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Volumn 25, Issue 2, 2009, Pages 357-371

Design of Recombinant Hemoglobins for Use in Transfusion Fluids

Author keywords

Blood substitute; Hemoglobin; Myoglobin; Nitric oxide; Oxygen carrier; Transfusion

Indexed keywords

ARTIFICIAL BLOOD; BLOOD SUBSTITUTE; DIASPIRIN CROSSLINKED HEMOGLOBIN; HEME; HEMOGLOBIN; HEMOSPAN; MUTANT PROTEIN; MYOGLOBIN; OXYVITA; PLASMA SUBSTITUTE; POLYMERIZED HEMOGLOBIN; RECOMBINANT HEMOGLOBIN; SANGUINATE; UNCLASSIFIED DRUG;

EID: 63049083139     PISSN: 07490704     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ccc.2008.12.010     Document Type: Review
Times cited : (17)

References (71)
  • 1
    • 0032829052 scopus 로고    scopus 로고
    • Blood substitutes. Haemoglobin therapeutics in clinical practice
    • Baron J.F. Blood substitutes. Haemoglobin therapeutics in clinical practice. Crit Care 3 (1999) R99-102
    • (1999) Crit Care , vol.3
    • Baron, J.F.1
  • 3
    • 0035105732 scopus 로고    scopus 로고
    • Progress in the development of RBC substitutes
    • Stowell C.P., Levin J., Spiess B.D., et al. Progress in the development of RBC substitutes. Transfusion 41 (2001) 287-299
    • (2001) Transfusion , vol.41 , pp. 287-299
    • Stowell, C.P.1    Levin, J.2    Spiess, B.D.3
  • 4
    • 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
  • 5
    • 41149136346 scopus 로고    scopus 로고
    • Blood substitutes: time for a deep breath
    • Stowell C. Blood substitutes: time for a deep breath. Transfusion 48 (2008) 574-575
    • (2008) Transfusion , vol.48 , pp. 574-575
    • Stowell, C.1
  • 6
    • 0025907017 scopus 로고
    • Intravascular retention and renal handling of purified natural and intramolecularly cross-linked hemoglobins
    • Urbaitis B., Razynska A., Corteza Q., et al. Intravascular retention and renal handling of purified natural and intramolecularly cross-linked hemoglobins. J Lab Clin Med 117 (1991) 115-121
    • (1991) J Lab Clin Med , vol.117 , pp. 115-121
    • Urbaitis, B.1    Razynska, A.2    Corteza, Q.3
  • 7
    • 0033806357 scopus 로고    scopus 로고
    • Appearance of dissociable and cross-linked hemoglobins in the renal hilar lymph
    • Matheson B., Razynska A., Kwansa H., et al. Appearance of dissociable and cross-linked hemoglobins in the renal hilar lymph. J Lab Clin Med 135 (2000) 459-464
    • (2000) J Lab Clin Med , vol.135 , pp. 459-464
    • Matheson, B.1    Razynska, A.2    Kwansa, H.3
  • 8
    • 23944469330 scopus 로고    scopus 로고
    • Role of nitric oxide scavenging in vascular response to cell-free hemoglobin transfusion
    • Sampei K., Ulatowski J.A., Asano Y., et al. Role of nitric oxide scavenging in vascular response to cell-free hemoglobin transfusion. Am J Physiol Heart Circ Physiol 289 (2005) H1191-H1201
    • (2005) Am J Physiol Heart Circ Physiol , vol.289
    • Sampei, K.1    Ulatowski, J.A.2    Asano, Y.3
  • 9
    • 0031851792 scopus 로고    scopus 로고
    • Oxygen transport by erythrocyte/hemoglobin solution mixtures in an in vitro capillary as a model of hemoglobin-based oxygen carrier performance
    • Page T.C., Light W.R., McKay C.B., et al. Oxygen transport by erythrocyte/hemoglobin solution mixtures in an in vitro capillary as a model of hemoglobin-based oxygen carrier performance. Microvasc Res 55 (1998) 54-64
    • (1998) Microvasc Res , vol.55 , pp. 54-64
    • Page, T.C.1    Light, W.R.2    McKay, C.B.3
  • 10
