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Volumn 13, Issue 3, 2004, Pages 69-79

Production of a human monoclonal IgM directed against human cardiac myosin in a hollow-fiber bioreactor for Membrane Anion Exchange Chromatography one-step purification

Author keywords

human monoclonal antibody; IgM Purification; membrane ion exchangers; myosin

Indexed keywords

CARDIAC MYOSIN; IMMUNOGLOBULIN M; MONOCLONAL ANTIBODY;

EID: 12844258976     PISSN: 10932607     EISSN: None     Source Type: Journal    
DOI: 10.3233/hab-2004-13303     Document Type: Article
Times cited : (11)

References (27)
  • 1
    • 0027213256 scopus 로고
    • Purification of two inurine monoclonal antibodies of the IgM class by hydroxylapatite chromatography and gel filtration
    • A.J. Henniker and K.F. Bradstock, Purification of two inurine monoclonal antibodies of the IgM class by hydroxylapatite chromatography and gel filtration, Biomed. Chromatogr. 7 (1993), 121-125.
    • (1993) Biomed. Chromatogr. , vol.7 , pp. 121-125
    • Henniker, A.J.1    Bradstock, K.F.2
  • 2
    • 0025968208 scopus 로고
    • Purification of a murine monoclonal antibody of IgM class
    • V.P. Knutson, R.A. Buck and R.M. Moreno, Purification of a murine monoclonal antibody of IgM class J, Immunol. Methods 136 (1991), 151-157.
    • (1991) J, Immunol. Methods , vol.136 , pp. 151-157
    • Knutson, V.P.1    Buck, R.A.2    Moreno, R.M.3
  • 3
    • 0028144495 scopus 로고
    • Purification and immunochemical characterization of a natural human polyractive monoclonal IgM antibody
    • D. Roggenbuck, U. Marx, S.T. Kiessig, G. Schoenherr, S. Jahn and T. Forstmann, Purification and immunochemical characterization of a natural human polyractive monoclonal IgM antibody, J. Immunol. Methods 167 (1994), 207-218.
    • (1994) J. Immunol. Methods , vol.167 , pp. 207-218
    • Roggenbuck, D.1    Marx, U.2    Kiessig, S.T.3    Schoenherr, G.4    Jahn, S.5    Forstmann, T.6
  • 6
    • 0034650977 scopus 로고    scopus 로고
    • Multiple human serum components act as bridging molecules in rosette formation by Plasmodium falciparum-infected erythrocytes
    • E.A. Sommer, J. Black and G. Pasvol, Multiple human serum components act as bridging molecules in rosette formation by Plasmodium falciparum-infected erythrocytes, Blood 95(2) (2000), 674-682.
    • (2000) Blood , vol.95 , Issue.2 , pp. 674-682
    • Sommer, E.A.1    Black, J.2    Pasvol, G.3
  • 7
    • 0031971221 scopus 로고    scopus 로고
    • Quantitation of IgG and IgM human anti-mouse antibodies (HAMA) interference in CA 125 measurements using affinity chromatography
    • N.P. Koper, C.M. Thomas, L.F. Massuger, M.F. Segers, A.J. Olthaar and A.L. Verbeek, Quantitation of IgG and IgM human anti-mouse antibodies (HAMA) interference in CA 125 measurements using affinity chromatography, Clin Chem Lab Med 36(1) (1998), 23-28.
    • (1998) Clin Chem Lab Med , vol.36 , Issue.1 , pp. 23-28
    • Koper, N.P.1    Thomas, C.M.2    Massuger, L.F.3    Segers, M.F.4    Olthaar, A.J.5    Verbeek, A.L.6
  • 8
    • 0027696608 scopus 로고
    • Application of a hollow fiber membrane cell culture system in medicine
    • U. Marx, H. Matthes, A. Nagel and R.V. Baehr, Application of a hollow fiber membrane cell culture system in medicine, Am. Biotechmol. Lab 11 (1993), 26.
    • (1993) Am. Biotechmol. Lab , vol.11 , pp. 26
    • Marx, U.1    Matthes, H.2    Nagel, A.3    Baehr, R.V.4
  • 9
