메뉴 건너뛰기




Volumn 52, Issue 1S, 2019, Pages 28-40

Current challenges in the development of acellular hemoglobin oxygen carriers by protein engineering

Author keywords

Autooxidation; blood substitutes; globin unfolding; hemin loss; hemoglobin toxicity; hemoglobin based oxygen carriers (HBOCs); NO scavenging; oxygen affinity

Indexed keywords

DIMER; GLOBIN; HAPTOGLOBIN; HEME; HEMIN; HEMOGLOBIN; NITRIC OXIDE; OXYGEN; REACTIVE OXYGEN METABOLITE; BLOOD SUBSTITUTE;

EID: 85065127266     PISSN: 10732322     EISSN: 15400514     Source Type: Journal    
DOI: 10.1097/SHK.0000000000001053     Document Type: Review
Times cited : (19)

References (93)
  • 1
    • 85072133781 scopus 로고    scopus 로고
    • Mechanisms of toxicity and modulation of hemoglobin-based oxygen carriers (HBOCs)
    • Alayash AI: Mechanisms of toxicity and modulation of hemoglobin-based oxygen carriers (HBOCs). Shock 52(Suppl. 1):41-49, 2019.
    • (2019) Shock , vol.52 , pp. 41-49
    • Alayash, A.I.1
  • 3
    • 33845903253 scopus 로고    scopus 로고
    • Chapter 1: Historical background
    • Winslow RM, editor, San Diego, CA: Academic Press
    • Winslow RM: Chapter 1: Historical background. In:Winslow RM, editor. Blood Substitutes. San Diego, CA: Academic Press; 2006. pp. 5-16.
    • (2006) Blood Substitutes , pp. 5-16
    • Winslow, R.M.1
  • 4
    • 84979136206 scopus 로고
    • Blood substitutes
    • Amberson WR: Blood substitutes. Biol Rev 12(1):48-86, 1937.
    • (1937) Biol Rev , vol.12 , Issue.1 , pp. 48-86
    • Amberson, W.R.1
  • 6
    • 77149146184 scopus 로고    scopus 로고
    • Fluid resuscitation: Past, present, and the future
    • Santry HP, Alam HB: Fluid resuscitation: Past, present, and the future. Shock 33(3):229-241, 2010.
    • (2010) Shock , vol.33 , Issue.3 , pp. 229-241
    • Santry, H.P.1    Alam, H.B.2
  • 7
    • 0036727717 scopus 로고    scopus 로고
    • Blood substitutes and oxygen therapeutics: An overview and current status
    • Jahr JS, Nesargi SB, Lewis K, Johnson C: Blood substitutes and oxygen therapeutics: An overview and current status. Am J Ther 9(5):437-443, 2002.
    • (2002) Am J Ther , vol.9 , Issue.5 , pp. 437-443
    • Jahr, J.S.1    Nesargi, S.B.2    Lewis, K.3    Johnson, C.4
  • 8
    • 77953353898 scopus 로고    scopus 로고
    • Setbacks in blood substitutes research and development: A biochemical perspective
    • Alayash AI: Setbacks in blood substitutes research and development: A biochemical perspective. Clin Lab Med 30(2):381-389, 2010.
    • (2010) Clin Lab Med , vol.30 , Issue.2 , pp. 381-389
    • Alayash, A.I.1
  • 9
    • 77957331298 scopus 로고    scopus 로고
    • Hemoglobin-based oxygen carriers: From mechanisms of toxicity and clearance to rational drug design
    • Buehler PW, D'Agnillo F, Schaer DJ: Hemoglobin-based oxygen carriers: From mechanisms of toxicity and clearance to rational drug design. Trends Mol Med 16(10):447-457, 2010.
    • (2010) Trends Mol Med , vol.16 , Issue.10 , pp. 447-457
    • Buehler, P.W.1    D'Agnillo, F.2    Schaer, D.J.3
  • 10
    • 84896546440 scopus 로고    scopus 로고
    • Blood substitutes: Why haven't we been more successful
    • Alayash AI: Blood substitutes: Why haven't we been more successful Trends Biotechnol 32(4):177-185, 2014.
    • (2014) Trends Biotechnol , vol.32 , Issue.4 , pp. 177-185
    • Alayash, A.I.1
  • 11
    • 84911384914 scopus 로고    scopus 로고
    • Hemoglobin-based oxygen carriers: Disclosed history and theway ahead: The relativity of safety
    • Weiskopf RB: Hemoglobin-based oxygen carriers: Disclosed history and theway ahead: The relativity of safety. Anesth Analg 119(4):758-760, 2014.
