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Volumn 25, Issue 1, 2009, Pages 189-199

Tangential flow filtration of hemoglobin

Author keywords

Blood substiutute; Hemoglobin; Oxygen carrier; Purification; Tangential flow filtration

Indexed keywords

EQUILIBRIUM CURVES; GLOBIN CHAINS; HOLLOW FIBERS; HUMAN RED BLOOD CELLS; IMPURITY BANDS; IMPURITY PEAKS; MOLECULAR IONS; OXYGEN AFFINITIES; OXYGEN CARRIER; RETENTATE; SDS PAGES; SIMPLE METHODS; TANGENTIAL FLOW FILTRATION;

EID: 64549100352     PISSN: 87567938     EISSN: None     Source Type: Journal    
DOI: 10.1002/btpr.119     Document Type: Article
Times cited : (75)

References (49)
  • 3
    • 4644302054 scopus 로고    scopus 로고
    • Do transfusions get to the heart of the matter?
    • Hebert PC, Fergusson DA. Do transfusions get to the heart of the matter? J Am Med Assoc A. 2004;292:1610-1612.
    • (2004) J Am Med Assoc A , vol.292 , pp. 1610-1612
    • Hebert, P.C.1    Fergusson, D.A.2
  • 4
    • 3242701589 scopus 로고    scopus 로고
    • Is there a place for epoetin alfa in managing anemia during critical illness?
    • Givens M, Lapointe M. Is there a place for epoetin alfa in managing anemia during critical illness? Clin Ther. 2004;26:819-829.
    • (2004) Clin Ther , vol.26 , pp. 819-829
    • Givens, M.1    Lapointe, M.2
  • 5
    • 0347517730 scopus 로고    scopus 로고
    • Surgery without blood
    • Shander A. Surgery without blood. Crit Care Med. 2003;31: S708-S714.
    • (2003) Crit Care Med , vol.31
    • Shander, A.1
  • 8
    • 2942722660 scopus 로고    scopus 로고
    • Oxidized mono-, di-, tri-, and polysaccha- rides as potential hemoglobin crosslinking reagents for the synthesis of high oxygen affinity artificial blood substitutes
    • Eike JH, Palmer AF. Oxidized mono-, di-, tri-, and polysaccha- rides as potential hemoglobin crosslinking reagents for the synthesis of high oxygen affinity artificial blood substitutes. Biotechnol Prog. 2004;20:953-962.
    • (2004) Biotechnol Prog , vol.20 , pp. 953-962
    • Eike, J.H.1    Palmer, A.F.2
  • 10
    • 11144330501 scopus 로고    scopus 로고
    • Liposome-encapsulated actin hemoglobin (LEAcHb) artificial blood substitutes
    • Li S, Nickels J, Palmer AF. Liposome-encapsulated actin hemoglobin (LEAcHb) artificial blood substitutes. Biomaterials.2005; 26:3759-3769.
    • (2005) Biomaterials , vol.26 , pp. 3759-3769
    • Li, S.1    Nickels, J.2    Palmer, A.F.3
  • 11
    • 21644460121 scopus 로고    scopus 로고
    • A novel tetrafunc- tional reagent for simultaneous intramolecular and intermolecu- lar cross-linking of bovine hemoglobin
    • Yun Q, He M, Xing W, Bi J, Ma G, Su Z. A novel tetrafunc- tional reagent for simultaneous intramolecular and intermolecu- lar cross-linking of bovine hemoglobin. Biotechnol Lett. 2004; 26:1359-1363.
    • (2004) Biotechnol Lett , vol.26 , pp. 1359-1363
    • Yun, Q.1    He, M.2    Xing, W.3    Bi, J.4    Ma, G.5    Su, Z.6
  • 12
    • 2942700266 scopus 로고    scopus 로고
    • 4 concentration and reaction time on physical properties of glutaraldehyde-polymerized hemoglobin
    • 4 concentration and reaction time on physical properties of glutaraldehyde-polymerized hemoglobin. Biotechnol Prog. 2004;20:946-952.
