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Volumn 40, Issue 3, 2000, Pages 153-169

Purification and chemical modifications of hemoglobin in developing hemoglobin based oxygen carriers

Author keywords

Blood substitutes; Cross linking; Hypertensive drug effects; Polymerization

Indexed keywords

BLOOD SUBSTITUTES; CHEMICAL MODIFICATION; CROSSLINKING; POLYMERIZATION; PURIFICATION; TOXICITY;

EID: 0343852148     PISSN: 0169409X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0169-409X(99)00047-2     Document Type: Article
Times cited : (59)

References (94)
  • 2
    • 0014160019 scopus 로고
    • Evaluation of a stroma-free hemoglobin solution for use as a plasma expander
    • Rabiner S.F., Helbert J.R., Lopas H., Friedman L.H. Evaluation of a stroma-free hemoglobin solution for use as a plasma expander. J. Exp. Med. 126:1967;1127-1142.
    • (1967) J. Exp. Med. , vol.126 , pp. 1127-1142
    • Rabiner, S.F.1    Helbert, J.R.2    Lopas, H.3    Friedman, L.H.4
  • 5
    • 0019765114 scopus 로고
    • Preparation of blood hemoglobins of vertebrates
    • Riggs A. Preparation of blood hemoglobins of vertebrates. Methods Enzymol. 76:1981;5-29.
    • (1981) Methods Enzymol. , vol.76 , pp. 5-29
    • Riggs, A.1
  • 8
    • 0014423708 scopus 로고
    • Studies on the heterogeneity of hemoglobin. 13. Chromatography of various human and animal hemoglobin types on DEAE-Sephadex
    • Dozy A.M., Kleihauer E.F., Huisman T.H. Studies on the heterogeneity of hemoglobin. 13. Chromatography of various human and animal hemoglobin types on DEAE-Sephadex. J. Chromatogr. 32:1968;723-727.
    • (1968) J. Chromatogr. , vol.32 , pp. 723-727
    • Dozy, A.M.1    Kleihauer, E.F.2    Huisman, T.H.3
  • 9
    • 0013788528 scopus 로고
    • Studies on the heterogeneity of hemoglobin. IX. The use of tris(hydroxymethyl)aminomethane-HCl buffers in the anion-exchange chromatography of hemoglobins
    • Huisman T.H., Dozy A.M. Studies on the heterogeneity of hemoglobin. IX. The use of tris(hydroxymethyl)aminomethane-HCl buffers in the anion-exchange chromatography of hemoglobins. J. Chromatogr. 19:1965;160-169.
    • (1965) J. Chromatogr. , vol.19 , pp. 160-169
    • Huisman, T.H.1    Dozy, A.M.2
  • 10
    • 0020626848 scopus 로고
    • Selective carboxymethylation of the alpha-amino groups of hemoglobin. Effect on functional properties
    • DiDonato A., Fantl W.J., Acharya A.S., Manning J.M. Selective carboxymethylation of the alpha-amino groups of hemoglobin. Effect on functional properties. J. Biol. Chem. 258:1983;11890-11895.
    • (1983) J. Biol. Chem. , vol.258 , pp. 11890-11895
    • Didonato, A.1    Fantl, W.J.2    Acharya, A.S.3    Manning, J.M.4
  • 11
    • 0028243265 scopus 로고
    • Pilot-scale preparation of hemoglobin solutions
    • Winslow R.M., Chapman K.W. Pilot-scale preparation of hemoglobin solutions. Methods Enzymol. 231:1994;3-16.
    • (1994) Methods Enzymol. , vol.231 , pp. 3-16
    • Winslow, R.M.1    Chapman, K.W.2
  • 12
    • 0015879567 scopus 로고
    • A convenient chromatographic method for the preparation of human hemoglobin
    • Williams R.C. Jr., Tsay K.Y. A convenient chromatographic method for the preparation of human hemoglobin. Anal. Biochem. 54:1973;137-145.