    • (2014) Anesth Analg , vol.119 , Issue.4 , pp. 758-760
    • Weiskopf, R.B.1
  • 13
    • 0014508657 scopus 로고
    • The renal handling of hemoglobin. I. Glomerular filtration
    • Bunn HF, Esham WT, Bull RW: The renal handling of hemoglobin. I. Glomerular filtration. J Exp Med 129(5):909-923, 1969.
    • (1969) J Exp Med , vol.129 , Issue.5 , pp. 909-923
    • Bunn, H.F.1    Esham, W.T.2    Bull, R.W.3
  • 14
    • 0014510315 scopus 로고
    • The renal handling of hemoglobin. II. Catabolism
    • Bunn HF, Jandl JH: The renal handling of hemoglobin. II. Catabolism. J Exp Med 129(5):925-934, 1969.
    • (1969) J Exp Med , vol.129 , Issue.5 , pp. 925-934
    • Bunn, H.F.1    Jandl, J.H.2
  • 15
    • 84859712543 scopus 로고    scopus 로고
    • Hemoglobin-driven pathophysiology is an in vivo consequence of the red blood cell storage lesion that can be attenuated in Guinea pigs by haptoglobin therapy
    • Baek JH, D'Agnillo F, Vallelian F, Pereira CP, Williams MC, Jia Y, Schaer DJ, Buehler PW: Hemoglobin-driven pathophysiology is an in vivo consequence of the red blood cell storage lesion that can be attenuated in guinea pigs by haptoglobin therapy. J Clin Invest 122(4):1444-1458, 2012.
    • (2012) J Clin Invest , vol.122 , Issue.4 , pp. 1444-1458
    • Baek, J.H.1    D'Agnillo, F.2    Vallelian, F.3    Pereira, C.P.4    Williams, M.C.5    Jia, Y.6    Schaer, D.J.7    Buehler, P.W.8
  • 16
    • 84904605942 scopus 로고    scopus 로고
    • The efficacy and safety of liquid stored blood and storage duration: A confused subject; Are patients confused
    • Weiskopf RB: The efficacy and safety of liquid stored blood and storage duration: A confused subject; are patients confused Anesth Analg 119(2):224-229, 2014.
    • (2014) Anesth Analg , vol.119 , Issue.2 , pp. 224-229
    • Weiskopf, R.B.1
  • 17
    • 30144435054 scopus 로고    scopus 로고
    • CD163 is the macrophage scavenger receptor for native and chemically modified hemoglobins in the absence of haptoglobin
    • Schaer DJ, Schaer CA, Buehler PW, Boykins RA, Schoedon G, Alayash AI, Schaffner A: CD163 is the macrophage scavenger receptor for native and chemically modified hemoglobins in the absence of haptoglobin. Blood 107(1):373-380, 2006.
    • (2006) Blood , vol.107 , Issue.1 , 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
  • 18
    • 84874439878 scopus 로고    scopus 로고
    • Hemolysis and free hemoglobin revisited: Exploring hemoglobin and hemin scavengers as a novel class of therapeutic proteins
    • Schaer DJ, Buehler PW, Alayash AI, Belcher JD, Vercellotti GM: Hemolysis and free hemoglobin revisited: Exploring hemoglobin and hemin scavengers as a novel class of therapeutic proteins. Blood 121(8):1276-1284, 2013.
    • (2013) Blood , vol.121 , Issue.8 , pp. 1276-1284
    • Schaer, D.J.1    Buehler, P.W.2    Alayash, A.I.3    Belcher, J.D.4    Vercellotti, G.M.5
  • 20
    • 0027251288 scopus 로고
    • Systemic and pulmonary hypertension after resuscitation with cell-free hemoglobin
    • Hess JR, MacDonaldVW, BrinkleyWW: Systemic and pulmonary hypertension after resuscitation with cell-free hemoglobin. J Appl Physiol 74(4):1769-1778, 1993.
    • (1993) J Appl Physiol , vol.74 , Issue.4 , pp. 1769-1778
    • Hess, J.R.1    MacDonald, V.W.2    Brinkley, W.W.3
  • 21
    • 52049114134 scopus 로고    scopus 로고
    • Cell-free oxygen carriers: Scientific foundations clinical development and new directions
    • Winslow RM: Cell-free oxygen carriers: Scientific foundations, clinical development, and new directions. Biochim Biophys Acta 1784(10):1382-1386, 2008.
