메뉴 건너뛰기




Volumn 14, Issue 4, 2010, Pages 538-543

Red cell substitutes from hemoglobin-Do we start all over again?

Author keywords

[No Author keywords available]

Indexed keywords

BLOOD SUBSTITUTE; DEOXYHEMOGLOBIN; HEMOGLOBIN; HEMOGLOBIN DERIVATIVE; MACROGOL; NITRIC OXIDE; NITRITE; NITRITE REDUCTASE; OXYHEMOGLOBIN;

EID: 77955321374     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpa.2010.03.021     Document Type: Review
Times cited : (49)

References (73)
  • 1
    • 0020309256 scopus 로고
    • Crosslinked stroma-free polyhemoglobin as a potential blood substitute
    • Keipert P., Minkowitz J., Chang T.M.S. Crosslinked stroma-free polyhemoglobin as a potential blood substitute. Int J Artif Organs 1982, 5:383-385.
    • (1982) Int J Artif Organs , vol.5 , pp. 383-385
    • Keipert, P.1    Minkowitz, J.2    Chang, T.M.S.3
  • 2
    • 0009864722 scopus 로고
    • Appraisal of red cell substitutes: hemoglobin solution and perfluorochemical emulsions
    • Sehgal L.R., Gould S.A., Rosen A.L., Sehgal H.L., Moss G.S. Appraisal of red cell substitutes: hemoglobin solution and perfluorochemical emulsions. Lab Med 1983, 14:545-548.
    • (1983) Lab Med , vol.14 , pp. 545-548
    • Sehgal, L.R.1    Gould, S.A.2    Rosen, A.L.3    Sehgal, H.L.4    Moss, G.S.5
  • 4
    • 0033856049 scopus 로고    scopus 로고
    • Haemoglobin-based oxygen carriers
    • Vandegriff K.D. Haemoglobin-based oxygen carriers. Exp Opin Investig Drugs 2000, 9:1967-1984.
    • (2000) Exp Opin Investig Drugs , vol.9 , pp. 1967-1984
    • Vandegriff, K.D.1
  • 6
    • 0024310191 scopus 로고
    • Blood substitutes-current status
    • Winslow R.M. Blood substitutes-current status. Transfusion 1989, 29:753-754.
    • (1989) Transfusion , vol.29 , pp. 753-754
    • Winslow, R.M.1
  • 7
    • 0343852152 scopus 로고    scopus 로고
    • Blood substitutes
    • Winslow R.M. Blood substitutes. Adv Drug Del Rev 2000, 40:131-142.
    • (2000) Adv Drug Del Rev , vol.40 , pp. 131-142
    • Winslow, R.M.1
  • 9
    • 29144443581 scopus 로고    scopus 로고
    • What happened to blood substitutes?
    • Stowell C.P. What happened to blood substitutes?. Transfus Clin Biol 2005, 12:374-379.
    • (2005) Transfus Clin Biol , vol.12 , pp. 374-379
    • Stowell, C.P.1
  • 10
    • 0038571272 scopus 로고    scopus 로고
    • Nitric oxide (NO)-biogeneration, regulation, and relevence to human diseases
    • Bian K., Murad F. Nitric oxide (NO)-biogeneration, regulation, and relevence to human diseases. Front Biosci 2003, 8:D264-D278.
    • (2003) Front Biosci , vol.8
    • Bian, K.1    Murad, F.2
  • 11
    • 0034036715 scopus 로고    scopus 로고
    • A short history of nitroglycerine and nitric oxide in pharmacology and physiology
    • Marsh N., Marsh A. A short history of nitroglycerine and nitric oxide in pharmacology and physiology. Clin Exp Pharmacol Physiol 2000, 27:313-319.