    • (1973) Anal. Biochem. , vol.54 , pp. 137-145
    • Williams R.C., Jr.1    Tsay, K.Y.2
  • 14
    • 0343668025 scopus 로고    scopus 로고
    • Pasteurizable, freeze-driable hemoglobin-based blood substitute, U.S. Pat. No. 4,857,636, 1989
    • J.C. Hsia, Pasteurizable, freeze-driable hemoglobin-based blood substitute, U.S. Pat. No. 4,857,636, 1989.
    • Hsia, J.C.1
  • 15
    • 0030205132 scopus 로고    scopus 로고
    • Production and characteristics of an infusible oxygen-carrying fluid based on hemoglobin intramolecularly cross-linked with sebacic acid [see comments]
    • Bucci E., Razynska A., Kwansa H., Matheson-Urbaitis B., O'Hearne M., Ulatowski J.A., Koehler R.C. Production and characteristics of an infusible oxygen-carrying fluid based on hemoglobin intramolecularly cross-linked with sebacic acid [see comments]. 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    Matheson-Urbaitis, B.4    O'Hearne, M.5    Ulatowski, J.A.6    Koehler, R.C.7
  • 17
    • 0021162143 scopus 로고
    • Solvent regulation of oxygen affinity in hemoglobin. Sensitivity of bovine hemoglobin to chloride ions
    • Fronticelli C., Bucci E., Orth C. Solvent regulation of oxygen affinity in hemoglobin. Sensitivity of bovine hemoglobin to chloride ions. J. Biol. Chem. 259:1984;10841-10844.
    • (1984) J. Biol. Chem. , vol.259 , pp. 10841-10844
    • Fronticelli, C.1    Bucci, E.2    Orth, C.3
  • 18
    • 0031856673 scopus 로고    scopus 로고
    • Rate of reaction with nitric oxide determines the hypertensive effect of cell-free hemoglobin [see comments]
    • Doherty D.H., Doyle M.P., Curry S.R., Vali R.J., Fattor T.J., Olson J.S., Lemon D.D. Rate of reaction with nitric oxide determines the hypertensive effect of cell-free hemoglobin [see comments]. 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    Vali, R.J.4    Fattor, T.J.5    Olson, J.S.6    Lemon, D.D.7
  • 20
    • 0027358190 scopus 로고
    • Production of human hemoglobin in transgenic swine: An approach to a blood substitute
    • O'Donnell J.K., Martin M.J., Logan J.S., Kumar R. Production of human hemoglobin in transgenic swine: an approach to a blood substitute. Cancer Detect. Prev. 17:1993;307-312.
    • (1993) Cancer Detect. Prev. , vol.17 , pp. 307-312
    • O'Donnell, J.K.1    Martin, M.J.2    Logan, J.S.3    Kumar, R.4
  • 21
    • 0023626651 scopus 로고
    • Hemoglobin-based blood substitutes: Characterization of five pyridoxal 5′-phosphate derivatives of hemoglobin
    • McGarrity M.J., Hsia J.C., Er S.S. Hemoglobin-based blood substitutes: characterization of five pyridoxal 5′-phosphate derivatives of hemoglobin. J. Chromatogr. 419:1987;37-50.
    • (1987) J. Chromatogr. , vol.419 , pp. 37-50
    • McGarrity, M.J.1    Hsia, J.C.2    Er, S.S.3
  • 22
    • 0031056208 scopus 로고    scopus 로고
    • The toxicities of native and modified hemoglobins
    • Everse J., Hsia N. The toxicities of native and modified hemoglobins. Free Radic. Biol. Med. 22:1997;1075-1099.
    • (1997) Free Radic. Biol. Med. , vol.22 , pp. 1075-1099
    • Everse, J.1    Hsia, N.2
  • 24
    • 0028797258 scopus 로고
    • Effects of intra- And intermolecular crosslinking on the free radical reactions of bovine hemoglobins
    • Alayash A.I. Effects of intra- and intermolecular crosslinking on the free radical reactions of bovine hemoglobins. Free Radic. Biol. Med. 18:1995;295-301.