    • (2008) Biochim Biophys Acta , vol.1784 , Issue.10 , pp. 1382-1386
    • Winslow, R.M.1
  • 22
    • 0024342431 scopus 로고
    • Ultrapure, stromafree, polymerized bovine hemoglobin solution: Evaluation of renal toxicity
    • Lee R, Atsumi N, Jacobs EE Jr, Austen WG, Vlahakes GJ: Ultrapure, stromafree, polymerized bovine hemoglobin solution: Evaluation of renal toxicity. J Surg Res 47(5):407-411, 1989.
    • (1989) J Surg Res , vol.47 , Issue.5 , pp. 407-411
    • Lee, R.1    Atsumi, N.2    Jacobs, E.E.3    Austen, W.G.4    Vlahakes, G.J.5
  • 23
    • 0023025879 scopus 로고
    • The development of polymerized pyridoxylated hemoglobin solution as a red cell substitute
    • Gould SA, Sehgal LR, Rosen AL, Sehgal HL, Moss GS: The development of polymerized pyridoxylated hemoglobin solution as a red cell substitute. Ann Emerg Med 15(12):1416-1419, 1986.
    • (1986) Ann Emerg Med , vol.15 , Issue.12 , pp. 1416-1419
    • Gould, S.A.1    Sehgal, L.R.2    Rosen, A.L.3    Sehgal, H.L.4    Moss, G.S.5
  • 24
    • 0023428522 scopus 로고
    • HbXL99 alpha: A hemoglobin derivative that is cross-linked between the alpha subunits is useful as a blood substitute
    • Snyder SR, Welty EV, Walder RY, Williams LA, Walder JA: HbXL99 alpha: A hemoglobin derivative that is cross-linked between the alpha subunits is useful as a blood substitute. Proc Natl Acad Sci USA 84(20):7280-7284, 1987.
    • (1987) Proc Natl Acad Sci USA , vol.84 , Issue.20 , pp. 7280-7284
    • Snyder, S.R.1    Welty, E.V.2    Walder, R.Y.3    Williams, L.A.4    Walder, J.A.5
  • 29
    • 0037054809 scopus 로고    scopus 로고
    • Myoglobin as a model system for designing heme protein based blood substitutes
    • Dou Y, Maillett DH, Eich RF, Olson JS: Myoglobin as a model system for designing heme protein based blood substitutes. Biophys Chem 98(1-2):127-148, 2002.
    • (2002) Biophys Chem , vol.98 , Issue.1-2 , pp. 127-148
    • Dou, Y.1    Maillett, D.H.2    Eich, R.F.3    Olson, J.S.4
  • 30
    • 0021752563 scopus 로고
    • Morphological and physiological factors affecting oxygen uptake and release by red blood cells
    • Vandegriff KD, Olson JS: Morphological and physiological factors affecting oxygen uptake and release by red blood cells. J Biol Chem 259:12619-12627, 1984.
    • (1984) J Biol Chem , vol.259 , pp. 12619-12627
    • Vandegriff, K.D.1    Olson, J.S.2
  • 31
    • 0023269001 scopus 로고
    • Physiological factors affecting O2 transport by hemoglobin in an in vitro capillary system
    • Lemon DD, Nair PK, Boland EJ, Olson JS, Hellums JD: Physiological factors affecting O2 transport by hemoglobin in an in vitro capillary system. J Appl Physiol 62(2):798-806, 1987.
    • (1987) J Appl Physiol , vol.62 , Issue.2 , pp. 798-806
    • Lemon, D.D.1    Nair, P.K.2    Boland, E.J.3    Olson, J.S.4    Hellums, J.D.5
  • 32
    • 0023245315 scopus 로고
    • An in vitro capillary system for studies on microcirculatory O2 transport
    • Boland EJ, Nair PK, Lemon DD, Olson JS, Hellums JD: An in vitro capillary system for studies on microcirculatory O2 transport. J Appl Physiol 62(2):791-797, 1987.
    • (1987) J Appl Physiol , vol.62 , Issue.2 , pp. 791-797
    • Boland, E.J.1    Nair, P.K.2    Lemon, D.D.3    Olson, J.S.4    Hellums, J.D.5
  • 33
    • 0031851792 scopus 로고    scopus 로고
    • Oxygen transport by erythrocyte/hemoglobin solution mixtures in an in vitro capillary as a model of hemoglobinbased oxygen carrier performance
    • Page TC, Light WR, McKay CB, Hellums JD: Oxygen transport by erythrocyte/hemoglobin solution mixtures in an in vitro capillary as a model of hemoglobinbased oxygen carrier performance. Microvasc Res 55(1):54-64, 1998.