    • 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 M.R., Vandegriff K.D., and Winslow R.M. The role of facilitated diffusion in oxygen transport by cell-free hemoglobins: implications for the design of hemoglobin-based oxygen carriers. Biophys Chem 92 (2001) 103-117
    • (2001) Biophys Chem , vol.92 , pp. 103-117
    • McCarthy, M.R.1    Vandegriff, K.D.2    Winslow, R.M.3
  • 11
    • 14644410424 scopus 로고    scopus 로고
    • 2 delivery by low-p50 hemoglobin: a new basis for hemoglobin-based oxygen carriers
    • 2 delivery by low-p50 hemoglobin: a new basis for hemoglobin-based oxygen carriers. Artif Cells Blood Substit Immobil Biotechnol 33 (2005) 1-12
    • (2005) Artif Cells Blood Substit Immobil Biotechnol , vol.33 , pp. 1-12
    • Winslow, R.M.1
  • 12
    • 33751198276 scopus 로고    scopus 로고
    • Dissociation of local nitric oxide concentration and vasoconstriction in the presence of cell-free hemoglobin oxygen carriers
    • Tsai A.G., Cabrales P., Manjula B.N., et al. Dissociation of local nitric oxide concentration and vasoconstriction in the presence of cell-free hemoglobin oxygen carriers. Blood 108 (2006) 3603-3610
    • (2006) Blood , vol.108 , pp. 3603-3610
    • Tsai, A.G.1    Cabrales, P.2    Manjula, B.N.3
  • 14
    • 0038170347 scopus 로고    scopus 로고
    • Resuscitation with polyethylene glycol-modified human hemoglobin improves microcirculatory blood flow and tissue oxygenation after hemorrhagic shock in awake hamsters
    • Wettstein R., Tsai A.G., Erni D., et al. Resuscitation with polyethylene glycol-modified human hemoglobin improves microcirculatory blood flow and tissue oxygenation after hemorrhagic shock in awake hamsters. Crit Care Med 31 (2003) 1824-1830
    • (2003) Crit Care Med , vol.31 , pp. 1824-1830
    • Wettstein, R.1    Tsai, A.G.2    Erni, D.3
  • 15
    • 0033624586 scopus 로고    scopus 로고
    • αα-crosslinked hemoglobin: was failure predicted by preclinical testing?
    • Winslow R.M. αα-crosslinked hemoglobin: was failure predicted by preclinical testing?. Vox Sang 79 (2000) 1-20
    • (2000) Vox Sang , vol.79 , pp. 1-20
    • Winslow, R.M.1
  • 16
    • 0029888711 scopus 로고    scopus 로고
    • Physiology and pharmacokinetics of a novel hemoglobin-based oxygen carrier in humans
    • Hughes G.S., Antal E.J., Locker P.K., et al. Physiology and pharmacokinetics of a novel hemoglobin-based oxygen carrier in humans. Crit Care Clin 24 (1996) 756-764
    • (1996) Crit Care Clin , vol.24 , pp. 756-764
    • Hughes, G.S.1    Antal, E.J.2    Locker, P.K.3
  • 17
    • 0029990895 scopus 로고    scopus 로고
    • Effects of a hemoglobin-based oxygen carrier (HBOC-201) on hemodynamics and oxygen transport in patients undergoing preoperative hemodilution for elective abdominal aortic surgery
    • Kasper S.M., Walter M., Grune F., et al. Effects of a hemoglobin-based oxygen carrier (HBOC-201) on hemodynamics and oxygen transport in patients undergoing preoperative hemodilution for elective abdominal aortic surgery. Anesth Analg 83 (1996) 921-927
    • (1996) Anesth Analg , vol.83 , pp. 921-927
    • Kasper, S.M.1    Walter, M.2    Grune, F.3
  • 18
    • 0031858604 scopus 로고    scopus 로고
    • The first randomized trial of human polymerized hemoglobin as a blood substitute in acute trauma and emergent surgery
    • Gould S.A., Moore E.E., Hoyt D.B., et al. The first randomized trial of human polymerized hemoglobin as a blood substitute in acute trauma and emergent surgery. J Am Coll Surg 187 (1998) 113-120
    • (1998) J Am Coll Surg , vol.187 , pp. 113-120
    • Gould, S.A.1    Moore, E.E.2    Hoyt, D.B.3