    • (1995) Free Radic. Biol. Med. , vol.18 , pp. 295-301
    • Alayash, A.I.1
  • 26
    • 0028943361 scopus 로고
    • Effects of polymerization on the oxygen carrying and redox properties of diaspirin cross-linked hemoglobin
    • Rogers M.S., Alayash A.I., Cashon R.E., Ryan B.B. Effects of polymerization on the oxygen carrying and redox properties of diaspirin cross-linked hemoglobin. Biochim. Biophys. Acta. 27:1995;135-142.
    • (1995) Biochim. Biophys. Acta , vol.27 , pp. 135-142
    • Rogers, M.S.1    Alayash, A.I.2    Cashon, R.E.3    Ryan, B.B.4
  • 27
    • 0030896551 scopus 로고    scopus 로고
    • The globin-based free radical of ferryl hemoglobin is detected in normal human blood
    • Svistunenko D.A., Patel R.P., Voloshchenko S.V., Wilson M.T. The globin-based free radical of ferryl hemoglobin is detected in normal human blood. J. Biol. Chem. 272:1997;7114-7121.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7114-7121
    • Svistunenko, D.A.1    Patel, R.P.2    Voloshchenko, S.V.3    Wilson, M.T.4
  • 28
    • 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. 69:1997;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
  • 29
    • 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., 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
  • 30
    • 0029998050 scopus 로고    scopus 로고
    • Clinical development of human polymerized hemoglobin as a blood substitute
    • Gould S.A., Moss G.S. Clinical development of human polymerized hemoglobin as a blood substitute. World J. Surg. 20:1996;1200-1207.
    • (1996) World J. Surg. , vol.20 , pp. 1200-1207
    • Gould, S.A.1    Moss, G.S.2
  • 31
    • 0024237501 scopus 로고
    • Long-term observation following traumatic-hemorrhagic shock in the dog: A comparison of crystalloidal vs. colloidal fluids
    • Hein L.G., Albrecht M., Dworschak M., Frey L., Bruckner U.B. Long-term observation following traumatic-hemorrhagic shock in the dog: a comparison of crystalloidal vs. colloidal fluids. Circ. Shock. 26:1988;353-364.
    • (1988) Circ. Shock , vol.26 , pp. 353-364
    • Hein, L.G.1    Albrecht, M.2    Dworschak, M.3    Frey, L.4    Bruckner, U.B.5
  • 32
    • 0001560180 scopus 로고
    • Microcirculatory consequences of blood substitution with alpha-alpha-hemoglobin
    • R.M. Winslow, K.D. Vandegriff, & M. Intaglietta. Boston: Birkhäuser
    • Tsai A.G., Kerger H., Intaglietta M. Microcirculatory consequences of blood substitution with alpha-alpha-hemoglobin. Winslow R.M., Vandegriff K.D., Intaglietta M. Blood Substitutes: Physiological Basis of Efficacy. 1995;155-174 Birkhäuser, Boston.
    • (1995) Blood Substitutes: Physiological Basis of Efficacy , pp. 155-174
    • Tsai, A.G.1    Kerger, H.2    Intaglietta, M.3
  • 33
    • 0003397525 scopus 로고    scopus 로고
    • Advances in blood substitutes: Industrial opportunities and medical challenges
    • Birkhäuser, Boston, 336
    • R.M. Winslow, K.D. Vandegriff, M. Intaglietta, Advances in blood substitutes: industrial opportunities and medical challenges., Advances in blood substitutes; v. 3. Birkhäuser, Boston, 1997, pp. xiv, 336.
    • (1997) Advances in Blood Substitutes , vol.3
    • Winslow, R.M.1    Vandegriff, K.D.2    Intaglietta, M.3
  • 36
    • 0031239389 scopus 로고    scopus 로고
    • An improved blood substitute. In vivo evaluation of its renal effects
    • Simoni J., Feola M., Hartsell A., Simoni G. An improved blood substitute. In vivo evaluation of its renal effects. Asaio J. 43:1997;M714-M725.