    • (1998) Microvasc Res , vol.55 , Issue.1 , pp. 54-64
    • Page, T.C.1    Light, W.R.2    McKay, C.B.3    Hellums, J.D.4
  • 34
    • 52049110127 scopus 로고    scopus 로고
    • Chapter 5: The role of oxygen and hemoglobin diffusioin in oxygen transport by cell-free hemolgobins
    • Winslow R M, editor, San Diego, CA: Academic Press
    • Vandegriff KD: Chapter 5: The role of oxygen and hemoglobin diffusioin in oxygen transport by cell-free hemolgobins. In: Winslow R M, editor. Blood Substitutes. San Diego, CA: Academic Press; 2006. pp. 60-71.
    • (2006) Blood Substitutes , pp. 60-71
    • Vandegriff, K.D.1
  • 35
    • 52049111684 scopus 로고    scopus 로고
    • Chapter 6: Oxygen transport properties of hemoglobinbased-oxygen-carriers: Studies using artificial capillaries and mathematical simulation
    • Winslow RM, editor, San Diego, CA: Academic Press
    • Page TC, Hellums JD: Chapter 6: Oxygen transport properties of hemoglobinbased-oxygen-carriers: Studies using artificial capillaries and mathematical simulation. In: Winslow RM, editor. Blood Substitutes. San Diego, CA: Academic Press; 2006. pp. 72-83.
    • (2006) Blood Substitutes , pp. 72-83
    • Page, T.C.1    Hellums, J.D.2
  • 37
    • 0030773396 scopus 로고    scopus 로고
    • Myoglobin discriminates between O2, NO, and CO by electrostatic interactions with the bound ligand
    • Olson JS, Phillips GN: Myoglobin discriminates between O2, NO, and CO by electrostatic interactions with the bound ligand. J Biol Inorg Chem 2(4):544-552, 1997.
    • (1997) J Biol Inorg Chem , vol.2 , Issue.4 , pp. 544-552
    • Olson, J.S.1    Phillips, G.N.2
  • 38
    • 53249127146 scopus 로고    scopus 로고
    • Interfacial and distal-heme pocket mutations exhibit additive effects on the structure and function of hemoglobin
    • Maillett DH, Simplaceanu V, Shen TJ, Ho NT, Olson JS, Ho C: Interfacial and distal-heme pocket mutations exhibit additive effects on the structure and function of hemoglobin. Biochemistry 47(40):10551-10563, 2008.
    • (2008) Biochemistry , vol.47 , Issue.40 , pp. 10551-10563
    • Maillett, D.H.1    Simplaceanu, V.2    Shen, T.J.3    Ho, N.T.4    Olson, J.S.5    Ho, C.6
  • 39
    • 77950548846 scopus 로고    scopus 로고
    • Distal histidine stabilizes bound O2 and acts as a gate for ligand entry in both subunits of adult human hemoglobin
    • Birukou I, Schweers RL, Olson JS: Distal histidine stabilizes bound O2 and acts as a gate for ligand entry in both subunits of adult human hemoglobin. J Biol Chem 285(12):8840-8854, 2010.
    • (2010) J Biol Chem , vol.285 , Issue.12 , pp. 8840-8854
    • Birukou, I.1    Schweers, R.L.2    Olson, J.S.3
  • 40
    • 80051971672 scopus 로고    scopus 로고
    • Modulating distal cavities in the alpha and beta subunits of human HbA reveals the primary ligand migration pathway
    • Birukou I, Maillett DH, Birukova A, Olson JS: Modulating distal cavities in the alpha and beta subunits of human HbA reveals the primary ligand migration pathway. Biochemistry 50(34):7361-7374, 2011.
    • (2011) Biochemistry , vol.50 , Issue.34 , pp. 7361-7374
    • Birukou, I.1    Maillett, D.H.2    Birukova, A.3    Olson, J.S.4
  • 44
  • 45
    • 67649305095 scopus 로고    scopus 로고
    • Hemoglobin vesicles and red blood cells as carriers of carbon monoxide prior to oxygen for resuscitation after hemorrhagic shock in a rat model
    • Sakai H, Horinouchi H, Tsuchida E, Kobayashi K: Hemoglobin vesicles and red blood cells as carriers of carbon monoxide prior to oxygen for resuscitation after hemorrhagic shock in a rat model. Shock 31(5):507-514, 2009.
