메뉴 건너뛰기




Volumn 37, Issue 4, 2009, Pages 147-155

Solid phase pegylation of hemoglobin

Author keywords

Hemoglobin; Polyethylene glycol; Red blood cell substitute; Solid phase

Indexed keywords

BOVINE HEMOGLOBIN; CONVENTIONAL METHODS; ION EXCHANGE CHROMATOGRAPHY; LIQUID PHASE; MOBILE PHASE; PEGYLATED HEMOGLOBINS; PEGYLATION; RED BLOOD CELL; RED BLOOD CELL SUBSTITUTE; SDS-PAGE; SOLID MEDIUM; SOLID PHASE;

EID: 68849121480     PISSN: 10731199     EISSN: 15324184     Source Type: Journal    
DOI: 10.1080/10731190903041188     Document Type: Article
Times cited : (13)

References (21)
  • 1
    • 0017701219 scopus 로고
    • Alteration of immunological properties of bovine serum albumin by covalent attachment of polyethylene glycol
    • Abuchowski, A., Es, T.V. et al. (1977). Alteration of immunological properties of bovine serum albumin by covalent attachment of polyethylene glycol. J. Biol. Chem 252:3578-3581.
    • (1977) J. Biol. Chem , vol.252 , pp. 3578-3581
    • Abuchowski, A.1    Es, T.V.2
  • 2
    • 33646909899 scopus 로고    scopus 로고
    • Structure-function engineering of interferon-beta-1b for improving stability, solubility, potency, immunogenicity, and pharmacokinetic properties by site-selective mono-pegylation
    • Basu, A., Yang, K. et al. (2006). Structure-function engineering of interferon-beta-1b for improving stability, solubility, potency, immunogenicity, and pharmacokinetic properties by site-selective mono-pegylation. Bioconjug Chem 17:618-630.
    • (2006) Bioconjug Chem , vol.17 , pp. 618-630
    • Basu, A.1    Yang, K.2
  • 3
    • 0033079841 scopus 로고    scopus 로고
    • Future prospects for artificial blood
    • 181
    • Chang, T.M.S. (1999). Future prospects for artificial blood. Trends in Boitechnology. Tibtech 17(2): 181:61-67.
    • (1999) Trends in Boitechnology. Tibtech , vol.17 , Issue.2 , pp. 61-67
    • Chang, T.M.S.1
  • 5
    • 0021162143 scopus 로고
    • Solvent regulation of oxygen affinity in hemoglobin
    • Fronticelli, C., Bucci, E., Orth, C. (1984). Solvent regulation of oxygen affinity in hemoglobin. J. Biol. Chem 259:10841-10844.
    • (1984) J. Biol. Chem , vol.259 , pp. 10841-10844
    • Fronticelli, C.1    Bucci, E.2    Orth, C.3
  • 6
    • 33744539498 scopus 로고    scopus 로고
    • Lowry method for the determination of pegylated proteins: The error, it reason, and a method for eliminating it
    • Gong, X.W., Wei, D.Z. et al. (2006). Lowry method for the determination of pegylated proteins: the error, it reason, and a method for eliminating it. Anal Biochem 354:157-158.
    • (2006) Anal Biochem , vol.354 , pp. 157-158
    • Gong, X.W.1    Wei, D.Z.2
  • 7
    • 34247525975 scopus 로고    scopus 로고
    • Conjugation of methoxypolyethylene glycol to the surface of bovine red blood cells
    • Gundersen, S., Palmer, A.F. (2007). Conjugation of methoxypolyethylene glycol to the surface of bovine red blood cells. Biotechnology and Bioengineering 96(6): 1199-1210.
    • (2007) Biotechnology and Bioengineering , vol.96 , Issue.6 , pp. 1199-1210
    • Gundersen, S.1    Palmer, A.F.2
  • 8
    • 0033805142 scopus 로고    scopus 로고
    • Surface modification of diaspirin cross-linked hemoglobin (DCLHb) with chondroitin-4-sulfate derivatives, part 1
    • Hai, T.T., Pereira, D.E. et al. (2000). Surface modification of diaspirin cross-linked hemoglobin (DCLHb) with chondroitin-4-sulfate derivatives, part 1. Bioconjug Chem 11: 705-713.
    • (2000) Bioconjug Chem , vol.11 , pp. 705-713
    • Hai, T.T.1    Pereira, D.E.2
  • 10
    • 0037362655 scopus 로고    scopus 로고
    • Effect of pegylation on pharmaceuticals
    • Harris, J.M., Chess, R.B. (2003). Effect of pegylation on pharmaceuticals. Nat Rev Drug Discov 2:214-21.
    • (2003) Nat Rev Drug Discov , vol.2 , pp. 214-221
    • Harris, J.M.1    Chess, R.B.2
  • 11
    • 0037434443 scopus 로고    scopus 로고
    • A solid phase adsorption method for preparation of bovine serum albumin bovine hemoglobin conjugate
    • Hu, T., Su, Z.G. (2003). A solid phase adsorption method for preparation of bovine serum albumin bovine hemoglobin conjugate. Journal of Biotechnology 100:267-275.