    • (1997) Asaio J. , vol.43
    • Simoni, J.1    Feola, M.2    Hartsell, A.3    Simoni, G.4
  • 37
    • 0030298208 scopus 로고    scopus 로고
    • Mapping cross-linking sites in modified proteins with mass spectrometry: An application to cross-linked hemoglobins
    • Yang T., Horejsh D.R., Mahan K.J., Zaluzec E.J., Watson T.J., Gage D.A. Mapping cross-linking sites in modified proteins with mass spectrometry: an application to cross-linked hemoglobins. Anal. Biochem. 242:1996;55-63.
    • (1996) Anal. Biochem. , vol.242 , pp. 55-63
    • Yang, T.1    Horejsh, D.R.2    Mahan, K.J.3    Zaluzec, E.J.4    Watson, T.J.5    Gage, D.A.6
  • 38
    • 0023428522 scopus 로고
    • HbXL99 alpha: A hemoglobin derivative that is cross-linked between the alpha subunits is useful as a blood substitute
    • Snyder S.R., Welty E.V., Walder R.Y., Williams L.A., Walder J.A. HbXL99 alpha: a hemoglobin derivative that is cross-linked between the alpha subunits is useful as a blood substitute. Proc. Natl. Acad. Sci. USA. 84:1987;7280-7284.
    • (1987) Proc. Natl. Acad. Sci. USA , 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
  • 39
    • 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., 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
  • 42
    • 0029947557 scopus 로고    scopus 로고
    • Role of endothelin in the cardiovascular effects of diaspirin crosslinked and stroma reduced hemoglobin
    • Gulati A., Sharma A.C., Singh G. Role of endothelin in the cardiovascular effects of diaspirin crosslinked and stroma reduced hemoglobin. Crit. Care Med. 24:1996;137-147.
    • (1996) Crit. Care Med. , vol.24 , pp. 137-147
    • Gulati, A.1    Sharma, A.C.2    Singh, G.3
  • 43
    • 0029019041 scopus 로고
    • Yohimbine modulates diaspirin crosslinked hemoglobin-induced systemic hemodynamics and regional circulatory effects [see comments]
    • Sharma A.C., Gulati A. Yohimbine modulates diaspirin crosslinked hemoglobin-induced systemic hemodynamics and regional circulatory effects [see comments]. Crit. Care Med. 23:1995;874-884.
    • (1995) Crit. Care Med. , vol.23 , pp. 874-884
    • Sharma, A.C.1    Gulati, A.2
  • 44
    • 0028884356 scopus 로고
    • Role of NO mechanism in cardiovascular effects of diaspirin cross-linked hemoglobin in anesthetized rats
    • Sharma A.C., Singh G., Gulati A. Role of NO mechanism in cardiovascular effects of diaspirin cross-linked hemoglobin in anesthetized rats. Am. J. Physiol. 269:1995;H1379-H1388.
    • (1995) Am. J. Physiol. , vol.269
    • Sharma, A.C.1    Singh, G.2    Gulati, A.3
  • 45
    • 0028085536 scopus 로고
    • Diaspirin cross-linked hemoglobin (DCLHB): Involvement of adrenergic mechanisms in the pressor effect
    • Gulati A., Rebello S. Diaspirin cross-linked hemoglobin (DCLHB): involvement of adrenergic mechanisms in the pressor effect. Artif. Cells Blood Substit. Immobil. Biotechnol. 22:1994;603-612.
    • (1994) Artif. Cells Blood Substit. Immobil. Biotechnol. , vol.22 , pp. 603-612
    • Gulati, A.1    Rebello, S.2
  • 47
    • 0028364227 scopus 로고
    • Prazosin blocks the pressor but not the regional circulatory effects of diaspirin crosslinked hemoglobin
    • Gulati A., Sharma A.C. Prazosin blocks the pressor but not the regional circulatory effects of diaspirin crosslinked hemoglobin. Life Sci. 55:1994;121-130.
    • (1994) Life Sci. , vol.55 , pp. 121-130
    • Gulati, A.1    Sharma, A.C.2
  • 50
    • 0028027517 scopus 로고
    • The modification of hemoglobin by a long crosslinking reagent: Bis(3,5-dibromosalicyl) sebacate
    • Zhang Q., Olsen K.W. The modification of hemoglobin by a long crosslinking reagent: bis(3,5-dibromosalicyl) sebacate. Biochem. Biophys. Res. Commun. 203:1994;1463-1470.