    • (2000) Clin Exp Pharmacol Physiol , vol.27 , pp. 313-319
    • Marsh, N.1    Marsh, A.2
  • 12
    • 0029875840 scopus 로고    scopus 로고
    • S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control
    • Jia L., Bonaventura C., Bonaventura J., Stamler J.S. S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control. Nature 1996, 380:221-226.
    • (1996) Nature , vol.380 , pp. 221-226
    • Jia, L.1    Bonaventura, C.2    Bonaventura, J.3    Stamler, J.S.4
  • 14
    • 77955330589 scopus 로고
    • Etobickoke firm in hot race to produce artificial blood
    • September 29
    • Thompson A. Etobickoke firm in hot race to produce artificial blood. Toronto Star 1992, c1-c2. September 29.
    • (1992) Toronto Star
    • Thompson, A.1
  • 15
    • 77955317610 scopus 로고    scopus 로고
    • US Food and Drug Administration: Guidance for Industry: Criteria for Safety and Efficacy Evaluation of Oxygen Therapeutics as Red Blood Cell Substitutes. Washington, D.C.
    • US Food and Drug Administration: Guidance for Industry: Criteria for Safety and Efficacy Evaluation of Oxygen Therapeutics as Red Blood Cell Substitutes. Washington, D.C.; 2004:1-19.
    • (2004) , pp. 1-19
  • 16
    • 77955318114 scopus 로고    scopus 로고
    • FDA shoots down Northfield Labs blood substitute
    • April 30
    • Jaspen B. FDA shoots down Northfield Labs blood substitute. Chicago Tribune 2009, April 30.
    • (2009) Chicago Tribune
    • Jaspen, B.1
  • 17
    • 41149119147 scopus 로고    scopus 로고
    • Basic science focus on blood substitutes: a summary of the NHLBI division of blood diseases and resources working group workshop, March 1, 2006
    • Estep T., Bucci E., Farmer M., Greenburg G., Harrington J., Kim H.W., Klein H., Mitchell P., Nemo G., Olsen K., et al. Basic science focus on blood substitutes: a summary of the NHLBI division of blood diseases and resources working group workshop, March 1, 2006. Transfusion 2008, 48:776-782.
    • (2008) Transfusion , vol.48 , pp. 776-782
    • Estep, T.1    Bucci, E.2    Farmer, M.3    Greenburg, G.4    Harrington, J.5    Kim, H.W.6    Klein, H.7    Mitchell, P.8    Nemo, G.9    Olsen, K.10
  • 18
    • 62249214890 scopus 로고    scopus 로고
    • Modern cross-linking strategies for synthesizing acellular hemoglobin-based oxygen carriers
    • Harris D.R., Palmer A.F. Modern cross-linking strategies for synthesizing acellular hemoglobin-based oxygen carriers. Biotechnol Prog 2008, 24:1215-1225.
    • (2008) Biotechnol Prog , vol.24 , pp. 1215-1225
    • Harris, D.R.1    Palmer, A.F.2
  • 19
    • 3142666846 scopus 로고    scopus 로고
    • Oxygen-carrying blood substitutes: a microvascular perspective
    • Tsai A.G., Cabrales P., Intaglietta M. Oxygen-carrying blood substitutes: a microvascular perspective. Exp Opin Biol Ther 2004, 4:1147-1157.
    • (2004) Exp Opin Biol Ther , vol.4 , pp. 1147-1157
    • Tsai, A.G.1    Cabrales, P.2    Intaglietta, M.3
  • 20
    • 0025951322 scopus 로고
    • Hemoglobin tetramers stabilized by a single intramolecular cross-link
    • Benesch R.E., Kwong S. Hemoglobin tetramers stabilized by a single intramolecular cross-link. J Protein Chem 1991, 10:503-510.
    • (1991) J Protein Chem , vol.10 , pp. 503-510
    • Benesch, R.E.1    Kwong, S.2
  • 22
    • 0031568811 scopus 로고    scopus 로고
    • Structures of a hemoglobin-based blood substitute: insights into the function of allosteric proteins
    • Kroeger K.S., Kundrot C.E. Structures of a hemoglobin-based blood substitute: insights into the function of allosteric proteins. Structure 1997, 5:227-237.