    • (2004) Biotechnol Prog , vol.20 , pp. 946-952
    • Eike, J.H.1    Palmer, A.F.2
  • 13
    • 4043084061 scopus 로고    scopus 로고
    • Effect of glutaraldehyde concentration on the physical properties of polymerized hemoglobin-based oxygen carriers
    • Eike JH, Palmer AF. 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
  • 14
    • 5444226407 scopus 로고    scopus 로고
    • + on the oxygen binding properties of glutaraldehyde-polymerized bovine hemoglo- binbased blood substitutes. Biotechnol Prog. 2004;20:1543-1549.
    • + on the oxygen binding properties of glutaraldehyde-polymerized bovine hemoglo- binbased blood substitutes. Biotechnol Prog. 2004;20:1543-1549.
  • 15
    • 34249794235 scopus 로고    scopus 로고
    • 2 affinity hemoglobin-based oxygen carriers synthesized via polymerization of hemoglobin with ring-opened 2-chloroethyl-β-D-fructopyranoside and 1-o-octyl-β-D- glucopyranoside
    • 2 affinity hemoglobin-based oxygen carriers synthesized via polymerization of hemoglobin with ring-opened 2-chloroethyl-β-D-fructopyranoside and 1-o-octyl-β-D- glucopyranoside. Biotechnol. Bioeng 2007;97:462-472.
    • (2007) Biotechnol. Bioeng , vol.97 , pp. 462-472
    • Dimino, M.L.1    Palmer, A.F.2
  • 16
    • 33749234394 scopus 로고    scopus 로고
    • Extension arm facilitated PEGylation of hemoglobin: Correlation of the properties with the extent of PEGylation
    • Li D, Manjula BN, Acharya AS. Extension arm facilitated PEGylation of hemoglobin: correlation of the properties with the extent of PEGylation. Protein J. 2006;25:263-274.
    • (2006) Protein J , vol.25 , pp. 263-274
    • Li, D.1    Manjula, B.N.2    Acharya, A.S.3
  • 17
    • 33644899373 scopus 로고    scopus 로고
    • Physical properties of hemoglobin-poly (acrylamide) hydrogel-based oxygen carriers: Effect of reaction pH
    • Patton JN, Palmer AF. Physical properties of hemoglobin-poly (acrylamide) hydrogel-based oxygen carriers: effect of reaction pH. Langmuir. 2006;22:2212-2221.
    • (2006) Langmuir , vol.22 , pp. 2212-2221
    • Patton, J.N.1    Palmer, A.F.2
  • 18
    • 22944461112 scopus 로고    scopus 로고
    • Engineering temperature-sensitive hydro- gel nanoparticles entrapping hemoglobin as a novel type of oxygen carrier
    • Patton JN, Palmer AF. Engineering temperature-sensitive hydro- gel nanoparticles entrapping hemoglobin as a novel type of oxygen carrier. Biomacromolecules. 2005;6:2204-2212.
    • (2005) Biomacromolecules , vol.6 , pp. 2204-2212
    • Patton, J.N.1    Palmer, A.F.2
  • 19
    • 0347413685 scopus 로고    scopus 로고
    • Determination of size distribution and encapsulation efficiency of liposome-encapsulated hemoglobin blood substitutes using asymmetric flow field-flow fractionation coupled with multi-angle static light scattering
    • Arifin DR, Palmer AF. Determination of size distribution and encapsulation efficiency of liposome-encapsulated hemoglobin blood substitutes using asymmetric flow field-flow fractionation coupled with multi-angle static light scattering. Biotechnol Prog. 2003;19:1798-1811.
    • (2003) Biotechnol Prog , vol.19 , pp. 1798-1811
    • Arifin, D.R.1    Palmer, A.F.2
  • 21
    • 22944465780 scopus 로고    scopus 로고
    • Polymersome encapsulated hemoglobin: A novel type of oxygen carrier
    • Arifin DR, Palmer AF. Polymersome encapsulated hemoglobin: a novel type of oxygen carrier. Biomacromolecules. 2005;6: 2172-2181.