    • (1994) Biochem. Biophys. Res. Commun. , vol.203 , pp. 1463-1470
    • Zhang, Q.1    Olsen, K.W.2
  • 51
    • 0028068393 scopus 로고
    • Thermal stabilities of hemoglobins crosslinked with different length reagents
    • Huang H., Olsen K.W. Thermal stabilities of hemoglobins crosslinked with different length reagents. Artif. Cells Blood Substit. Immobil. Biotechnol. 22:1994;719-724.
    • (1994) Artif. Cells Blood Substit. Immobil. Biotechnol. , vol.22 , pp. 719-724
    • Huang, H.1    Olsen, K.W.2
  • 52
    • 0026671059 scopus 로고
    • Carbodiimide-mediated coupling of benzenepentacarboxylate to human hemoglobin: Structural and functional consequences
    • Brouwer M., Cashon R., Bonaventura J. Carbodiimide-mediated coupling of benzenepentacarboxylate to human hemoglobin: structural and functional consequences. Biomater. Artif. Cells Immobil. Biotechnol. 20:1992;323-326.
    • (1992) Biomater. Artif. Cells Immobil. Biotechnol. , vol.20 , pp. 323-326
    • Brouwer, M.1    Cashon, R.2    Bonaventura, J.3
  • 53
    • 0026728057 scopus 로고
    • A potential blood substitute from carboxylic dextran and oxyhemoglobin. II. Physicochemical and physiological assessments. Preliminary results on guinea pig
    • Faivre B., Menu P., Labrude P., Grandgeorge M., Vigneron C., Dellacherie E. A potential blood substitute from carboxylic dextran and oxyhemoglobin. II. Physicochemical and physiological assessments. Preliminary results on guinea pig. Biomater. Artif. Cells Immobil. Biotechnol. 20:1992;597-600.
    • (1992) Biomater. Artif. Cells Immobil. Biotechnol. , vol.20 , pp. 597-600
    • Faivre, B.1    Menu, P.2    Labrude, P.3    Grandgeorge, M.4    Vigneron, C.5    Dellacherie, E.6
  • 55
    • 0027338983 scopus 로고
    • Low oxygen affinity derivatives of human hemoglobin by fixation of polycarboxylic dextran to the oxyform
    • Prouchayret F., 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
  • 57
    • 0018251642 scopus 로고
    • Characterization of the pyridoxal phosphate site in glycogen phosphorylase b from rabbit muscle
    • Shimomura S., Fukui T. Characterization of the pyridoxal phosphate site in glycogen phosphorylase b from rabbit muscle. Biochemistry. 17:1978;5359-5367.
    • (1978) Biochemistry , vol.17 , pp. 5359-5367
    • Shimomura, S.1    Fukui, T.2
  • 58
    • 0024341178 scopus 로고
    • Functional properties of a new crosslinked hemoglobin designed for use as a red cell substitute [see comments]
    • Keipert P.E., Adeniran A.J., Kwong S., Benesch R.E. Functional properties of a new crosslinked hemoglobin designed for use as a red cell substitute [see comments]. Transfusion. 29:1989;768-773.
    • (1989) Transfusion , vol.29 , pp. 768-773
    • Keipert, P.E.1    Adeniran, A.J.2    Kwong, S.3    Benesch, R.E.4
  • 59
    • 0015923368 scopus 로고
    • Synthesis of 2-nor-2-formylpyridoxal 5′-phosphate, a bifunctional reagent specific for the cofactor site in proteins
    • Pocker A. Synthesis of 2-nor-2-formylpyridoxal 5′-phosphate, a bifunctional reagent specific for the cofactor site in proteins. J. Org. Chem. 38:1973;4295-4299.