    • (1997) Structure , vol.5 , pp. 227-237
    • Kroeger, K.S.1    Kundrot, C.E.2
  • 24
    • 0026539643 scopus 로고
    • Characteristics of artificial red cells. Hemoglobin encapsulated in poly-lipid vesicles
    • Satoh T., Kobayashi K., Sekiguchi S., Tsuchida E. Characteristics of artificial red cells. Hemoglobin encapsulated in poly-lipid vesicles. ASAIO J 1992, 38:M580-584.
    • (1992) ASAIO J , vol.38
    • Satoh, T.1    Kobayashi, K.2    Sekiguchi, S.3    Tsuchida, E.4
  • 26
    • 0028432586 scopus 로고
    • Diaspirin cross-linked hemoglobin: tissue distribution and long-term excretion after exchange transfusion
    • Keipert P.E., Gomez C.L., Gonzales A., MacDonald V.W., Hess J.R., Winslow R.M. Diaspirin cross-linked hemoglobin: tissue distribution and long-term excretion after exchange transfusion. J Lab Clin Med 1994, 123:701-711.
    • (1994) J Lab Clin Med , vol.123 , pp. 701-711
    • Keipert, P.E.1    Gomez, C.L.2    Gonzales, A.3    MacDonald, V.W.4    Hess, J.R.5    Winslow, R.M.6
  • 27
    • 0031239389 scopus 로고    scopus 로고
    • An improved blood substitute-in vivo evaluation of its renal effects
    • Simoni J., Simoni G., Hartsell A., Feola M. An improved blood substitute-in vivo evaluation of its renal effects. ASAIO J 1997, 43:M714-M725.
    • (1997) ASAIO J , vol.43
    • Simoni, J.1    Simoni, G.2    Hartsell, A.3    Feola, M.4
  • 28
    • 42449127111 scopus 로고    scopus 로고
    • Role of haptoglobin on the uptake of native and β-chain [trimesyl-(lys82)β(ys82)β] cross-linked human hemoglobins in isolated perfused rat livers
    • Wrighton S., Chow E.C.Y., Liu L., Ship N., Kluger, Pang K.S. Role of haptoglobin on the uptake of native and β-chain [trimesyl-(lys82)β(ys82)β] cross-linked human hemoglobins in isolated perfused rat livers. Drug Metab Disp 2008, 36:937-945.
    • (2008) Drug Metab Disp , vol.36 , pp. 937-945
    • Wrighton, S.1    Chow, E.C.Y.2    Liu, L.3    Ship, N.4    Kluger5    Pang, K.S.6
  • 29
    • 19644365269 scopus 로고    scopus 로고
    • Binding of acellular, native and cross-linked human hemoglobins to haptoglobin: enhanced distribution and clearance in the rat
    • Ship N.J., Toprak A., Lai R.P., Tseng E., Kluger R., Pang K.S. Binding of acellular, native and cross-linked human hemoglobins to haptoglobin: enhanced distribution and clearance in the rat. Am J Physiol Gastrointest Liv Physiol 2005, 288:G1301-G1309.
    • (2005) Am J Physiol Gastrointest Liv Physiol , vol.288
    • Ship, N.J.1    Toprak, A.2    Lai, R.P.3    Tseng, E.4    Kluger, R.5    Pang, K.S.6
  • 32
    • 0023428522 scopus 로고
    • HbXL99a: a hemoglobin derivaitve that is cross-linked between the a subunits is useful as a blood substitute
    • Snyder S.R., Welty E.V., Walder R.Y., Williams L.A., Walder J.A. HbXL99a: a hemoglobin derivaitve that is cross-linked between the a subunits is useful as a blood substitute. Proc Natl Acad Sci U S A 1987, 84:7280-7284.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 7280-7284
    • Snyder, S.R.1    Welty, E.V.2    Walder, R.Y.3    Williams, L.A.4    Walder, J.A.5
  • 33
    • 0001553768 scopus 로고
    • Dicarboxylic acid bis(methyl phosphates): anionic biomimetic cross-linking reagents
    • Kluger R., Grant A.S., Bearne S.L., Trachsel M.R. Dicarboxylic acid bis(methyl phosphates): anionic biomimetic cross-linking reagents. J Org Chem 1990, 55:2864-2868.
