer or lipid-protein membranes. Adv. Exp. Med. Biol. 238 (1988) 215-223
    • (1988) Adv. Exp. Med. Biol. , vol.238 , pp. 215-223
    • Chang, T.M.1
  • 212
    • 0023775078 scopus 로고
    • Attempts to find a method to prepare artificial hemoglobin corpuscles
    • Chang T.M. Attempts to find a method to prepare artificial hemoglobin corpuscles. Biomater. Artif. Cell Immobil. Biotechnol. 16 (1988) 1-9
    • (1988) Biomater. Artif. Cell Immobil. Biotechnol. , vol.16 , pp. 1-9
    • Chang, T.M.1
  • 213
    • 0028015898 scopus 로고
    • Efficacy, physical properties and pharmacokinetics of sterically-stabilized liposome-encapsulated hemoglobin
    • Zheng S., Zheng Y., and Beissinger R. Efficacy, physical properties and pharmacokinetics of sterically-stabilized liposome-encapsulated hemoglobin. Artif. Cells Blood Substit. Immobil. Biotechnol. 22 (1994) 487-501
    • (1994) Artif. Cells Blood Substit. Immobil. Biotechnol. , vol.22 , pp. 487-501
    • Zheng, S.1    Zheng, Y.2    Beissinger, R.3
  • 214
    • 0028577243 scopus 로고
    • Microencapsulation of hemoglobin in liposomes using a double emulsion, film dehydration/rehydration approach
    • Zheng S., Zheng Y., Beissinger R.L., and Fresco R. Microencapsulation of hemoglobin in liposomes using a double emulsion, film dehydration/rehydration approach. Biochim. Biophys. Acta 1196 (1994) 123-130
    • (1994) Biochim. Biophys. Acta , vol.1196 , pp. 123-130
    • Zheng, S.1    Zheng, Y.2    Beissinger, R.L.3    Fresco, R.4
  • 215
    • 11144330501 scopus 로고    scopus 로고
    • Liposome-encapsulated actin-hemoglobin (LEAcHb) artificial blood substitutes
    • Li S., Nickels J., and Palmer A.F. Liposome-encapsulated actin-hemoglobin (LEAcHb) artificial blood substitutes. Biomaterials 26 (2005) 3759-3769
    • (2005) Biomaterials , vol.26 , pp. 3759-3769
    • Li, S.1    Nickels, J.2    Palmer, A.F.3
  • 216
    • 22944465780 scopus 로고    scopus 로고
    • Polymersome encapsulated hemoglobin: a novel type of oxygen carrier
    • Arifin D.R., and Palmer A.F. Polymersome encapsulated hemoglobin: a novel type of oxygen carrier. Biomacromolecules 6 (2005) 2172-2181
    • (2005) Biomacromolecules , vol.6 , pp. 2172-2181
    • Arifin, D.R.1    Palmer, A.F.2
  • 217
    • 20044381699 scopus 로고    scopus 로고
    • Physical properties and stability mechanisms of poly(ethylene glycol) conjugated liposome encapsulated hemoglobin dispersions
    • Arifin D.R., and Palmer A.F. Physical properties and stability mechanisms of poly(ethylene glycol) conjugated liposome encapsulated hemoglobin dispersions. Artif. Cells Blood Substit. Immobil. Biotechnol. 33 (2005) 137-162
    • (2005) Artif. Cells Blood Substit. Immobil. Biotechnol. , vol.33 , pp. 137-162
    • Arifin, D.R.1    Palmer, A.F.2
  • 218
    • 0037885021 scopus 로고    scopus 로고
    • Future generations of red blood cell substitutes
    • Chang T.M. Future generations of red blood cell substitutes. J. Intern. Med. 253 (2003) 527-535
    • (2003) J. Intern. Med. , vol.253 , pp. 527-535
    • Chang, T.M.1
  • 219
    • 0028068407 scopus 로고
    • Submicron biodegradable polymer membrane hemoglobin nanocapsules as potential blood substitutes: a preliminary report
    • Yu W.P., and Chang T.M. Submicron biodegradable polymer membrane hemoglobin nanocapsules as potential blood substitutes: a preliminary report. Artif. Cells Blood Substit. Immobil. Biotechnol. 22 (1994) 889-893
    • (1994) Artif. Cells Blood Substit. Immobil. Biotechnol. , vol.22 , pp. 889-893
    • Yu, W.P.1    Chang, T.M.2
  • 220
    • 0029991651 scopus 로고    scopus 로고
    • Submicron polymer membrane hemoglobin nanocapsules as potential blood substitutes: preparation and characterization
    • Yu W.P., and Chang T.M. Submicron polymer membrane hemoglobin nanocapsules as potential blood substitutes: preparation and characterization. Artif. Cells Blood Substit. Immobil. Biotechnol. 24 (1996) 169-183
    • (1996) Artif. Cells Blood Substit. Immobil. Biotechnol. , vol.24 , pp. 169-183
    • Yu, W.P.1    Chang, T.M.2
  • 221
    • 1142297583 scopus 로고    scopus 로고
    • Heparin coated poly(alkylcyanoacrylate) nanoparticles coupled to hemoglobin: a new oxygen carrier
    • Chauvierre C., Marden M.C., Vauthier C., Labarre D., Couvreur P., and Leclerc L. Heparin coated poly(alkylcyanoacrylate) nanoparticles coupled to hemoglobin: a new oxygen carrier. Biomaterials 25 (2004) 3081-3086
    • (2004) Biomaterials , vol.25 , pp. 3081-3086
    • Chauvierre, C.1    Marden, M.C.2    Vauthier, C.3    Labarre, D.4    Couvreur, P.5    Leclerc, L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.