    • (2009) Shock , vol.31 , Issue.5 , pp. 507-514
    • Sakai, H.1    Horinouchi, H.2    Tsuchida, E.3    Kobayashi, K.4
  • 47
    • 12344337449 scopus 로고    scopus 로고
    • Effects of recombinanthemoglobin solutions rHb2.0 and rHb1.1 on blood pressure, intestinal blood flow, and gut oxygenation in a rat model of hemorrhagic shock
    • Raat NJ, Liu JF, Doyle MP, Burhop KE, Klein J, Ince C: Effects of recombinanthemoglobin solutions rHb2.0 and rHb1.1 on blood pressure, intestinal blood flow, and gut oxygenation in a rat model of hemorrhagic shock. J Lab Clin Med 145(1):21-32, 2005.
    • (2005) J Lab Clin Med , vol.145 , Issue.1 , pp. 21-32
    • Raat, N.J.1    Liu, J.F.2    Doyle, M.P.3    Burhop, K.E.4    Klein, J.5    Ince, C.6
  • 48
    • 33947494971 scopus 로고    scopus 로고
    • Structural basis of peroxide-mediated changes in human hemoglobin: A novel oxidative pathway
    • Jia Y, Buehler PW, Boykins RA, Venable RM, Alayash AI: Structural basis of peroxide-mediated changes in human hemoglobin: A novel oxidative pathway. J Biol Chem 282:4894-4907, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 4894-4907
    • Jia, Y.1    Buehler, P.W.2    Boykins, R.A.3    Venable, R.M.4    Alayash, A.I.5
  • 50
    • 85019887690 scopus 로고    scopus 로고
    • Oxidative pathways in the sickle cell and beyond
    • Alayash AI: Oxidative pathways in the sickle cell and beyond. Blood Cells Mol Dis 70:78-86, 2018.
    • (2018) Blood Cells Mol Dis , vol.70 , pp. 78-86
    • Alayash, A.I.1
  • 51
    • 85009754849 scopus 로고    scopus 로고
    • Hemoglobin-based blood substitutes and the treatment of sickle cell disease: More harm than help
    • Alayash AI: Hemoglobin-based blood substitutes and the treatment of sickle cell disease: More harm than help Biomolecules 7(1): Pii: E2, 2017
    • (2017) Biomolecules , vol.7 , Issue.1 , pp. E2
    • Alayash, A.I.1
  • 52
    • 56949088820 scopus 로고    scopus 로고
    • Tyrosine residues as redox cofactors in human hemoglobin: Implications for engineering nontoxic blood substitutes
    • Reeder BJ, Grey M, Silaghi-Dumitrescu RL, Svistunenko DA, Bulow L, Cooper CE, Wilson MT: Tyrosine residues as redox cofactors in human hemoglobin: Implications for engineering nontoxic blood substitutes. J Biol Chem 283(45):30780-30787, 2008.
    • (2008) J Biol Chem , vol.283 , Issue.45 , pp. 30780-30787
    • Reeder, B.J.1    Grey, M.2    Silaghi-Dumitrescu, R.L.3    Svistunenko, D.A.4    Bulow, L.5    Cooper, C.E.6    Wilson, M.T.7
  • 53
    • 84860875640 scopus 로고    scopus 로고
    • Engineering tyrosinebased electron flow pathways in proteins: The case of aplysia myoglobin
    • Reeder BJ, Svistunenko DA, Cooper CE, Wilson MT: Engineering tyrosinebased electron flow pathways in proteins: The case of aplysia myoglobin. J Am Chem Soc 134(18):7741-7749, 2012.
    • (2012) J Am Chem Soc , vol.134 , Issue.18 , pp. 7741-7749
    • Reeder, B.J.1    Svistunenko, D.A.2    Cooper, C.E.3    Wilson, M.T.4
  • 56
    • 0001902954 scopus 로고
    • The oxidation of haemoglobin to methaemoglobin by oxygen
    • Brooks J: The oxidation of haemoglobin to methaemoglobin by oxygen. Proc R Soc Lond 109:35-50, 1931.
    • (1931) Proc R Soc Lond , vol.109 , pp. 35-50
    • Brooks, J.1
  • 57
    • 0000675667 scopus 로고
    • The oxidation of haemoglobin to methaemoglobin by oxygen. II-the relation between the rate of oxidation and the partial pressure of oxygen
    • Brooks J: The oxidation of haemoglobin to methaemoglobin by oxygen. II-the relation between the rate of oxidation and the partial pressure of oxygen. Proc R Soc Lond B Biol Sci 118:560-577, 1935.
    • (1935) Proc R Soc Lond B Biol Sci , vol.118 , pp. 560-577
    • Brooks, J.1
  • 58
    • 84881509224 scopus 로고
    • The oxidation of haemoglobin to methaemoglobin by oxygen
    • Brooks J: The oxidation of haemoglobin to methaemoglobin by oxygen. J Physiol 107(3):332-335, 1948.