    • 0019408803 scopus 로고
    • Human immunoglobulin M purification by affinity chromatography on protein A-Sepharose
    • M.A. Vidal and F.P. Conde, Human immunoglobulin M purification by affinity chromatography on protein A-Sepharose, J Biochem Biophys Methods 3-4 (1981), 155-161.
    • (1981) J Biochem Biophys Methods , vol.3 , Issue.4 , pp. 155-161
    • Vidal, M.A.1    Conde, F.P.2
  • 10
    • 0025145598 scopus 로고
    • The mecanism of carbohydrate-mediated complement activation by serum mannan-binding protein, T Kawasaki
    • M. Ohta, M. Okada and I. Yamashina, The mecanism of carbohydrate-mediated complement activation by serum mannan-binding protein, T Kawasaki, J. Biol. Chem. 265 (1990), 1980-1984.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1980-1984
    • Ohta, M.1    Okada, M.2    Yamashina, I.3
  • 11
    • 0035975903 scopus 로고    scopus 로고
    • Affinity membrane chromatography for the analysis and purification of proteins
    • H. Zou, Q. Luo and D. Zhou, Affinity membrane chromatography for the analysis and purification of proteins, J. Biochem. Biophys. Methods 49 (2001), 199-240.
    • (2001) J. Biochem. Biophys. Methods , vol.49 , pp. 199-240
    • Zou, H.1    Luo, Q.2    Zhou, D.3
  • 12
    • 0032243406 scopus 로고    scopus 로고
    • Fast assay and mini-purification of protein by high performance membrane affinity chromatography
    • D. Zhou, H. Zou, J. Ni, L. Yang, L. Jia and Y. Zhang, Fast assay and mini-purification of protein by high performance membrane affinity chromatography, Chin J Biotechnol 14(4) (1998), 233-240.
    • (1998) Chin J Biotechnol , vol.14 , Issue.4 , pp. 233-240
    • Zhou, D.1    Zou, H.2    Ni, J.3    Yang, L.4    Jia, L.5    Zhang, Y.6
  • 13
    • 0032906357 scopus 로고    scopus 로고
    • Membrane supports as the stationary phase in highperformance immunoaffinity chromatography
    • D. Zhou, H. Zou, J. Ni, L. Yang, L. Jia, Q. Zhang and Y. Zhang, Membrane supports as the stationary phase in highperformance immunoaffinity chromatography, Anal. Chem. 71 (1999), 115-118.
    • (1999) Anal. Chem. , vol.71 , pp. 115-118
    • Zhou, D.1    Zou, H.2    Ni, J.3    Yang, L.4    Jia, L.5    Zhang, Q.6    Zhang, Y.7
  • 14
    • 0032489399 scopus 로고    scopus 로고
    • Effect of porous structureof macroporous polymer supports on resolution in high-performance membrane chromatography of proteins
    • M.B. Tennikov, N.V. Gazdina, T.B. Tennikova and F. Svec, Effect of porous structureof macroporous polymer supports on resolution in high-performance membrane chromatography of proteins, Chromatogr 798(1-2) (1998), 55-64.
    • (1998) Chromatogr , vol.798 , Issue.1-2 , pp. 55-64
    • Tennikov, M.B.1    Gazdina, N.V.2    Tennikova, T.B.3    Svec, F.4
  • 15
    • 0025782993 scopus 로고
    • Carrier membrane as a stationary phase for affinity chromatography and kinetic studies of membrane-bound enzymes
    • H. Abou-Rebyeh, F. Korber, K. Schubert-Rehberg, J. Reusch and D.J. Josic, Carrier membrane as a stationary phase for affinity chromatography and kinetic studies of membrane-bound enzymes, J. Chromatogr. 566 (1991), 341-350.
    • (1991) J. Chromatogr. , vol.566 , pp. 341-350
    • Abou-Rebyeh, H.1    Korber, F.2    Schubert-Rehberg, K.3    Reusch, J.4    Josic, D.J.5
  • 16
    • 0026502058 scopus 로고
    • Carrier membrane as a stationary phase for affinity chromatography and kinetic studies of membrane-bound enzymes
