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Volumn 38, Issue 1, 2008, Pages 1-8

Statistical optimization of immunoaffinity purification of hepatitis B surface antigen using response surface methodology

Author keywords

Affinity; Chromatography; Hepatitis B surface antigen; Monoclonal antibodies; Optimization; Response surfaces methodology

Indexed keywords

CHROMATOGRAPHY; IMMUNOLOGY; MONOCLONAL ANTIBODIES; OPTIMIZATION; STATISTICAL METHODS; SURFACE TREATMENT;

EID: 36849076753     PISSN: 1369703X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bej.2007.05.016     Document Type: Article
Times cited : (17)

References (37)
  • 1
    • 0034078342 scopus 로고    scopus 로고
    • Hepatitis B: an important public health issue
    • Maddrey W.C. Hepatitis B: an important public health issue. J. Med. Virol. 61 (2000) 362-366
    • (2000) J. Med. Virol. , vol.61 , pp. 362-366
    • Maddrey, W.C.1
  • 2
    • 0030707941 scopus 로고    scopus 로고
    • Hepatitis B virus infection
    • Lee W.M. Hepatitis B virus infection. N. Engl. J. Med. 337 (1997) 1733-1745
    • (1997) N. Engl. J. Med. , vol.337 , pp. 1733-1745
    • Lee, W.M.1
  • 3
    • 0019985965 scopus 로고
    • Synthesis and assembly of hepatitis B virus surface antigen particles in yeast
    • Valenzuela P., Medina A., Rutter W.J., Ammerer G., and Hall B.D. Synthesis and assembly of hepatitis B virus surface antigen particles in yeast. Nature 298 (1982) 347-350
    • (1982) Nature , vol.298 , pp. 347-350
    • Valenzuela, P.1    Medina, A.2    Rutter, W.J.3    Ammerer, G.4    Hall, B.D.5
  • 6
    • 0002170114 scopus 로고
    • The hepatitis B virus (HBV) infection and its prevention by a recombinant-DNA viral surface antigen (rec-HBsAg) vaccine
    • Pentón E., Muzio V., and Griego-González M. The hepatitis B virus (HBV) infection and its prevention by a recombinant-DNA viral surface antigen (rec-HBsAg) vaccine. Biotecnología Aplicada 11 (1994) 1-11
    • (1994) Biotecnología Aplicada , vol.11 , pp. 1-11
    • Pentón, E.1    Muzio, V.2    Griego-González, M.3
  • 7
    • 0001868509 scopus 로고
    • HIS 3 gene of Saccharomyces cerevisiae complement his mutation in yeast, Pichia pastoris
    • Yong V., González M.E., Herrera L.S., and Delgado J.M. HIS 3 gene of Saccharomyces cerevisiae complement his mutation in yeast, Pichia pastoris. Biotecnología Aplicada 9 (1992) 55-61
    • (1992) Biotecnología Aplicada , vol.9 , pp. 55-61
    • Yong, V.1    González, M.E.2    Herrera, L.S.3    Delgado, J.M.4
  • 8
    • 0343314905 scopus 로고    scopus 로고
    • Large-scale production of recombinant hepatitis B surface antigen from Pichia pastoris
    • Hardy E., Martinez E., Diago D., Diaz R., Gonzalez D., and Herrera L. Large-scale production of recombinant hepatitis B surface antigen from Pichia pastoris. J. Biotechnol. 77 (2000) 157-167
    • (2000) J. Biotechnol. , vol.77 , pp. 157-167
    • Hardy, E.1    Martinez, E.2    Diago, D.3    Diaz, R.4    Gonzalez, D.5    Herrera, L.6
  • 9
    • 0028237472 scopus 로고
    • Immunoaffinity purification of recombinant hepatitis B surface antigen from yeast using a monoclonal antibody
    • Agraz A., Duarte C.A., Costa L., Pérez L., Páez R., Pujol V., and Fontirrochi G. Immunoaffinity purification of recombinant hepatitis B surface antigen from yeast using a monoclonal antibody. J. Chromatogr. A 672 (1994) 25-33
    • (1994) J. Chromatogr. A , vol.672 , pp. 25-33
    • Agraz, A.1    Duarte, C.A.2    Costa, L.3    Pérez, L.4    Páez, R.5    Pujol, V.6    Fontirrochi, G.7
  • 10
    • 0347478147 scopus 로고    scopus 로고
    • Expression and characterization of an anti-(hepatitis B surface antigen) glycosylated mouse antibody in transgenic tobacco (Nicotiana tabacum) plants and its use in the immunopurification of its target antigen
    • Ramírez N., Rodríguez M., Ayala M., Cremata J., Pérez M., Martínez A., Linares M., Hevia Y., Páez R., Valdés R., Gavilondo J.V., and Selman-Housein G. Expression and characterization of an anti-(hepatitis B surface antigen) glycosylated mouse antibody in transgenic tobacco (Nicotiana tabacum) plants and its use in the immunopurification of its target antigen. Biotechnol. Appl. Biochem. 38 Pt 3 (2003) 223-230
    • (2003) Biotechnol. Appl. Biochem. , vol.38 , Issue.PART 3 , pp. 223-230