    • (1948) J Physiol , vol.107 , Issue.3 , pp. 332-335
    • Brooks, J.1
  • 59
    • 0019995366 scopus 로고
    • Mechanism of autooxidation for hemoglobins and myoglobins. Promotion of superoxide production by protons and anions
    • Wallace WJ, Houtchens RA, Maxwell JC, Caughey WS: Mechanism of autooxidation for hemoglobins and myoglobins. Promotion of superoxide production by protons and anions. J Biol Chem 257(9):4966-4977, 1982.
    • (1982) J Biol Chem , vol.257 , Issue.9 , pp. 4966-4977
    • Wallace, W.J.1    Houtchens, R.A.2    Maxwell, J.C.3    Caughey, W.S.4
  • 60
    • 0021503754 scopus 로고
    • A controversy on the mechanism of autoxidation of oxymyoglobin and oxyhaemoglobin: Oxidation dissociation or displacement
    • Shikama K: A controversy on the mechanism of autoxidation of oxymyoglobin and oxyhaemoglobin: Oxidation, dissociation, or displacement Biochem J 223(1):279-280, 1984.
    • (1984) Biochem J , vol.223 , Issue.1 , pp. 279-280
    • Shikama, K.1
  • 62
    • 0000448117 scopus 로고
    • The oxidation of myoglobin to metmyglobin by oxygen. 2. the relation between the first order rate constant and the partial pressure of oxygen
    • George P, Stratmann CJ: The oxidation of myoglobin to metmyglobin by oxygen. 2. The relation between the first order rate constant and the partial pressure of oxygen. Biochem J 51(3):418-425, 1952.
    • (1952) Biochem J , vol.51 , Issue.3 , pp. 418-425
    • George, P.1    Stratmann, C.J.2
  • 63
    • 0016156128 scopus 로고
    • The mechanisms of hemoglobin autoxidation. Evidence for proton-assisted nucleophilic displacement of superoxide by anions
    • Wallace WJ, Maxwell JC, Caughey WS: The mechanisms of hemoglobin autoxidation. Evidence for proton-assisted nucleophilic displacement of superoxide by anions. Biochem Biophys Res Commun 57(4):1104-1110, 1974.
    • (1974) Biochem Biophys Res Commun , vol.57 , Issue.4 , pp. 1104-1110
    • Wallace, W.J.1    Maxwell, J.C.2    Caughey, W.S.3
  • 64
    • 0002424327 scopus 로고
    • Nature of the iron-oxygen bond in oxyhaemoglobin
    • Weiss JJ: Nature of the iron-oxygen bond in oxyhaemoglobin. Nature 202:83-84, 1964.
    • (1964) Nature , vol.202 , pp. 83-84
    • Weiss, J.J.1
  • 65
    • 0029894282 scopus 로고    scopus 로고
    • Kinetic pathways and barriers for ligand binding to myoglobin
    • Olson JS, Phillips GN Jr: Kinetic pathways and barriers for ligand binding to myoglobin. J Biol Chem 271(30):17593-17596, 1996.
    • (1996) J Biol Chem , vol.271 , Issue.30 , pp. 17593-17596
    • Olson, J.S.1    Phillips, G.N.2
  • 67
    • 0026354021 scopus 로고
    • Autoxidation of hemoglobin enhanced by dissociation into dimers
    • Zhang L, Levy A, Rifkind JM: Autoxidation of hemoglobin enhanced by dissociation into dimers. J Biol Chem 266(36):24698-24701, 1991.
    • (1991) J Biol Chem , vol.266 , Issue.36 , pp. 24698-24701
    • Zhang, L.1    Levy, A.2    Rifkind, J.M.3
  • 69
    • 0015238997 scopus 로고
    • Functional heterogeneity of the alpha and beta chains in the oxidation-reduction reaction of human hemoglobin
    • MacQuarrie RA, Gibson QH: Functional heterogeneity of the alpha and beta chains in the oxidation-reduction reaction of human hemoglobin. J Biol Chem 246(2):517-522, 1971.
    • (1971) J Biol Chem , vol.246 , Issue.2 , pp. 517-522
    • MacQuarrie, R.A.1    Gibson, Q.H.2
  • 70
    • 0032502724 scopus 로고    scopus 로고
    • The molecular mechanism of autoxidation for human oxyhemoglobin. Tilting of the distal histidine causes nonequivalent oxidation in the b chain
    • Tsuruga M, Matsuoka A, Hachimori A, Sugawara Y, Shikama K: The molecular mechanism of autoxidation for human oxyhemoglobin. Tilting of the distal histidine causes nonequivalent oxidation in the b chain. J Biol Chem 273(15):8607-8615, 1998.