    • (1973) J. Org. Chem. , vol.38 , pp. 4295-4299
    • Pocker, A.1
  • 61
    • 46149128444 scopus 로고
    • Prolonged vascular retention of a hemoglobin solution modified by cross-linking with 2-nor-2-formylpyridoxal 5′-phosphate
    • Bleeker W.K., van der Plas J., Agterberg J., Rigter G., Bakker J.C. Prolonged vascular retention of a hemoglobin solution modified by cross-linking with 2-nor-2-formylpyridoxal 5′-phosphate. J. Lab. Clin. Med. 108:1986;448-455.
    • (1986) J. Lab. Clin. Med. , vol.108 , pp. 448-455
    • Bleeker, W.K.1    Van Der Plas, J.2    Agterberg, J.3    Rigter, G.4    Bakker, J.C.5
  • 63
    • 0027251288 scopus 로고
    • Systemic and pulmonary hypertension after resuscitation with cell-free hemoglobin
    • Hess J.R., MacDonald V.W., Brinkley W.W. Systemic and pulmonary hypertension after resuscitation with cell-free hemoglobin. J. Appl. Physiol. 74:1993;1769-1778.
    • (1993) J. Appl. Physiol. , vol.74 , pp. 1769-1778
    • Hess, J.R.1    MacDonald, V.W.2    Brinkley, W.W.3
  • 64
    • 0027327542 scopus 로고
    • Acute changes in systemic blood pressure and urine output of conscious rats following exchange transfusion with diaspirin-crosslinked hemoglobin solution
    • Keipert P.E., Gonzales A., Gomez C.L., MacDonald V.W., Hess J.R., Winslow R.M. Acute changes in systemic blood pressure and urine output of conscious rats following exchange transfusion with diaspirin-crosslinked hemoglobin solution. Transfusion. 33:1993;701-708.
    • (1993) Transfusion , vol.33 , pp. 701-708
    • Keipert, P.E.1    Gonzales, A.2    Gomez, C.L.3    MacDonald, V.W.4    Hess, J.R.5    Winslow, R.M.6
  • 65
    • 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. 123:1994;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
  • 66
    • 0031858604 scopus 로고    scopus 로고
    • The first randomized trial of human polymerized hemoglobin as a blood substitute in acute trauma and emergent surgery [see comments]
    • Gould S.A., Moore E.E., Hoyt D.B., Burch J.M., Haenel J.B., Garcia J., DeWoskin R., Moss G.S. The first randomized trial of human polymerized hemoglobin as a blood substitute in acute trauma and emergent surgery [see comments]. 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    Burch, J.M.4    Haenel, J.B.5    Garcia, J.6    Dewoskin, R.7    Moss, G.S.8
  • 69
    • 0022349758 scopus 로고
    • Characterization of a modified, stroma-free hemoglobin solution as an oxygen-carrying plasma substitute
    • Kothe N., Eichentopf B., Bonhard K. Characterization of a modified, stroma-free hemoglobin solution as an oxygen-carrying plasma substitute. Surg. Gynecol. Obstet. 161:1985;563-569.
    • (1985) Surg. Gynecol. Obstet. , vol.161 , pp. 563-569
    • Kothe, N.1    Eichentopf, B.2    Bonhard, K.3
  • 71
    • 0007763432 scopus 로고    scopus 로고
    • Hemorrhagic disorders after administration of glutaraldehyde-polymerized hemoglobin
    • R.M. Winslow, K.D. Vandegriff, & M. Intaglietta. Boston: Birkhäuser
    • Bleeker W.K., Berbers G.A., den Boer P.J., Agterberg J., Rigter G., Bakker J.C. Hemorrhagic disorders after administration of glutaraldehyde-polymerized hemoglobin. Winslow R.M., Vandegriff K.D., Intaglietta M. Blood Substitutes: New Challenges. 1996;112 Birkhäuser, Boston.
    • (1996) Blood Substitutes: New Challenges , pp. 112
    • Bleeker, W.K.1    Berbers, G.A.2    Den Boer, P.J.3    Agterberg, J.4    Rigter, G.5    Bakker, J.C.6
  • 72
    • 0029131674 scopus 로고
    • Limitations of the efficacy of hemoglobin-based oxygen-carrying solutions
    • Lee R., Vlahakes G.J., Svizzero T.A., Neya K. Limitations of the efficacy of hemoglobin-based oxygen-carrying solutions. J. Appl. Physiol. 79:1995;236-242.