    • Ramírez, N.1    Rodríguez, M.2    Ayala, M.3    Cremata, J.4    Pérez, M.5    Martínez, A.6    Linares, M.7    Hevia, Y.8    Páez, R.9    Valdés, R.10    Gavilondo, J.V.11    Selman-Housein, G.12
  • 13
    • 0032730427 scopus 로고    scopus 로고
    • Comparison of different elution conditions for the immunopurification of recombinant hepatitis B surface antigen
    • Ibarra N., Caballero A., González E., and Valdés R. Comparison of different elution conditions for the immunopurification of recombinant hepatitis B surface antigen. J. Chromatogr. B 735 (1999) 271-277
    • (1999) J. Chromatogr. B , vol.735 , pp. 271-277
    • Ibarra, N.1    Caballero, A.2    González, E.3    Valdés, R.4
  • 14
    • 0026124847 scopus 로고
    • Elution conditions and degradation mechanisms in long-term immunosorbent use
    • Pickard-Antonsen K., Colton C.K., and Yarmush M.L. Elution conditions and degradation mechanisms in long-term immunosorbent use. Biotechnol. Prog. 7 (1991) 159-172
    • (1991) Biotechnol. Prog. , vol.7 , pp. 159-172
    • Pickard-Antonsen, K.1    Colton, C.K.2    Yarmush, M.L.3
  • 15
    • 0035975871 scopus 로고    scopus 로고
    • Efficient elution of functional proteins in affinity chromatography
    • Firer M.A. Efficient elution of functional proteins in affinity chromatography. J. Biochem. Biophys. Methods 49 (2001) 433-442
    • (2001) J. Biochem. Biophys. Methods , vol.49 , pp. 433-442
    • Firer, M.A.1
  • 16
    • 0031242744 scopus 로고    scopus 로고
    • Optimisation of immunoaffinity purification of Wuchereria bancrofti specific antibodies from human sera
    • Kannan K., Lalitha P., Rao K.V., Narayanan R.B., and Kaliraj P. Optimisation of immunoaffinity purification of Wuchereria bancrofti specific antibodies from human sera. Indian J. Exp. Biol. 35 (1997) 1076-1079
    • (1997) Indian J. Exp. Biol. , vol.35 , pp. 1076-1079
    • Kannan, K.1    Lalitha, P.2    Rao, K.V.3    Narayanan, R.B.4    Kaliraj, P.5
  • 17
    • 0029934276 scopus 로고    scopus 로고
    • Rapid purification of the oxygenase component of toluene dioxygenase from a polyol-responsive monoclonal antibody
    • Lynch N.A., Jiang H., and Gibson D.T. Rapid purification of the oxygenase component of toluene dioxygenase from a polyol-responsive monoclonal antibody. Appl. Environ. Microbiol. 62 (1996) 2133-2137
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 2133-2137
    • Lynch, N.A.1    Jiang, H.2    Gibson, D.T.3
  • 18
    • 0023017718 scopus 로고
    • Generation of a new monoclonal antibody and its application for the determination and purification of biologically active human gamma-interferon
    • Oda S., Akinaga S., Kumagai A., Inoue A., Nakamizo N., and Yoshida H. Generation of a new monoclonal antibody and its application for the determination and purification of biologically active human gamma-interferon. Hybridoma 5 (1986) 329-338
    • (1986) Hybridoma , vol.5 , pp. 329-338
    • Oda, S.1    Akinaga, S.2    Kumagai, A.3    Inoue, A.4    Nakamizo, N.5    Yoshida, H.6
  • 19
    • 0031573405 scopus 로고    scopus 로고
    • Effect of three elution buffers on the recovery and structure of monoclonal antibodies
    • Narhi L.O., Caughey D.J., Horan T., Kita Y., Chang D., and Arakawa T. Effect of three elution buffers on the recovery and structure of monoclonal antibodies. Anal. Biochem. 253 (1997) 236-245
    • (1997) Anal. Biochem. , vol.253 , pp. 236-245
    • Narhi, L.O.1    Caughey, D.J.2    Horan, T.3    Kita, Y.4    Chang, D.5    Arakawa, T.6
  • 21
    • 0036126093 scopus 로고    scopus 로고
    • Lipase-catalyzed incorporation of docosahexaenoic acid (DHA) into borage oil: optimization using response surface methodology
    • Senanayake S.P.J., and Shahidi F. Lipase-catalyzed incorporation of docosahexaenoic acid (DHA) into borage oil: optimization using response surface methodology. Food Chem. 77 (2002) 115-123
    • (2002) Food Chem. , vol.77 , pp. 115-123
    • Senanayake, S.P.J.1    Shahidi, F.2
  • 22
    • 0038068846 scopus 로고    scopus 로고
    • Use of response surface methodology for optimizing process parameters for the production of α-amylase by Aspergillus oryzae
    • Francis F., Sabu A., Nampoothiri K.M., Ramachandran S., Ghosh S., Szakacs G., and Pandey A. Use of response surface methodology for optimizing process parameters for the production of α-amylase by Aspergillus oryzae. Biochem. Eng. J. 15 (2003) 107-115