    • (1998) J Biol Chem , vol.273 , Issue.15 , pp. 8607-8615
    • Tsuruga, M.1    Matsuoka, A.2    Hachimori, A.3    Sugawara, Y.4    Shikama, K.5
  • 72
    • 85072251174 scopus 로고    scopus 로고
    • Chapter 1: Mammalian myoglobin as a model for understanding ligand affinities and discrimination in heme proteins
    • Ghosh A, editor, London: Elsevier
    • Olson JS, Ghosh A: Chapter 1: Mammalian myoglobin as a model for understanding ligand affinities and discrimination in heme proteins. In: Ghosh A, editor. The Smallest Biomolecules: Perspectives on Heme-Diatomic Interactions. London: Elsevier; 2007. pp. 2-17.
    • (2007) The Smallest Biomolecules: Perspectives on Heme-Diatomic Interactions , pp. 2-17
    • Olson, J.S.1    Ghosh, A.2
  • 74
    • 18544388369 scopus 로고    scopus 로고
    • A biophysical investigation of recombinant hemoglobins with aromatic B10 mutations in the distal heme pockets
    • Wiltrout ME, Giovannelli JL, Simplaceanu V, Lukin JA, Ho NT, Ho C: A biophysical investigation of recombinant hemoglobins with aromatic B10 mutations in the distal heme pockets. Biochemistry 44(19):7207-7217, 2005.
    • (2005) Biochemistry , vol.44 , Issue.19 , pp. 7207-7217
    • Wiltrout, M.E.1    Giovannelli, J.L.2    Simplaceanu, V.3    Lukin, J.A.4    Ho, N.T.5    Ho, C.6
  • 75
    • 84883359703 scopus 로고    scopus 로고
    • Autoxidation and oxygen binding properties of recombinant hemoglobins with substitutions at the alphaVal-62 or betaVal-67 position of the distal heme pocket
    • Tam MF, Rice NW, Maillett DH, Simplaceanu V, Ho NT, Tam TC, Shen TJ, Ho C: Autoxidation and oxygen binding properties of recombinant hemoglobins with substitutions at the alphaVal-62 or betaVal-67 position of the distal heme pocket. J Biol Chem 288(35):25512-25521, 2013.
    • (2013) J Biol Chem , vol.288 , Issue.35 , pp. 25512-25521
    • Tam, M.F.1    Rice, N.W.2    Maillett, D.H.3    Simplaceanu, V.4    Ho, N.T.5    Tam, T.C.6    Shen, T.J.7    Ho, C.8
  • 76
    • 0029737827 scopus 로고    scopus 로고
    • The stability of holomyoglobin is determined by heme affinity
    • Hargrove MS, Olson JS: The stability of holomyoglobin is determined by heme affinity. Biochemistry 35(35):11310-11318, 1996.
    • (1996) Biochemistry , vol.35 , Issue.35 , pp. 11310-11318
    • Hargrove, M.S.1    Olson, J.S.2
  • 77
    • 0030814099 scopus 로고    scopus 로고
    • Quaternary structure regulates hemin dissociation from human hemoglobin
    • Hargrove MS, Whitaker T, Olson JS, Vali RJ, Mathews AJ: Quaternary structure regulates hemin dissociation from human hemoglobin. J Biol Chem 272(28): 17385-17389, 1997.
    • (1997) J Biol Chem , vol.272 , Issue.28 , pp. 17385-17389
    • Hargrove, M.S.1    Whitaker, T.2    Olson, J.S.3    Vali, R.J.4    Mathews, A.J.5
  • 79
    • 0029737668 scopus 로고    scopus 로고
    • Structural factors governing hemin dissociation from metmyoglobin
    • Hargrove MS, Wilkinson AJ, Olson JS: Structural factors governing hemin dissociation from metmyoglobin. Biochemistry 35(35):11300-11309, 1996.
    • (1996) Biochemistry , vol.35 , Issue.35 , pp. 11300-11309
    • Hargrove, M.S.1    Wilkinson, A.J.2    Olson, J.S.3
  • 82
    • 84942288015 scopus 로고    scopus 로고
    • Apoglobin stability is the major factor governing both cell-free and in vivo expression of holomyoglobin
    • Samuel PP, Smith LP, Phillips GN Jr, Olson JS: Apoglobin stability is the major factor governing both cell-free and in vivo expression of holomyoglobin. J Biol Chem 290(39):23479-23495, 2015.