  • 19
    • 0036789874 scopus 로고    scopus 로고
    • The life-sustaining capacity of human polymerized hemoglobin when red cells might be unavailable
    • Gould S.A., Moore E.E., Hoyt D.B., et al. The life-sustaining capacity of human polymerized hemoglobin when red cells might be unavailable. J Am Coll Surg 195 (2002) 445-452
    • (2002) J Am Coll Surg , vol.195 , pp. 445-452
    • Gould, S.A.1    Moore, E.E.2    Hoyt, D.B.3
  • 20
    • 0036785040 scopus 로고    scopus 로고
    • Vascular response to infusions of a nonextravasating hemoglobin polymer
    • Matheson B., Kwansa H.E., Bucci E., et al. Vascular response to infusions of a nonextravasating hemoglobin polymer. J Appl Phys 93 (2002) 1479-1486
    • (2002) J Appl Phys , vol.93 , pp. 1479-1486
    • Matheson, B.1    Kwansa, H.E.2    Bucci, E.3
  • 21
    • 0026699027 scopus 로고
    • PEG-bovine hemoglobin: safety in a canine dehydrated hypovolemic-hemorrhagic shock model
    • Nho K., Glower D., Bredehoeft S., et al. PEG-bovine hemoglobin: safety in a canine dehydrated hypovolemic-hemorrhagic shock model. Biomater Artif Cells Immobilization Biotechnol 20 (1992) 511-524
    • (1992) Biomater Artif Cells Immobilization Biotechnol , vol.20 , pp. 511-524
    • Nho, K.1    Glower, D.2    Bredehoeft, S.3
  • 22
    • 33751338255 scopus 로고    scopus 로고
    • A multicenter clinical study of the safety and activity of maleimide-polyethylene glycol-modified hemoglobin (Hemospan) in patients undergoing major orthopedic surgery
    • Olofsson C., Ahl T., Johansson T., et al. A multicenter clinical study of the safety and activity of maleimide-polyethylene glycol-modified hemoglobin (Hemospan) in patients undergoing major orthopedic surgery. Anesthesiology 105 (2006) 1153-1163
    • (2006) Anesthesiology , vol.105 , pp. 1153-1163
    • Olofsson, C.1    Ahl, T.2    Johansson, T.3
  • 23
    • 39049134910 scopus 로고    scopus 로고
    • A randomized, single-blind, increasing dose safety trial of an oxygen-carrying plasma expander (Hemospan) administered to orthopaedic surgery patients with spinal anaesthesia
    • Olofsson C., Nygards E.B., Ponzer S., et al. A randomized, single-blind, increasing dose safety trial of an oxygen-carrying plasma expander (Hemospan) administered to orthopaedic surgery patients with spinal anaesthesia. Transfus Med 18 (2008) 28-39
    • (2008) Transfus Med , vol.18 , pp. 28-39
    • Olofsson, C.1    Nygards, E.B.2    Ponzer, S.3
  • 24
    • 44249093233 scopus 로고    scopus 로고
    • Cell-free hemoglobin-based blood substitutes and risk of myocardial infarction and death: a meta-analysis
    • Natanson C., Kern S.J., Lurie P., et al. Cell-free hemoglobin-based blood substitutes and risk of myocardial infarction and death: a meta-analysis. JAMA 299 (2008) 2304-2312
    • (2008) JAMA , vol.299 , pp. 2304-2312
    • Natanson, C.1    Kern, S.J.2    Lurie, P.3
  • 25
    • 0021153567 scopus 로고
    • Generation of beta-globin by sequence-specific proteolysis of a hybrid protein produced in Escherichia coli
    • Nagai K., and Thogersen H.C. Generation of beta-globin by sequence-specific proteolysis of a hybrid protein produced in Escherichia coli. Nature 309 (1984) 810-812
    • (1984) Nature , vol.309 , pp. 810-812
    • Nagai, K.1    Thogersen, H.C.2
  • 26
    • 0026002149 scopus 로고
    • Recombinant human hemoglobin: expression and refolding of beta-globin from Escherichia coli
    • Fronticelli C., O'Donnell J.K., and Brinigar W.S. Recombinant human hemoglobin: expression and refolding of beta-globin from Escherichia coli. J Protein Chem 10 (1991) 495-501