    • (2003) Biochem. Eng. J. , vol.15 , pp. 107-115
    • Francis, F.1    Sabu, A.2    Nampoothiri, K.M.3    Ramachandran, S.4    Ghosh, S.5    Szakacs, G.6    Pandey, A.7
  • 23
    • 0033054494 scopus 로고    scopus 로고
    • Performance of pectolytic enzymes during hydrolysis of pectic substances under assay conditions: a statistical approach
    • Naidu G.S.N., and Panda T. Performance of pectolytic enzymes during hydrolysis of pectic substances under assay conditions: a statistical approach. Enzyme Microb. Technol. 25 (1999) 116-124
    • (1999) Enzyme Microb. Technol. , vol.25 , pp. 116-124
    • Naidu, G.S.N.1    Panda, T.2
  • 24
    • 0034096370 scopus 로고    scopus 로고
    • Application of response surface methodology to the study of methyl glucoside polyester synthesis parameters in a solvent-free system
    • Shieh C.J., and Lai Y.F. Application of response surface methodology to the study of methyl glucoside polyester synthesis parameters in a solvent-free system. J. Agric. Food Chem. 48 (2000) 1124-1128
    • (2000) J. Agric. Food Chem. , vol.48 , pp. 1124-1128
    • Shieh, C.J.1    Lai, Y.F.2
  • 25
    • 0002363078 scopus 로고
    • On the experimental attainment of optimum multifactorial conditions
    • Box G.E.P., and Wilson K.B. On the experimental attainment of optimum multifactorial conditions. R. Stat. Soc. 13 (1951) 1-12
    • (1951) R. Stat. Soc. , vol.13 , pp. 1-12
    • Box, G.E.P.1    Wilson, K.B.2
  • 26
    • 0028837672 scopus 로고
    • Optimization and characterization of controlled release pellets coated with experimental latex. I. Anionic drug
    • Singh S.K., Dodge J., Durrani M.J., and Khan M.A. Optimization and characterization of controlled release pellets coated with experimental latex. I. Anionic drug. Int. J. Pharm. 125 (1995) 243-255
    • (1995) Int. J. Pharm. , vol.125 , pp. 243-255
    • Singh, S.K.1    Dodge, J.2    Durrani, M.J.3    Khan, M.A.4
  • 28
    • 0027443515 scopus 로고
    • The recovery of the hepatitis B surface antigen (HBsAg) from a recombinant P. pastoris strain: disruption and precipitation studies
    • Páez R., Agraz A., and Herrera L. The recovery of the hepatitis B surface antigen (HBsAg) from a recombinant P. pastoris strain: disruption and precipitation studies. Acta Biotechnol. 13 (1993) 117-122
    • (1993) Acta Biotechnol. , vol.13 , pp. 117-122
    • Páez, R.1    Agraz, A.2    Herrera, L.3
  • 29
    • 0027703530 scopus 로고
    • Adsorption-desorption of recombinant hepatitis B surface antigen (r-HBsAg) from P. pastoris on diatomaceous heart matrix: optimization of parameters for purification
    • Agraz A., Quiñonez Y., Expósito N., Breña F., Madruga Y., Pentón E., and Herrera L. Adsorption-desorption of recombinant hepatitis B surface antigen (r-HBsAg) from P. pastoris on diatomaceous heart matrix: optimization of parameters for purification. Biotechnol Bioeng. 42 (1993) 1238-1244
    • (1993) Biotechnol Bioeng. , vol.42 , pp. 1238-1244
    • Agraz, A.1    Quiñonez, Y.2    Expósito, N.3    Breña, F.4    Madruga, Y.5    Pentón, E.6    Herrera, L.7
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 31
    • 0019551730 scopus 로고
    • "Western blotting": electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A
    • Burnette W.N. "Western blotting": electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal. Biochem. 112 (1981) 195-203
    • (1981) Anal. Biochem. , vol.112 , pp. 195-203
    • Burnette, W.N.1
  • 32
    • 8244245527 scopus 로고
    • Cuantificación del HBsAg en muestras biológicas con fines asistenciales y preparativos
    • González A., Alerm A., Salgado A., Ramírez V., and González T. Cuantificación del HBsAg en muestras biológicas con fines asistenciales y preparativos. Biotecnología Aplicada 10 (1993) 104-105
    • (1993) Biotecnología Aplicada , vol.10 , pp. 104-105
    • González, A.1    Alerm, A.2    Salgado, A.3    Ramírez, V.4    González, T.5
  • 33
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantification of microgram quantities of proteins utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for quantification of microgram quantities of proteins utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 34
    • 36849086358 scopus 로고    scopus 로고
    • Design Expert Version 6.0.1, User's Guide, Section 12, Stat-Ease Inc., USA, 2005.


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