    • (2003) Journal of Biotechnology , vol.100 , pp. 267-275
    • Hu, T.1    Su, Z.G.2
  • 12
    • 0030844580 scopus 로고    scopus 로고
    • The different faces of poly (ethylene glycol)
    • Israelachvili, J. (1997). The different faces of poly (ethylene glycol). Proc Natl Acad Sci USA 94:8378-8379.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 8378-8379
    • Israelachvili, J.1
  • 13
    • 0035858379 scopus 로고    scopus 로고
    • Improvements in protein PEGylation: Pegylated interferons for treatment of hepatitis C
    • Kozlowski, A., Harris, J.M. (2001). Improvements in protein PEGylation: pegylated interferons for treatment of hepatitis C. J. Control. Release 72:217-224.
    • (2001) J. Control. Release , vol.72 , pp. 217-224
    • Kozlowski, A.1    Harris, J.M.2
  • 14
    • 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. (1997). Structures of a hemoglobin-based blood substitute: insights into the function of allosteric proteins. Structure 5(2):227-237.
    • (1997) Structure , vol.5 , Issue.2 , pp. 227-237
    • Kroeger, K.S.1    Kundrot, C.E.2
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural protein during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970). Cleavage of structural protein during the assembly of the head of bacteriophage T4. Nature 227(259):680-685.
    • (1970) Nature , vol.227 , Issue.259 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 36849064395 scopus 로고    scopus 로고
    • Solid-phase pegylation of recombinant interferon α-2a for site-specific modification: Process performance, characterization, and in vitro bioactivity
    • Lee, B. K., Lee, E. K. et al. (2007). Solid-phase pegylation of recombinant interferon α-2a for site-specific modification: process performance, characterization, and in vitro bioactivity. Bioconjugate Chem 18:1728-1734.
    • (2007) Bioconjugate Chem , vol.18 , pp. 1728-1734
    • Lee, B.K.1    Lee, E.K.2
  • 17
    • 3042551057 scopus 로고    scopus 로고
    • Purification of hemoglobin by ion exchange chromatography in flow-through mode with PEG as an escort institute of process engineering
    • Lu, X.L., Zhao, D.X., Su, Z.G. (2004). Purification of hemoglobin by ion exchange chromatography in flow-through mode with PEG as an escort institute of process engineering. Artificial Cell, Blood Substitutes, and Biotechnology 32(2):209-227.
    • (2004) Artificial Cell, Blood Substitutes, and Biotechnology , vol.32 , Issue.2 , pp. 209-227
    • Lu, X.L.1    Zhao, D.X.2    Su, Z.G.3
  • 18
    • 0345909511 scopus 로고    scopus 로고
    • Isolation of positional isomers of monopoly (ethylene glycol)ylated inter-feron-2a and the determination of their biochemical and biological characteristics
    • Harris, J.M, Zalipsky, S, Poly(ethyleneglycol) ACS, American Chemical Society, Washington, DC
    • Monkarsh, S.P., Spence, et al. (1997). Isolation of positional isomers of monopoly (ethylene glycol)ylated inter-feron-2a and the determination of their biochemical and biological characteristics. In Harris, J.M., Zalipsky, S., Poly(ethyleneglycol) ACS Symposium Series, American Chemical Society, Washington, DC., 207-216.
    • (1997) Symposium Series , pp. 207-216
    • Monkarsh, S.P.1    Spence2
  • 19
    • 0037124389 scopus 로고    scopus 로고
    • Solid-phase synthesis of new peptide-arene hybrids from N-TCP amino acids
    • Planas, M., Cros, E. et al. (2002). Solid-phase synthesis of new peptide-arene hybrids from N-TCP amino acids. Tetrahedron Letters 43:4431-4434.
    • (2002) Tetrahedron Letters , vol.43 , pp. 4431-4434
    • Planas, M.1    Cros, E.2
  • 21
    • 0026812687 scopus 로고
    • Evaluation of a new reagent for covalent attachment of polyethylene glycol to proteins
    • Zalipsky, S., Seltzar, R., Menon-Rudolph, S. (1992). Evaluation of a new reagent for covalent attachment of polyethylene glycol to proteins. Biotechnol Appl Biochem 15:100-114.
    • (1992) Biotechnol Appl Biochem , vol.15 , pp. 100-114
    • Zalipsky, S.1    Seltzar, R.2    Menon-Rudolph, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.