    • (1991) J Protein Chem , vol.10 , pp. 495-501
    • Fronticelli, C.1    O'Donnell, J.K.2    Brinigar, W.S.3
  • 27
    • 0025760849 scopus 로고
    • Functional role of the distal valine (E11) residue of alpha subunits in human haemoglobin
    • Tame J., Shih D.T., Pagnier J., et al. Functional role of the distal valine (E11) residue of alpha subunits in human haemoglobin. J Mol Biol 218 (1991) 761-767
    • (1991) J Mol Biol , vol.218 , pp. 761-767
    • Tame, J.1    Shih, D.T.2    Pagnier, J.3
  • 28
    • 0031034230 scopus 로고    scopus 로고
    • Assembly of human hemoglobin. Studies with Escherichia coli-expressed alpha-globin
    • Sanna M.T., Razynska A., Karavitis M., et al. Assembly of human hemoglobin. Studies with Escherichia coli-expressed alpha-globin. J Biol Chem 272 (1997) 3478-3486
    • (1997) J Biol Chem , vol.272 , pp. 3478-3486
    • Sanna, M.T.1    Razynska, A.2    Karavitis, M.3
  • 29
    • 0026550785 scopus 로고
    • A human recombinant haemoglobin designed for use as a blood substitute
    • Looker D., Abbott-Brown D., Cozart P., et al. A human recombinant haemoglobin designed for use as a blood substitute. Nature 356 (1992) 258-260
    • (1992) Nature , vol.356 , pp. 258-260
    • Looker, D.1    Abbott-Brown, D.2    Cozart, P.3
  • 30
    • 0028245069 scopus 로고
    • Expression of recombinant human hemoglobin in Escherichia coli
    • Looker D., Mathews A.J., Neway J.O., et al. Expression of recombinant human hemoglobin in Escherichia coli. Meth Enzymol 231 (1994) 364-374
    • (1994) Meth Enzymol , vol.231 , pp. 364-374
    • Looker, D.1    Mathews, A.J.2    Neway, J.O.3
  • 31
    • 0027169919 scopus 로고
    • Production of unmodified human adult hemoglobin in Escherichia coli
    • Shen T.J., Ho N.T., Simplaceanu V., et al. Production of unmodified human adult hemoglobin in Escherichia coli. Proc Natl Acad Sci USA 90 (1993) 8108-8112
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 8108-8112
    • Shen, T.J.1    Ho, N.T.2    Simplaceanu, V.3
  • 32
    • 0034282637 scopus 로고    scopus 로고
    • The stabilities of mammalian apomyoglobins vary over a 600-fold range and can be enhanced by comparative mutagenesis
    • Scott E.E., Paster E.V., and Olson J.S. The stabilities of mammalian apomyoglobins vary over a 600-fold range and can be enhanced by comparative mutagenesis. J Biol Chem 275 (2000) 27129-27136
    • (2000) J Biol Chem , vol.275 , pp. 27129-27136
    • Scott, E.E.1    Paster, E.V.2    Olson, J.S.3
  • 33
    • 0037071860 scopus 로고    scopus 로고
    • An abundant erythroid protein that stabilizes free alpha-haemoglobin
    • Kihm A.J., Kong Y., Hong W., et al. An abundant erythroid protein that stabilizes free alpha-haemoglobin. Nature 417 (2002) 758-763
    • (2002) Nature , vol.417 , pp. 758-763
    • Kihm, A.J.1    Kong, Y.2    Hong, W.3
  • 34
    • 0037175053 scopus 로고    scopus 로고
    • Biophysical characterization of the alpha-globin binding protein alpha-hemoglobin stabilizing protein
    • Gell D., Kong Y., Eaton S.A., et al. Biophysical characterization of the alpha-globin binding protein alpha-hemoglobin stabilizing protein. J Biol Chem 277 (2002) 40602-40609
    • (2002) J Biol Chem , vol.277 , pp. 40602-40609
    • Gell, D.1    Kong, Y.2    Eaton, S.A.3
  • 35
    • 8844285199 scopus 로고    scopus 로고
    • Molecular mechanism of AHSP-mediated stabilization of alpha-hemoglobin