    • (1990) J Org Chem , vol.55 , pp. 2864-2868
    • Kluger, R.1    Grant, A.S.2    Bearne, S.L.3    Trachsel, M.R.4
  • 34
  • 36
    • 4043084061 scopus 로고    scopus 로고
    • Effect of glutaraldehyde concentration on the physical properties of polymerized hemoglobin-based oxygen carriers
    • Eike J.H., Palmer A.F. Effect of glutaraldehyde concentration on the physical properties of polymerized hemoglobin-based oxygen carriers. Biotechnol Prog 2004, 20:1225-1232.
    • (2004) Biotechnol Prog , vol.20 , pp. 1225-1232
    • Eike, J.H.1    Palmer, A.F.2
  • 37
    • 44249093233 scopus 로고    scopus 로고
    • Cell-free hemoglobin-based blood substitutes and risk of myocardial infarction and death: a meta-analysis
    • Natanson C., Kern S.J., Lurie P., Banks S.M., Wolfe S.M. Cell-free hemoglobin-based blood substitutes and risk of myocardial infarction and death: a meta-analysis. J Am Med Assoc 2008, 299:2304-2312.
    • (2008) J Am Med Assoc , vol.299 , pp. 2304-2312
    • Natanson, C.1    Kern, S.J.2    Lurie, P.3    Banks, S.M.4    Wolfe, S.M.5
  • 38
    • 0021240763 scopus 로고
    • Acylation of hemoglobin by aspirin-like diacyl esters
    • Massil S.E., Shi G.Y., Klotz I.M. Acylation of hemoglobin by aspirin-like diacyl esters. J Pharm Sci 1984, 73:1013-1014.
    • (1984) J Pharm Sci , vol.73 , pp. 1013-1014
    • Massil, S.E.1    Shi, G.Y.2    Klotz, I.M.3
  • 39
    • 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., Klotz I.M. Diaspirins that cross-link beta-chains of hemoglobin-bis-(3,5-dibromosalicyl) succinate and bis-(3,5-dibromosalicyl) fumarate. Biochemistry 1979, 18:4265-4270.
    • (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
  • 40
    • 0019798202 scopus 로고
    • Rational approaches to chemotherapy. Antisickling agents
    • Klotz I.M., Haney D.N., King L.C. Rational approaches to chemotherapy. Antisickling agents. Science (Washington D.C.) 1981, 213:724-731.
    • (1981) Science (Washington D.C.) , vol.213 , pp. 724-731
    • Klotz, I.M.1    Haney, D.N.2    King, L.C.3
  • 41
    • 0025984774 scopus 로고
    • Covalent inhibitors of the gelation of sickle cell hemoglobin and their effects on function
    • Manning J.M. Covalent inhibitors of the gelation of sickle cell hemoglobin and their effects on function. Adv Enzymol 1991, 64:55-91.
    • (1991) Adv Enzymol , vol.64 , pp. 55-91
    • Manning, J.M.1
  • 42
    • 0033972378 scopus 로고    scopus 로고
    • Mechanism of site-directed protein cross-linking. Protein-directed selectivity in reactions of hemoglobin with aryl trimesates
    • Kluger R., De Stefano V. Mechanism of site-directed protein cross-linking. Protein-directed selectivity in reactions of hemoglobin with aryl trimesates. J Org Chem 2000, 65:214-219.