    • (2005) Biomacromolecules , vol.6 , pp. 2172-2181
    • Arifin, D.R.1    Palmer, A.F.2
  • 22
    • 20044381699 scopus 로고    scopus 로고
    • Physical properties and stability mechanisms of poly(ethylene glycol) conjugated liposome encapsulated hemoglobin dispersions
    • Arifin DR, Palmer AF. Physical properties and stability mechanisms of poly(ethylene glycol) conjugated liposome encapsulated hemoglobin dispersions. Artif Cells Blood Substit Biotechnol Bioeng. 2005;33:137-162.
    • (2005) Artif Cells Blood Substit Biotechnol Bioeng , vol.33 , pp. 137-162
    • Arifin, D.R.1    Palmer, A.F.2
  • 23
    • 0010263999 scopus 로고
    • Hemoglobin purification
    • US Pat 5,407,579
    • Lee CJ, Kan P. Hemoglobin purification. US Pat 5,407,579 (1993).
    • (1993)
    • Lee, C.J.1    Kan, P.2
  • 24
    • 65349189419 scopus 로고    scopus 로고
    • Purification of red blood cells by separation and diafiltration
    • US Pat 7,001,715
    • Houtchens RA, Gawryl MS, Light WR, Baqai J. Purification of red blood cells by separation and diafiltration. US Pat 7,001,715 (2003).
    • (2003)
    • Houtchens, R.A.1    Gawryl, M.S.2    Light, W.R.3    Baqai, J.4
  • 25
    • 4544361769 scopus 로고    scopus 로고
    • Purification and characterization of human hemoglobin: Effect of the hemo-lysis conditions
    • Andrade CT, Barros LAM, Lima MCP, Azero EG. Purification and characterization of human hemoglobin: effect of the hemo-lysis conditions. Int J Biol Macromol. 2004;34:233-240.
    • (2004) Int J Biol Macromol , vol.34 , pp. 233-240
    • Andrade, C.T.1    Barros, L.A.M.2    Lima, M.C.P.3    Azero, E.G.4
  • 26
    • 12344296469 scopus 로고    scopus 로고
    • Novel internally staged ultrafiltration for protein purification
    • Feins M, Sirkar KK. Novel internally staged ultrafiltration for protein purification. J Membr Sci. 2005;248:137-148.
    • (2005) J Membr Sci , vol.248 , pp. 137-148
    • Feins, M.1    Sirkar, K.K.2
  • 28
    • 65349084827 scopus 로고    scopus 로고
    • Separation of hemoglobin from unpoly- merized hemoglobin on hydroxyapatite using HPLC
    • US Pat 5,691,453
    • Wertz CE, Gawryl MS. Separation of hemoglobin from unpoly- merized hemoglobin on hydroxyapatite using HPLC. US Pat 5,691,453 (1996).
    • (1996)
    • Wertz, C.E.1    Gawryl, M.S.2
  • 29
    • 3042551057 scopus 로고    scopus 로고
    • Purification of hemoglobin by ion exchange chromatography in flow-through mode with PEG as an escort
    • Lu X, Zhao D, Su Z. Purification of hemoglobin by ion exchange chromatography in flow-through mode with PEG as an escort. Artif Cells Blood Substit Immobil Biotechnol. 2004; 32:209-227.
    • (2004) Artif Cells Blood Substit Immobil Biotechnol , vol.32 , pp. 209-227
    • Lu, X.1    Zhao, D.2    Su, Z.3
  • 30
    • 34548140080 scopus 로고    scopus 로고
    • Purification of bovine hemoglobin via fast performance liquid chromatography
    • Dimino ML, Palmer AF. Purification of bovine hemoglobin via fast performance liquid chromatography. J Chromatogr B: Anal Technol Biomed Life Sci. 2007;856:353-357.