    • D.J. Josic, J. Reutsch, K. Loster, O. Baum and W. Reutter, Carrier membrane as a stationary phase for affinity chromatography and kinetic studies of membrane-bound enzymes, J. Chromatogr. 590 (1992), 59-76.
    • (1992) J. Chromatogr. , vol.590 , pp. 59-76
    • Josic, D.J.1    Reutsch, J.2    Loster, K.3    Baum, O.4    Reutter, W.5
  • 17
    • 12844288226 scopus 로고    scopus 로고
    • US., Pat 5247575, 1996
    • A.G. Sartorius, US., Pat 5247575, 1996.
    • Sartorius, A.G.1
  • 18
    • 12844259110 scopus 로고    scopus 로고
    • US., Pat 5739316, 1998
    • A.G. Sartorius, US., Pat 5739316, 1998.
    • Sartorius, A.G.1
  • 21
    • 0023640890 scopus 로고
    • A method suitable for the isolation of monoclonal antibodies from larges volumes of serum-containing hybridoma cell culture supernatant
    • B. Malm, A method suitable for the isolation of monoclonal antibodies from larges volumes of serum-containing hybridoma cell culture supernatant, J. Immunol. Methods. 104 (1987), 103-109.
    • (1987) J. Immunol. Methods. , vol.104 , pp. 103-109
    • Malm, B.1
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli, 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
  • 23
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitration of microgram quantities of proteins utilizing the principle of protein-dye binding
    • M.M. Bradford, A rapid and sensitive method for the quantitration 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
  • 24
    • 0032508701 scopus 로고
    • Affinity purification of immunoglobulin M using a novel synthetic ligand
    • G. Palombo, A. Verdliva and G. Fassina, Affinity purification of immunoglobulin M using a novel synthetic ligand, J. Chromatogr. B. 715 (1988), 137-145.
    • (1988) J. Chromatogr. B. , vol.715 , pp. 137-145
    • Palombo, G.1    Verdliva, A.2    Fassina, G.3
  • 25
    • 0031692815 scopus 로고    scopus 로고
    • Anti-myosin scintigraphy for diagnosis and follow-up of patients with clinically suspected myocarditis
    • B. Lauer, U. Kuhl, M. Souvatzoglu, H. Vosberg and H.P. Schultheiss, Anti-myosin scintigraphy for diagnosis and follow-up of patients with clinically suspected myocarditis, Z. Kardiol. 87 (1998), 691-698.
    • (1998) Z. Kardiol. , vol.87 , pp. 691-698
    • Lauer, B.1    Kuhl, U.2    Souvatzoglu, M.3    Vosberg, H.4    Schultheiss, H.P.5
  • 26
    • 0032080630 scopus 로고    scopus 로고
    • Evaluation of biopsy classification for rejection: Relation to detection of myocardial damage by monoclonal anti-myosin antibody imaging
    • M. Ballester, M. Bordes, H.D. Talezaar, I. Carrio, J. Marrugat, J. Narula and M.E. Billingham, Evaluation of biopsy classification for rejection: relation to detection of myocardial damage by monoclonal anti-myosin antibody imaging, J. Am. Coil. Cardiol. 31 (1998), 1357-1361.
    • (1998) J. Am. Coil. Cardiol. , vol.31 , pp. 1357-1361
    • Ballester, M.1    Bordes, M.2    Talezaar, H.D.3    Carrio, I.4    Marrugat, J.5    Narula, J.6    Billingham, M.E.7
  • 27
    • 0026657037 scopus 로고
    • 2, Indium-111 anti-myosin antibodies for detection of rejection and drug induced cardiomyopathies
    • I. Carrio 2, Indium-111 anti-myosin antibodies for detection of rejection and drug induced cardiomyopathies, J. Nucl. Biol. Med. 36 (1992), 56-61.
    • (1992) J. Nucl. Biol. Med. , vol.36 , pp. 56-61
    • Carrio, I.1


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