    • (2000) J Org Chem , vol.65 , pp. 214-219
    • Kluger, R.1    De Stefano, V.2
  • 43
    • 0034530012 scopus 로고    scopus 로고
    • Acyl phosphate esters: charge-directed acylation and aritficial blood
    • Kluger R. Acyl phosphate esters: charge-directed acylation and aritficial blood. Synlett 2000, 12:1708-1720.
    • (2000) Synlett , vol.12 , pp. 1708-1720
    • Kluger, R.1
  • 44
    • 77955316761 scopus 로고
    • Site-directed modifiers of proteins-acyl phosphate monoesters and their bifunctional analogs
    • Grant A., Bearne S., Kluger R. Site-directed modifiers of proteins-acyl phosphate monoesters and their bifunctional analogs. Biochemistry 1988, 27:3098.
    • (1988) Biochemistry , vol.27 , pp. 3098
    • Grant, A.1    Bearne, S.2    Kluger, R.3
  • 45
    • 0029813464 scopus 로고    scopus 로고
    • Systematically cross-linked human hemoglobin: functional effects of 10Å spans between beta subunits at lysine-82
    • Kluger R., Shen L., Xiao H., Jones R.T. Systematically cross-linked human hemoglobin: functional effects of 10Å spans between beta subunits at lysine-82. J Am Chem Soc 1996, 118:8782-8786.
    • (1996) J Am Chem Soc , vol.118 , pp. 8782-8786
    • Kluger, R.1    Shen, L.2    Xiao, H.3    Jones, R.T.4
  • 46
    • 0029062547 scopus 로고
    • Allosteric transition intermediates modeled by cross-linked hemoglobins
    • Schumacher M.A., Dixon M.M., Kluger R., Jones R.T., Brennan R.G. Allosteric transition intermediates modeled by cross-linked hemoglobins. Nature 1995, 375:84-87.
    • (1995) Nature , vol.375 , pp. 84-87
    • Schumacher, M.A.1    Dixon, M.M.2    Kluger, R.3    Jones, R.T.4    Brennan, R.G.5
  • 47
    • 0034283494 scopus 로고    scopus 로고
    • Effect of alpha-alpha diaspirin crosslinked hemoglobin (DCLHb (TM)) on the potency of sodium nitroprusside and nitroglycerine to decrease blood pressure in rats: a dose-response study
    • Erhart S.M., Cole D.J., Patel P.M., Drummond J.C., Burhop K.E. Effect of alpha-alpha diaspirin crosslinked hemoglobin (DCLHb (TM)) on the potency of sodium nitroprusside and nitroglycerine to decrease blood pressure in rats: a dose-response study. Artif Cells Blood Subs Immob Biotechnol 2000, 28:385-396.
    • (2000) Artif Cells Blood Subs Immob Biotechnol , vol.28 , pp. 385-396
    • Erhart, S.M.1    Cole, D.J.2    Patel, P.M.3    Drummond, J.C.4    Burhop, K.E.5
  • 48
    • 0027668810 scopus 로고
    • A role for endothelin and nitric-oxide in the pressor-response to diaspirin cross-linked hemoglobin
    • Schultz S.C., Grady B., Cole F., Hamilton I., Burhop K., Malcolm D.S. A role for endothelin and nitric-oxide in the pressor-response to diaspirin cross-linked hemoglobin. J Lab Clin Med 1993, 122:301-308.
    • (1993) J Lab Clin Med , vol.122 , pp. 301-308
    • Schultz, S.C.1    Grady, B.2    Cole, F.3    Hamilton, I.4    Burhop, K.5    Malcolm, D.S.6
  • 52
    • 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 K.D., Malavalli A., Minn C., Jiang E., Lohman J., Young M.A., Samaja M., Winslow R.M. Oxidation and haem loss kinetics of poly(ethylene glycol)-conjugated haemoglobin (MP4): dissociation between in vitro and in vivo oxidation rates. Biochem J 2006, 399:463-471.
