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Volumn 56, Issue 4, 1996, Pages 809-815

Preparation of a trivalent antigen-binding construct using polyoxime chemistry: Improved biodistribution and potential for therapeutic application

Author keywords

[No Author keywords available]

Indexed keywords

IMMUNOGLOBULIN F(AB) FRAGMENT; OXIME;

EID: 0030020157     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (25)

References (16)
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    • Modeling analysis of the global and microscopic distribution of immunoglobulin G. F(ab′)2, and Fab in tumors
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    • (1989) Cancer Res. , vol.49 , pp. 5656-5663
    • Fujimori, K.1    Covell, D.G.2    Fletcher, J.E.3    Weinstein, J.N.4
  • 3
    • 0028231302 scopus 로고
    • Facile synthesis of homogeneous artificial proteins
    • Rose, K. Facile synthesis of homogeneous artificial proteins. J. Am. Chem. Soc., 116. 30-33, 1994
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 30-33
    • Rose, K.1
  • 5
    • 0020571717 scopus 로고
    • Monoclonal antibodies to carcinoembryonic antigen: Ionic strength as a factor in the selection of antibodies for immunoscintigraphy
    • Haskell, C. M., Buchegger, F., Schreyer, M., Carrel, S , and Mach, J-P. Monoclonal antibodies to carcinoembryonic antigen: ionic strength as a factor in the selection of antibodies for immunoscintigraphy Cancer Res., 43. 3857-3864, 1983
    • (1983) Cancer Res. , vol.43 , pp. 3857-3864
    • Haskell, C.M.1    Buchegger, F.2    Schreyer, M.3    Carrel, S.4    Mach, J.-P.5
  • 6
    • 0028535272 scopus 로고
    • High-yield, site-specific coupling of N-terminally modified β-lactamase to a proteolytically derived single-sulfhydryl murine Fab′
    • Mikolajczyk, S. D., Meyer, D. L., Starling, J. J., Law, K. L., Rose, K , Dufour, B , and Offord, R. E. High-yield, site-specific coupling of N-terminally modified β-lactamase to a proteolytically derived single-sulfhydryl murine Fab′. Bioconjugate Chem., 5: 636-646, 1994.
    • (1994) Bioconjugate Chem. , vol.5 , pp. 636-646
    • Mikolajczyk, S.D.1    Meyer, D.L.2    Starling, J.J.3    Law, K.L.4    Rose, K.5    Dufour, B.6    Offord, R.E.7
  • 8
    • 0021236693 scopus 로고
    • Determination of the immunoreactive fraction of monoclonal antibodies by linear extrapolation to binding at infinite antigen excess
    • Lindmo, T., Boven, E , Cuttitta, F., Fedorko, J., and Bunn, P. A. Determination of the immunoreactive fraction of monoclonal antibodies by linear extrapolation to binding at infinite antigen excess J Immunol Methods, 72: 77-89, 1984.
    • (1984) J Immunol Methods , vol.72 , pp. 77-89
    • Lindmo, T.1    Boven, E.2    Cuttitta, F.3    Fedorko, J.4    Bunn, P.A.5
  • 9
    • 0342373035 scopus 로고
    • Determination of equilibrium binding parameters of monoclonal antibodies specific for cell surface antigens
    • Trucco, M., and de Petris, S. Determination of equilibrium binding parameters of monoclonal antibodies specific for cell surface antigens. Immunol. Methods, 2. 1-26, 1981
    • (1981) Immunol. Methods , vol.2 , pp. 1-26
    • Trucco, M.1    De Petris, S.2
  • 11
    • 0015313012 scopus 로고
    • The influence of polyvalency on the binding properties of antibodies
    • Crothers, D. M., and Metzger, H. The influence of polyvalency on the binding properties of antibodies. Immunochemistry, 9: 341-357, 1972.
    • (1972) Immunochemistry , vol.9 , pp. 341-357
    • Crothers, D.M.1    Metzger, H.2
  • 12
    • 0027572697 scopus 로고
    • Preparation, characterization and in vivo biodistribution properties of synthetically cross-linked multivalent antitumor antibody fragments
    • Schott, M. E , Frazier, K. A., Pollock, D. K., and Verbanac, K. M. Preparation, characterization and in vivo biodistribution properties of synthetically cross-linked multivalent antitumor antibody fragments Bioconjugate Chem., 4: 153-165, 1993.
    • (1993) Bioconjugate Chem. , vol.4 , pp. 153-165
    • Schott, M.E.1    Frazier, K.A.2    Pollock, D.K.3    Verbanac, K.M.4
  • 14
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    • Effect of bivalent interaction upon apparent antibody affinity: Experimental confirmation of theory using fluorescence photobleaching and implications for antibody binding assays
    • Kaufman, E. N., and Jain, R. K. Effect of bivalent interaction upon apparent antibody affinity: experimental confirmation of theory using fluorescence photobleaching and implications for antibody binding assays. Cancer Res., 52: 4157-4167, 1992.
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    • Kaufman, E.N.1    Jain, R.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.