    • (2015) J Biol Chem , vol.290 , Issue.39 , pp. 23479-23495
    • Samuel, P.P.1    Smith, L.P.2    Phillips, G.N.3    Olson, J.S.4
  • 84
    • 0035975686 scopus 로고    scopus 로고
    • The role of facilitated diffusion in oxygen transport by cell-free hemoglobins: Implications for the design of hemoglobin-based oxygen carriers
    • McCarthy MR, Vandegriff KD, Winslow RM: The role of facilitated diffusion in oxygen transport by cell-free hemoglobins: Implications for the design of hemoglobin-based oxygen carriers. Biophys Chem 92(1-2):103-117, 2001.
    • (2001) Biophys Chem , vol.92 , Issue.1-2 , pp. 103-117
    • McCarthy, M.R.1    Vandegriff, K.D.2    Winslow, R.M.3
  • 85
    • 70349623928 scopus 로고    scopus 로고
    • A review of blood substitutes: Examining the history, clinical trial results, and ethics of hemoglobin-based oxygen carriers
    • Chen JY, Scerbo M, Kramer G: A review of blood substitutes: Examining the history, clinical trial results, and ethics of hemoglobin-based oxygen carriers. Clinics (Sao Paulo) 64(8):803-813, 2009.
    • (2009) Clinics (Sao Paulo) , vol.64 , Issue.8 , pp. 803-813
    • Chen, J.Y.1    Scerbo, M.2    Kramer, G.3
  • 86
    • 44249093233 scopus 로고    scopus 로고
    • Cell-free hemoglobinbased blood substitutes and risk of myocardial infarction and death: A metaanalysis
    • Natanson C, Kern SJ, Lurie P, Banks SM, Wolfe SM: Cell-free hemoglobinbased blood substitutes and risk of myocardial infarction and death: A metaanalysis. JAMA 299(19):2304-2312, 2008.
    • (2008) JAMA , vol.299 , Issue.19 , pp. 2304-2312
    • Natanson, C.1    Kern, S.J.2    Lurie, P.3    Banks, S.M.4    Wolfe, S.M.5
  • 87
    • 0028958911 scopus 로고
    • Effect of diaspirin crosslinked and stroma-reduced hemoglobin on mean arterial pressure and endothelin-1 concentration in rats
    • Gulati A, Singh G, Rebello S, Sharma AC: Effect of diaspirin crosslinked and stroma-reduced hemoglobin on mean arterial pressure and endothelin-1 concentration in rats. Life Sci 56(17):1433-1442, 1995.
    • (1995) Life Sci , vol.56 , Issue.17 , pp. 1433-1442
    • Gulati, A.1    Singh, G.2    Rebello, S.3    Sharma, A.C.4
  • 88
    • 33750546863 scopus 로고    scopus 로고
    • Oxidation and haem loss kinetics of poly(ethylene glycol)-conjugated haemoglobin (MP4): Dissociation between in vitro and in vivo oxidation rates
    • Vandegriff KD, Malavalli A, Minn C, Jiang E, Lohman J, Young MA, Samaja M, Winslow RM: Oxidation and haem loss kinetics of poly(ethylene glycol)-conjugated haemoglobin (MP4): Dissociation between in vitro and in vivo oxidation rates. Biochem J 399(3):463-471, 2006.
    • (2006) Biochem J , vol.399 , Issue.3 , pp. 463-471
    • Vandegriff, K.D.1    Malavalli, A.2    Minn, C.3    Jiang, E.4    Lohman, J.5    Young, M.A.6    Samaja, M.7    Winslow, R.M.8
  • 91
    • 85017325015 scopus 로고    scopus 로고
    • SANGUINATE (PEGylated carboxyhemoglobin bovine): Mechanism of action and clinical update
    • Abuchowski A: SANGUINATE (PEGylated carboxyhemoglobin bovine): Mechanism of action and clinical update. Artif Organs 41(4):346-350, 2017.
    • (2017) Artif Organs , vol.41 , Issue.4 , pp. 346-350
    • Abuchowski, A.1
  • 93
    • 34547600479 scopus 로고    scopus 로고
    • Resuscitation with recombinant hemoglobin rHb2.0 in a rodent model of hemorrhagic shock
    • Hermann J, Corso C, Messmer KF: Resuscitation with recombinant hemoglobin rHb2.0 in a rodent model of hemorrhagic shock. Anesthesiology 107(2):273-280, 2007.
    • (2007) Anesthesiology , vol.107 , Issue.2 , pp. 273-280
    • Hermann, J.1    Corso, C.2    Messmer, K.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.