    • (2007) J Chromatogr B: Anal Technol Biomed Life Sci , vol.856 , pp. 353-357
    • Dimino, M.L.1    Palmer, A.F.2
  • 31
    • 42749087930 scopus 로고    scopus 로고
    • Preparation of ultrapure bovine and human hemoglobin by anion exchange chromatography
    • Sun G, Palmer AF. Preparation of ultrapure bovine and human hemoglobin by anion exchange chromatography. J Chromatogr B. 2008;867:1-7.
    • (2008) J Chromatogr B , vol.867 , pp. 1-7
    • Sun, G.1    Palmer, A.F.2
  • 33
    • 33646375361 scopus 로고    scopus 로고
    • Methods for the synthesis of a modified hemoglobin solution
    • US Pat 044214
    • Privalle CT, Stacey CJ, Talarico TL. Methods for the synthesis of a modified hemoglobin solution. US Pat 044214 (2002).
    • (2002)
    • Privalle, C.T.1    Stacey, C.J.2    Talarico, T.L.3
  • 34
    • 0021860548 scopus 로고
    • Processing cell lysate with tangential flow filtration
    • Gabler R, Ryan M. Processing cell lysate with tangential flow filtration. ACS Symp Ser. 1985;271:1-20.
    • (1985) ACS Symp Ser , vol.271 , pp. 1-20
    • Gabler, R.1    Ryan, M.2
  • 35
    • 0020758702 scopus 로고
    • Several uses for tangential-flow filtration in the pharmaceutical industry
    • Genovesi CS. Several uses for tangential-flow filtration in the pharmaceutical industry. J Parenter Sci Technol. 1983;37:81-86.
    • (1983) J Parenter Sci Technol , vol.37 , pp. 81-86
    • Genovesi, C.S.1
  • 36
    • 49749202424 scopus 로고
    • Standardization of hemoglobin- ometry. I. The extinction coefficient of hemiglobincyanide at Clin
    • Zijlstra WG, van Kampen EJ. Standardization of hemoglobin- ometry. I. The extinction coefficient of hemiglobincyanide at Clin Chim Acta. 1960;5:719-726.
    • (1960) Chim Acta , vol.5 , pp. 719-726
    • Zijlstra, W.G.1    van Kampen, E.J.2
  • 37
    • 0033991321 scopus 로고    scopus 로고
    • Endotoxin removal from protein solutions
    • Petsch D, Anspach FB. Endotoxin removal from protein solutions. J Biotechnol. 2000;76:97-119.
    • (2000) J Biotechnol , vol.76 , pp. 97-119
    • Petsch, D.1    Anspach, F.B.2
  • 38
    • 65349105801 scopus 로고    scopus 로고
    • The ABC's of filtration and biopro- cessing for the third millennium
    • Spectum Laboratories Inc, CA
    • Spectum Laboratories Inc. The ABC's of filtration and biopro- cessing for the third millennium. Spectum Laboratories, Inc: Rancho Dominguez, CA, 2002.
    • (2002) Spectum Laboratories, Inc: Rancho Dominguez
  • 39
    • 0031973525 scopus 로고    scopus 로고
    • Effect of superoxide anions on red blood cell rheologic properties
    • Baskurt OK, Temiz A, Meiselman HJ. Effect of superoxide anions on red blood cell rheologic properties. Free Radic Biol Med. 1998;24:102-110.
    • (1998) Free Radic Biol Med , vol.24 , pp. 102-110
    • Baskurt, O.K.1    Temiz, A.2    Meiselman, H.J.3
  • 40
    • 0015217710 scopus 로고
    • Further characterization of bovine superoxide dismutase and its isolation from bovine heart
    • Keele BB Jr, McCord JM, Fridovich I. Further characterization of bovine superoxide dismutase and its isolation from bovine heart. J Biol Chem. 1971;246:2875-2880.