    • Feng L., Gell D.A., Zhou S., et al. Molecular mechanism of AHSP-mediated stabilization of alpha-hemoglobin. Cell 119 (2004) 629-640
    • (2004) Cell , vol.119 , pp. 629-640
    • Feng, L.1    Gell, D.A.2    Zhou, S.3
  • 37
    • 0028092986 scopus 로고
    • Genetic engineering of myoglobin as a simple prototype for hemoglobin-based blood substitutes
    • Olson J.S. Genetic engineering of myoglobin as a simple prototype for hemoglobin-based blood substitutes. Artif Cells Blood Substit Immobil Biotechnol 22 (1994) 429-441
    • (1994) Artif Cells Blood Substit Immobil Biotechnol , vol.22 , pp. 429-441
    • Olson, J.S.1
  • 38
    • 0001306148 scopus 로고
    • Mechanisms of ligand recognition by myoglobin
    • Springer B.A., Sligar S.G., Olson J.S., et al. Mechanisms of ligand recognition by myoglobin. Chem Rev 94 (1994) 699-714
    • (1994) Chem Rev , vol.94 , pp. 699-714
    • Springer, B.A.1    Sligar, S.G.2    Olson, J.S.3
  • 39
    • 0035797912 scopus 로고    scopus 로고
    • Heme pocket disorder in myoglobin: reversal by acid-induced soft refolding
    • Piro M.C., Militello V., Leone M., et al. Heme pocket disorder in myoglobin: reversal by acid-induced soft refolding. Biochemistry 40 (2001) 11841-11850
    • (2001) Biochemistry , vol.40 , pp. 11841-11850
    • Piro, M.C.1    Militello, V.2    Leone, M.3
  • 41
    • 0027447814 scopus 로고
    • Recombinant human hemoglobin: modification of the polarity of the beta-heme pocket by a valine67(E11)→threonine mutation
    • Fronticelli C., Brinigar W.S., Olson J.S., et al. Recombinant human hemoglobin: modification of the polarity of the beta-heme pocket by a valine67(E11)→threonine mutation. Biochemistry 32 (1993) 1235-1242
    • (1993) Biochemistry , vol.32 , pp. 1235-1242
    • Fronticelli, C.1    Brinigar, W.S.2    Olson, J.S.3
  • 42
    • 0030068978 scopus 로고    scopus 로고
    • Crystallographic, molecular modeling, and biophysical characterization of the valine beta 67 (E11)→threonine variant of hemoglobin
    • Pechik I., Ji X., Fidelis K., et al. Crystallographic, molecular modeling, and biophysical characterization of the valine beta 67 (E11)→threonine variant of hemoglobin. Biochemistry 35 (1996) 1935-1945
    • (1996) Biochemistry , vol.35 , pp. 1935-1945
    • Pechik, I.1    Ji, X.2    Fidelis, K.3
  • 43
    • 1342264353 scopus 로고    scopus 로고
    • NO scavenging and the hypertensive effect of hemoglobin-based blood substitutes
    • Olson J.S., Foley E.W., Rogge C., et al. NO scavenging and the hypertensive effect of hemoglobin-based blood substitutes. Free Radic Biol Med 36 (2004) 685-697
    • (2004) Free Radic Biol Med , vol.36 , pp. 685-697
    • Olson, J.S.1    Foley, E.W.2    Rogge, C.3
  • 44
    • 0029862605 scopus 로고    scopus 로고
    • Regional blood flow alterations after bovine fumaryl ββ-crosslinked hemoglobin transfusion and nitric oxide synthase inhibition
    • Ulatowski J.A., Nishikawa T., Matheson-Urbaitis B., et al. Regional blood flow alterations after bovine fumaryl ββ-crosslinked hemoglobin transfusion and nitric oxide synthase inhibition. Crit Care Med 24 (1996) 558-565
    • (1996) Crit Care Med , vol.24 , pp. 558-565
    • Ulatowski, J.A.1    Nishikawa, T.2    Matheson-Urbaitis, B.3
  • 45
    • 84882504096 scopus 로고    scopus 로고
    • Designing recombinant hemoglobin for use as a blood substitute
    • Winslow R.M. (Ed), Academic Press/Elsevier, Amsterdam
    • Olson J.S., and Maillett D.S. Designing recombinant hemoglobin for use as a blood substitute. In: Winslow R.M. (Ed). Blood substitutes (2006), Academic Press/Elsevier, Amsterdam 354-374