    • (1995) J. Appl. Physiol. , vol.79 , pp. 236-242
    • Lee, R.1    Vlahakes, G.J.2    Svizzero, T.A.3    Neya, K.4
  • 73
    • 0343668008 scopus 로고    scopus 로고
    • Selective crosslinking of hemoglobin by oxidized, ring-opened saccharides, U.S. Pat. No. 5,532,352, 1996
    • D. Pliura, L.T. Wong, S.S. Er, Selective crosslinking of hemoglobin by oxidized, ring-opened saccharides, U.S. Pat. No. 5,532,352, 1996.
    • Pliura, D.1    Wong, L.T.2    Er, S.S.3
  • 74
    • 0030871422 scopus 로고    scopus 로고
    • The impact of polyethylene glycol conjugation on bovine hemoglobin's circulatory half-life and renal effects in a rabbit top-loaded transfusion model
    • Conover C.D., Gilbert C.W., Shum K.L., Shorr R.G. The impact of polyethylene glycol conjugation on bovine hemoglobin's circulatory half-life and renal effects in a rabbit top-loaded transfusion model. Artif. Organs. 21:1997;907-915.
    • (1997) Artif. Organs , vol.21 , pp. 907-915
    • Conover, C.D.1    Gilbert, C.W.2    Shum, K.L.3    Shorr, R.G.4
  • 76
    • 0031806430 scopus 로고    scopus 로고
    • Increased tissue oxygenation and enhanced radiation sensitivity of solid tumors in rodents following polyethylene glycol conjugated bovine hemoglobin administration
    • Linberg R., Conover C.D., Shum K.L., Shorr R.G. Increased tissue oxygenation and enhanced radiation sensitivity of solid tumors in rodents following polyethylene glycol conjugated bovine hemoglobin administration. In Vivo. 12:1998;167-173.
    • (1998) In Vivo , vol.12 , pp. 167-173
    • Linberg, R.1    Conover, C.D.2    Shum, K.L.3    Shorr, R.G.4
  • 77
    • 0342797714 scopus 로고    scopus 로고
    • Compositions and methods utilizing nitroxides to avoid oxygen toxicity, particularly in stabilized, polymerized, conjugated, or encapsulated hemoglobin used as a red cell substitute, U.S. Pat. No. 5,591,710, 1997
    • J.C. Hsia, Compositions and methods utilizing nitroxides to avoid oxygen toxicity, particularly in stabilized, polymerized, conjugated, or encapsulated hemoglobin used as a red cell substitute, U.S. Pat. No. 5,591,710, 1997.
    • Hsia, J.C.1
  • 78
    • 0027429840 scopus 로고
    • Cross-linked hemoglobin-superoxide dismutase-catalase scavenges oxygen-derived free radicals and prevents methemoglobin formation and iron release
    • D'Agnillo F., Chang T.M. Cross-linked hemoglobin-superoxide dismutase-catalase scavenges oxygen-derived free radicals and prevents methemoglobin formation and iron release. Biomater. Artif. Cells Immobil. Biotechnol. 21:1993;609-621.
    • (1993) Biomater. Artif. Cells Immobil. Biotechnol. , vol.21 , pp. 609-621
    • D'Agnillo, F.1    Chang, T.M.2
  • 79
    • 0033593343 scopus 로고    scopus 로고
    • Glutaraldehyde modification of recombinant human hemoglobin alters its hemodynamic properties
    • Doyle M.P., Apostol I., Kerwin B.A. Glutaraldehyde modification of recombinant human hemoglobin alters its hemodynamic properties. J. Biol. Chem. 274:1999;2583-2591.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2583-2591
    • Doyle, M.P.1    Apostol, I.2    Kerwin, B.A.3
  • 80
    • 0342362828 scopus 로고    scopus 로고
    • Characterization of a 260 kDa Tetrahemoglobin obtained by Chemical Crosslinking of a Cysteine-Containing Dihemoglobin. VII International Symposium on Blood Substitutes. Montreal, Quebec, Canada, 1997
    • Marquardt D.A., Epp J.K., Vincelette J., Suniga M., Dotle M.P., Anthony-Cahill S.J. Characterization of a 260 kDa Tetrahemoglobin obtained by Chemical Crosslinking of a Cysteine-Containing Dihemoglobin. VII International Symposium on Blood Substitutes. Montreal, Quebec, Canada, 1997. Abstracts. 1:1997;1-144.