    • (2006) Biochem J , vol.399 , 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
  • 53
    • 52349106464 scopus 로고    scopus 로고
    • Microvascular experimental evidence on the relative significance of restoring oxygen carrying capacity vs. blood viscosity in shock resuscitation
    • Vazquez B.Y.S., Wettstein R., Cabrales P., Tsai A.G., Intaglietta M. Microvascular experimental evidence on the relative significance of restoring oxygen carrying capacity vs. blood viscosity in shock resuscitation. Biochim Biophys Acta Proteins Proteom 2008, 1784:1421-1427.
    • (2008) Biochim Biophys Acta Proteins Proteom , vol.1784 , pp. 1421-1427
    • Vazquez, B.Y.S.1    Wettstein, R.2    Cabrales, P.3    Tsai, A.G.4    Intaglietta, M.5
  • 54
    • 77955338707 scopus 로고    scopus 로고
    • Sangart, Inc., San Diego, CA; Available online at: .
    • Sangart, Inc., San Diego, CA; 2009. Available online at: http://www.sangart.com/products/mp4ox.htm.
    • (2009)
  • 55
    • 68049097267 scopus 로고    scopus 로고
    • Microcirculatory effects of changing blood hemoglobin oxygen affinity during hemorrhagic shock resuscitation in an experimental model
    • Villela N.R., Cabrales P., Tsai A.G., Intaglietta M. Microcirculatory effects of changing blood hemoglobin oxygen affinity during hemorrhagic shock resuscitation in an experimental model. Shock 2009, 31:645-652.
    • (2009) Shock , vol.31 , pp. 645-652
    • Villela, N.R.1    Cabrales, P.2    Tsai, A.G.3    Intaglietta, M.4
  • 56
    • 0031466768 scopus 로고    scopus 로고
    • Colloid osmotic properties of modified hemoglobins: chemically cross-linked versus polyethylene glycol surface-conjugated
    • Vandegriff K.D., McCarthy M., Rohlfs R.J., Winslow R.M. Colloid osmotic properties of modified hemoglobins: chemically cross-linked versus polyethylene glycol surface-conjugated. Biophys Chem 1997, 69:23-30.
    • (1997) Biophys Chem , vol.69 , pp. 23-30
    • Vandegriff, K.D.1    McCarthy, M.2    Rohlfs, R.J.3    Winslow, R.M.4
  • 58
    • 10444222044 scopus 로고
    • The action of nitrite on haemoglobin in the absence of oxygen
    • Brooks J. The action of nitrite on haemoglobin in the absence of oxygen. Proc Royal Soc Lond Ser B Biol Sci 1937, 123:368-382.
    • (1937) Proc Royal Soc Lond Ser B Biol Sci , vol.123 , pp. 368-382
    • Brooks, J.1
  • 63
    • 10444220188 scopus 로고    scopus 로고
    • The reaction between nitrite and hemoglobin: the role of nitrite in hemoglobin-mediated hypoxic vasodilation
    • Kim-Shapiro D.B., Gladwin M.T., Patel R.P., Hogg N. The reaction between nitrite and hemoglobin: the role of nitrite in hemoglobin-mediated hypoxic vasodilation. J Inorg Biochem 2005, 99:237-246.
    • (2005) J Inorg Biochem , vol.99 , pp. 237-246
    • Kim-Shapiro, D.B.1    Gladwin, M.T.2    Patel, R.P.3    Hogg, N.4
  • 64
    • 61849150615 scopus 로고    scopus 로고
    • The new chemical biology of nitrite reactions with hemoglobin: R-state catalysis, oxidative denitrosylation, and nitrite reductase/anhydrase
    • Gladwin M.T., Grubina R., Doyle M.P. The new chemical biology of nitrite reactions with hemoglobin: R-state catalysis, oxidative denitrosylation, and nitrite reductase/anhydrase. Acc Chem Res 2009, 42:157-167.