    • (2006) Blood substitutes , pp. 354-374
    • Olson, J.S.1    Maillett, D.S.2
  • 46
    • 0031856673 scopus 로고    scopus 로고
    • Rate of reaction with nitric oxide determines the hypertensive effect of cell-free hemoglobin
    • Doherty D.H., Doyle M.P., Curry S.R., et al. Rate of reaction with nitric oxide determines the hypertensive effect of cell-free hemoglobin. Nat Biotechnol 16 (1998) 672-676
    • (1998) Nat Biotechnol , vol.16 , pp. 672-676
    • Doherty, D.H.1    Doyle, M.P.2    Curry, S.R.3
  • 47
    • 0032524907 scopus 로고    scopus 로고
    • Arterial blood pressure responses to cell-free hemoglobin solutions and the reaction with nitric oxide
    • Rohlfs R.J., Bruner E., Chiu A., et al. Arterial blood pressure responses to cell-free hemoglobin solutions and the reaction with nitric oxide. J Biol Chem 273 (1998) 12128-12134
    • (1998) J Biol Chem , vol.273 , pp. 12128-12134
    • Rohlfs, R.J.1    Bruner, E.2    Chiu, A.3
  • 48
    • 33644829756 scopus 로고    scopus 로고
    • Role of 20-HETE in the pial arteriolar constrictor response to decreased hematocrit after exchange transfusion of cell-free polymeric hemoglobin
    • Qin X., Kwansa H., Bucci E., et al. Role of 20-HETE in the pial arteriolar constrictor response to decreased hematocrit after exchange transfusion of cell-free polymeric hemoglobin. J Appl Phys 100 (2006) 336-342
    • (2006) J Appl Phys , vol.100 , pp. 336-342
    • Qin, X.1    Kwansa, H.2    Bucci, E.3
  • 49
    • 52049100803 scopus 로고    scopus 로고
    • Insensitivity of cerebral oxygen transport to oxygen affinity of hemoglobin-based oxygen carriers
    • Koehler R.C., Fronticelli C., and Bucci E. Insensitivity of cerebral oxygen transport to oxygen affinity of hemoglobin-based oxygen carriers. Biochim Biophys Acta 1784 (2008) 1387-1394
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 1387-1394
    • Koehler, R.C.1    Fronticelli, C.2    Bucci, E.3
  • 50
    • 0036785042 scopus 로고    scopus 로고
    • Rate of NO scavenging alters effects of recombinant hemoglobin solutions on pulmonary vasoreactivity
    • Resta T.C., Walker B.R., Eichinger M.R., et al. Rate of NO scavenging alters effects of recombinant hemoglobin solutions on pulmonary vasoreactivity. J Appl Phys 93 (2002) 1327-1336
    • (2002) J Appl Phys , vol.93 , pp. 1327-1336
    • Resta, T.C.1    Walker, B.R.2    Eichinger, M.R.3
  • 51
    • 12344337449 scopus 로고    scopus 로고
    • Effects of recombinant-hemoglobin solutions rHb2.0 and rHb1.1 on blood pressure, intestinal blood flow, and gut oxygenation in a rat model of hemorrhagic shock
    • Raat N.J., Liu J.F., Doyle M.P., et al. Effects of recombinant-hemoglobin 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 (2005) 21-32
    • (2005) J Lab Clin Med , vol.145 , pp. 21-32
    • Raat, N.J.1    Liu, J.F.2    Doyle, M.P.3
  • 52
    • 0029561342 scopus 로고
    • Allosteric modulation by tertiary structure in mammalian hemoglobins. Introduction of the functional characteristics of bovine hemoglobin into human hemoglobin by five amino acid substitutions
    • Fronticelli C., Sanna M.T., Perez-Alvarado G.C., et al. Allosteric modulation by tertiary structure in mammalian hemoglobins. Introduction of the functional characteristics of bovine hemoglobin into human hemoglobin by five amino acid substitutions. J Biol Chem 270 (1995) 30588-30592
    • (1995) J Biol Chem , vol.270 , pp. 30588-30592
    • Fronticelli, C.1    Sanna, M.T.2    Perez-Alvarado, G.C.3