    • (1997) Abstracts , vol.1 , pp. 1-144
    • Marquardt, D.A.1    Epp, J.K.2    Vincelette, J.3    Suniga, M.4    Dotle, M.P.5    Anthony-Cahill, S.J.6
  • 81
    • 0343668004 scopus 로고    scopus 로고
    • Design of new recombinant hemoglobins for oxygen carrying therapeutics
    • D.D. Lemon, Design of new recombinant hemoglobins for oxygen carrying therapeutics. ASAIO 45th Anniversary Meeting, 1999.
    • (1999) ASAIO 45th Anniversary Meeting
    • Lemon, D.D.1
  • 82
    • 0030708923 scopus 로고    scopus 로고
    • Recent advances in development of haemoglobin-based blood substitutes
    • Gulati A. Recent advances in development of haemoglobin-based blood substitutes. Expert Opin. Invest. Drugs. 6:1997;1659-1669.
    • (1997) Expert Opin. Invest. Drugs , vol.6 , pp. 1659-1669
    • Gulati, A.1
  • 86
    • 0030747017 scopus 로고    scopus 로고
    • Effect of polyethylene glycol conjugated bovine hemoglobin in both top-load and exchange transfusion rat models
    • Conover C.D., Shorr R.G., Shum K.L., Gilbert C.W., Linberg R. Effect of polyethylene glycol conjugated bovine hemoglobin in both top-load and exchange transfusion rat models. Artif. Organs. 21:1997;1066-1075.
    • (1997) Artif. Organs , vol.21 , pp. 1066-1075
    • Conover, C.D.1    Shorr, R.G.2    Shum, K.L.3    Gilbert, C.W.4    Linberg, R.5
  • 87
    • 0020622177 scopus 로고
    • Preparation and in vitro characteristics of polymerized pyridoxylated hemoglobin
    • Sehgal L.R., Rosen A.L., Gould S.A., Sehgal H.L., Moss G.S. Preparation and in vitro characteristics of polymerized pyridoxylated hemoglobin. Transfusion. 23:1983;158-162.
    • (1983) Transfusion , vol.23 , pp. 158-162
    • Sehgal, L.R.1    Rosen, A.L.2    Gould, S.A.3    Sehgal, H.L.4    Moss, G.S.5
  • 88
    • 0024360927 scopus 로고
    • Plasma retention and metabolic fate of hemoglobin modified with an interdimeric covalent cross link
    • Keipert P.E., Verosky M., Triner L. Plasma retention and metabolic fate of hemoglobin modified with an interdimeric covalent cross link. ASAIO Trans. 35:1989;153-159.
    • (1989) ASAIO Trans. , vol.35 , pp. 153-159
    • Keipert, P.E.1    Verosky, M.2    Triner, L.3
  • 94
    • 0026345858 scopus 로고
    • Physico-chemical and pharmacological comparison of pyridoxylated hemoglobin bound to polyoxyethylene or polymerized by glutaraldehyde
    • Menu P., Mouelle P., Clerc Y., Labrude P., Vigneron C. Physico-chemical and pharmacological comparison of pyridoxylated hemoglobin bound to polyoxyethylene or polymerized by glutaraldehyde. Int. J. Artif. Organs. 14:1991;805-809.
    • (1991) Int. J. Artif. Organs , vol.14 , pp. 805-809
    • Menu, P.1    Mouelle, P.2    Clerc, Y.3    Labrude, P.4    Vigneron, C.5


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