    • (1971) J Biol Chem , vol.246 , pp. 2875-2880
    • Keele Jr, B.B.1    McCord, J.M.2    Fridovich, I.3
  • 41
    • 14044255326 scopus 로고    scopus 로고
    • Photopolymerization of bovine hemoglobin entrapped nanoscale hydrogel particles within liposomal reactors for use as an artificial blood substitute
    • Patton JN, Palmer AF. Photopolymerization of bovine hemoglobin entrapped nanoscale hydrogel particles within liposomal reactors for use as an artificial blood substitute. Biomacromole- cules. 2005;6:414-24.
    • (2005) Biomacromole- cules , vol.6 , pp. 414-424
    • Patton, J.N.1    Palmer, A.F.2
  • 42
    • 0018860147 scopus 로고
    • Regulation of oxygen affinity of mammalian haemoglobins
    • Perutz MF, Imai K. Regulation of oxygen affinity of mammalian haemoglobins. J Mol Biol. 1980;136:183-191.
    • (1980) J Mol Biol , vol.136 , pp. 183-191
    • Perutz, M.F.1    Imai, K.2
  • 43
    • 29644434820 scopus 로고    scopus 로고
    • Influence of the chemistry of conjugation of poly(ethylene glycol) to Hb on the oxygen-binding and solution properties of the PEG-Hb conjugate
    • Hu T, Prabhakaran M, Acharya SA, Manjula BN. Influence of the chemistry of conjugation of poly(ethylene glycol) to Hb on the oxygen-binding and solution properties of the PEG-Hb conjugate. Biochem J. 2005;392:555-564.
    • (2005) Biochem J , vol.392 , pp. 555-564
    • Hu, T.1    Prabhakaran, M.2    Acharya, S.A.3    Manjula, B.N.4
  • 44
    • 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. 2001;92:103-117.
    • (2001) Biophys Chem , vol.92 , pp. 103-117
    • McCarthy, M.R.1    Vandegriff, K.D.2    Winslow, R.M.3
  • 45
    • 0016411716 scopus 로고
    • Cooperative interactions of hemoglobin
    • Edelstein SJ. Cooperative interactions of hemoglobin. Annu Rev Biochem. 1975;44:209-232.
    • (1975) Annu Rev Biochem , vol.44 , pp. 209-232
    • Edelstein, S.J.1
  • 46
    • 0345169971 scopus 로고    scopus 로고
    • Preparation and characterization of dimeric bovine hemoglobin tetramers
    • Hu T, Li D, Su Z. Preparation and characterization of dimeric bovine hemoglobin tetramers. J Protein Chem. 2003;22:411-416.
    • (2003) J Protein Chem , vol.22 , pp. 411-416
    • Hu, T.1    Li, D.2    Su, Z.3
  • 47
    • 0023258085 scopus 로고
    • Influence of anions and protons on the Adair coefficients of hemoglobins A and Cowtown (His HC3(146)Beta-]Leu)
    • Shih DTB, Perutz MF. Influence of anions and protons on the Adair coefficients of hemoglobins A and Cowtown (His HC3(146)Beta-]Leu). J Mol Biol. 1987;195:419-422.
    • (1987) J Mol Biol , vol.195 , pp. 419-422
    • Shih, D.T.B.1    Perutz, M.F.2
  • 48
    • 0032052777 scopus 로고    scopus 로고
    • Bovine hemoglobin R-globin chain polymorphism: Primary structure determination of two new genetic variants by mass spectrometry and amino acid sequencing
    • Scaloni A, Pieragostini E, Malorni A, Ferrara L, Di Luccia A. Bovine hemoglobin R-globin chain polymorphism: primary structure determination of two new genetic variants by mass spectrometry and amino acid sequencing. Biochimie. 1998;80: 333-338.
    • (1998) Biochimie , vol.80 , pp. 333-338
    • Scaloni, A.1    Pieragostini, E.2    Malorni, A.3    Ferrara, L.4    Di Luccia, A.5


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