  • 53
    • 0037054808 scopus 로고    scopus 로고
    • Introduction of a new regulatory mechanism into human hemoglobin
    • Fronticelli C., Bobofchak K.M., Karavitis M., et al. Introduction of a new regulatory mechanism into human hemoglobin. Biophys Chem 98 (2002) 115-126
    • (2002) Biophys Chem , vol.98 , pp. 115-126
    • Fronticelli, C.1    Bobofchak, K.M.2    Karavitis, M.3
  • 54
    • 0037054858 scopus 로고    scopus 로고
    • Recombinant hemoglobins with low oxygen affinity and high cooperativity
    • Tsai C.H., and Ho C. Recombinant hemoglobins with low oxygen affinity and high cooperativity. Biophys Chem 98 (2002) 15-25
    • (2002) Biophys Chem , vol.98 , pp. 15-25
    • Tsai, C.H.1    Ho, C.2
  • 55
    • 0002813725 scopus 로고    scopus 로고
    • Overview of preclinical and clinical efficacy of Biopure's HBOCs
    • Chang T. (Ed), Karger/Landes, Basel (Switzerland)
    • Pearce L., and Gawryl M. Overview of preclinical and clinical efficacy of Biopure's HBOCs. In: Chang T. (Ed). Blood substitutes: principles, methods, products and clinical trials (1998), Karger/Landes, Basel (Switzerland)
    • (1998) Blood substitutes: principles, methods, products and clinical trials
    • Pearce, L.1    Gawryl, M.2
  • 56
    • 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., et al. Solution structure of poly (ethylene) glycol-conjugated hemoglobin revealed by small-angle X-ray scattering: implications for a new oxygen therapeutic. Biophys J 94 (2008) 173-181
    • (2008) Biophys J , vol.94 , pp. 173-181
    • Svergun, D.I.1    Ekstrom, F.2    Vandegriff, K.D.3
  • 57
    • 0035882543 scopus 로고    scopus 로고
    • Molecular engineering of a polymer of tetrameric hemoglobins
    • Fronticelli C., Arosio D., Bobofchak K.M., et al. 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
  • 58
    • 33646403158 scopus 로고    scopus 로고
    • 2-affinity recombinant hemoglobin polymers in mouse
    • 2-affinity recombinant hemoglobin polymers in mouse. J Appl Phys 100 (2006) 1688-1691
    • (2006) J Appl Phys , vol.100 , pp. 1688-1691
    • Nemoto, M.1    Mito, T.2    Brinigar, W.S.3
  • 59
    • 0029411044 scopus 로고
    • Hematologic effects of a novel hemoglobin-based oxygen carrier in normal male and female subjects
    • Hughes G.S., Francom S.F., Antal E.J., et al. Hematologic effects of a novel hemoglobin-based oxygen carrier in normal male and female subjects. J Lab Clin Med 126 (1995) 444-451
    • (1995) J Lab Clin Med , vol.126 , pp. 444-451
    • Hughes, G.S.1    Francom, S.F.2    Antal, E.J.3
  • 60
    • 0033864326 scopus 로고    scopus 로고
    • A phase I study of oxidized raffinose cross-linked human hemoglobin
    • Carmichael F.J., Ali A.C., Campbell J.A., et al. A phase I study of oxidized raffinose cross-linked human hemoglobin. Crit Care Med 28 (2000) 2283-2292
    • (2000) Crit Care Med , vol.28 , pp. 2283-2292
    • Carmichael, F.J.1    Ali, A.C.2    Campbell, J.A.3
  • 61
    • 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., et al. 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
  • 62
    • 0032869183 scopus 로고    scopus 로고
    • Modified hemoglobins produce venular interendothelial gaps and albumin leakage in the rat mesentery
    • Baldwin A.L. Modified hemoglobins produce venular interendothelial gaps and albumin leakage in the rat mesentery. Am J Phys 277 (1999) H650-H659
    • (1999) Am J Phys , vol.277
    • Baldwin, A.L.1
  • 63
    • 7044237149 scopus 로고    scopus 로고