    • (2009) Acc Chem Res , vol.42 , pp. 157-167
    • Gladwin, M.T.1    Grubina, R.2    Doyle, M.P.3
  • 65
    • 53249134617 scopus 로고    scopus 로고
    • Polyethylene glycol conjugation enhances the nitrite reductase activity of native and cross-linked hemoglobin
    • Lui F.E., Dong P., Kluger R. Polyethylene glycol conjugation enhances the nitrite reductase activity of native and cross-linked hemoglobin. Biochemistry 2008, 47:10773-10780.
    • (2008) Biochemistry , vol.47 , pp. 10773-10780
    • Lui, F.E.1    Dong, P.2    Kluger, R.3
  • 66
    • 72449130852 scopus 로고    scopus 로고
    • Enhancing nitrite reductase activity of modified hemoglobin: bis-tetramers and their PEGylated derivatives
    • Lui F.E., Kluger R. Enhancing nitrite reductase activity of modified hemoglobin: bis-tetramers and their PEGylated derivatives. Biochemistry 2009, 48:11912-11919.
    • (2009) Biochemistry , vol.48 , pp. 11912-11919
    • Lui, F.E.1    Kluger, R.2
  • 67
    • 0043236018 scopus 로고    scopus 로고
    • Crosslinked bis-hemoglobins: connections and oxygen binding
    • Gourianov N., Kluger R. Crosslinked bis-hemoglobins: connections and oxygen binding. J Am Chem Soc 2003, 125:10885-10892.
    • (2003) J Am Chem Soc , vol.125 , pp. 10885-10892
    • Gourianov, N.1    Kluger, R.2
  • 68
    • 27744479440 scopus 로고    scopus 로고
    • Conjoined hemoglobins. Loss of cooperativity and protein-protein interactions
    • Gourianov N., Kluger R. Conjoined hemoglobins. Loss of cooperativity and protein-protein interactions. Biochemistry 2005, 44:14989-14999.
    • (2005) Biochemistry , vol.44 , pp. 14989-14999
    • Gourianov, N.1    Kluger, R.2
  • 69
    • 56749117870 scopus 로고    scopus 로고
    • Functional cross-linked hemoglobin bis-tetramers: geometry and cooperativity
    • Hu D.X., Kluger R. Functional cross-linked hemoglobin bis-tetramers: geometry and cooperativity. Biochemistry 2008, 47:12551-12561.
    • (2008) Biochemistry , vol.47 , pp. 12551-12561
    • Hu, D.X.1    Kluger, R.2
  • 71
    • 33847247338 scopus 로고    scopus 로고
    • Development of zero-link polymers of hemoglobin, which do not extravasate and do not induce pressure increases upon infusion
    • Bucci E., Kwansa H., Koehler R.C., Matheson B. Development of zero-link polymers of hemoglobin, which do not extravasate and do not induce pressure increases upon infusion. Artif Cells Blood Subs Biotechnol 2007, 35:11-18.
    • (2007) Artif Cells Blood Subs Biotechnol , vol.35 , pp. 11-18
    • Bucci, E.1    Kwansa, H.2    Koehler, R.C.3    Matheson, B.4
  • 72
    • 67649981402 scopus 로고    scopus 로고
    • High-level production of recombinant arenicola marina globin chains in Escherichia coli: a new generation of blood substitute
    • Harnois T., Rousselot M., Rogniaux H., Zal F. High-level production of recombinant arenicola marina globin chains in Escherichia coli: a new generation of blood substitute. Artif Cells Blood Subs Biotechnol 2009, 37:106-116.
    • (2009) Artif Cells Blood Subs Biotechnol , vol.37 , pp. 106-116
    • Harnois, T.1    Rousselot, M.2    Rogniaux, H.3    Zal, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.