    • Quantitative assessment of hemoglobin-induced endothelial barrier dysfunction
    • Dull R.O., DeWitt B.J., Dinavahi R., et al. Quantitative assessment of hemoglobin-induced endothelial barrier dysfunction. J Appl Phys 97 (2004) 1930-1937
    • (2004) J Appl Phys , vol.97 , pp. 1930-1937
    • Dull, R.O.1    DeWitt, B.J.2    Dinavahi, R.3
  • 65
    • 0031822162 scopus 로고    scopus 로고
    • Ultrastructural effects of intravascularly injected polyethylene glycol-hemoglobin in intestinal mucosa
    • Baldwin A.L., Wilson L.M., and Valeski J.E. Ultrastructural effects of intravascularly injected polyethylene glycol-hemoglobin in intestinal mucosa. Am J Physiol Heart Circ Physiol 275 (1998) H615-H625
    • (1998) Am J Physiol Heart Circ Physiol , vol.275
    • Baldwin, A.L.1    Wilson, L.M.2    Valeski, J.E.3
  • 66
    • 33746814411 scopus 로고    scopus 로고
    • Effects of S-nitrosation on hemoglobin-induced microvascular damage
    • Burke T.K., Teng X., Patel R.P., et al. Effects of S-nitrosation on hemoglobin-induced microvascular damage. Antioxid Redox Signal 8 (2006) 1093-1101
    • (2006) Antioxid Redox Signal , vol.8 , pp. 1093-1101
    • Burke, T.K.1    Teng, X.2    Patel, R.P.3
  • 67
    • 60549095846 scopus 로고    scopus 로고
    • Decreased damage from transient focal cerebral ischemia by transfusion of zero-link hemoglobin polymers in mouse
    • Mito T., Nemoto M., Kwansa H., et al. Decreased damage from transient focal cerebral ischemia by transfusion of zero-link hemoglobin polymers in mouse. Stroke 40 (2009) 278-284
    • (2009) Stroke , vol.40 , pp. 278-284
    • Mito, T.1    Nemoto, M.2    Kwansa, H.3
  • 68
    • 0030205132 scopus 로고    scopus 로고
    • Production and characteristics of an infusible oxygen-carrying fluid based on hemoglobin intramolecularly cross-linked with sebacic acid
    • Bucci E., Razynska A., Kwansa H., et al. Production and characteristics of an infusible oxygen-carrying fluid based on hemoglobin intramolecularly cross-linked with sebacic acid. J Lab Clin Med 128 (1996) 146-153
    • (1996) J Lab Clin Med , vol.128 , pp. 146-153
    • Bucci, E.1    Razynska, A.2    Kwansa, H.3
  • 69
    • 0030851588 scopus 로고    scopus 로고
    • Effects of the allosteric modification of hemoglobin on brain oxygen and infarct size in a feline model of stroke
    • Watson J.C., Doppenberg E.M.R., Bullock M.R., et al. Effects of the allosteric modification of hemoglobin on brain oxygen and infarct size in a feline model of stroke. Stroke 28 (1997) 1624-1630
    • (1997) Stroke , vol.28 , pp. 1624-1630
    • Watson, J.C.1    Doppenberg, E.M.R.2    Bullock, M.R.3
  • 70
    • 0023462496 scopus 로고
    • High-level expression of sperm whale myoglobin in E coli
    • Springer B.A., and Sligar S.G. High-level expression of sperm whale myoglobin in E coli. Proc Natl Acad Sci USA 84 (1987) 8961-8965
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 8961-8965
    • Springer, B.A.1    Sligar, S.G.2
  • 71
    • 23844456246 scopus 로고    scopus 로고
    • Conjugation of multiple copies of polyethylene glycol to hemoglobin facilitated through thiolation: influence on hemoglobin structure and function
    • Manjula B.N., Tsai A.G., Intaglietta M., et al. Conjugation of multiple copies of polyethylene glycol to hemoglobin facilitated through thiolation: influence on hemoglobin structure and function. Protein J 24 (2005) 133-146
    • (2005) Protein J , vol.24 , pp. 133-146
    • Manjula, B.N.1    Tsai, A.G.2    Intaglietta, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.