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Volumn 274, Issue 1-2, 2003, Pages 115-127

Bispecific monoclonal antibodies against a viral and an enzyme: Utilities in ultrasensitive virus ELISA and phage display technology

Author keywords

BsMAb; Filamentous phage M13; Phage peptide library; Phage sandwich ELISA

Indexed keywords

ALKALINE PHOSPHATASE; BISPECIFIC ANTIBODY; BUFFER; COAT PROTEIN; HYBRID PROTEIN; LIGAND; MONOCLONAL ANTIBODY; PEPTIDE LIBRARY; PHOSPHATE; VIRUS ANTIBODY;

EID: 0037374090     PISSN: 00221759     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-1759(02)00511-2     Document Type: Article
Times cited : (8)

References (40)
  • 1
    • 0028962883 scopus 로고
    • Characterization of phage that bind plastic from phage displayed random peptide library
    • Adey N.B., Mataragnon A.H., Rider J.E., Carter J.M., Kay B.K. Characterization of phage that bind plastic from phage displayed random peptide library. Gene. 156:1995;27-31.
    • (1995) Gene , vol.156 , pp. 27-31
    • Adey, N.B.1    Mataragnon, A.H.2    Rider, J.E.3    Carter, J.M.4    Kay, B.K.5
  • 2
    • 20244380724 scopus 로고
    • The purification of alphavirus virions and subviral particles using ultrafiltration and gel exclusion chromatography
    • Alan J., Crooks J.M.L., John R.S. The purification of alphavirus virions and subviral particles using ultrafiltration and gel exclusion chromatography. Arch. Biochem. Biophys. 45:1985;275-281.
    • (1985) Arch. Biochem. Biophys. , vol.45 , pp. 275-281
    • Alan, J.1    Crooks, J.M.L.2    John, R.S.3
  • 3
    • 0023258208 scopus 로고
    • Measurement of monoclonal antibody affinity by non-competitive enzyme immunoassay
    • Beatty J.D., Beatty B.G., Vlahos W.G. Measurement of monoclonal antibody affinity by non-competitive enzyme immunoassay. J. Immunol. Methods. 100:1987;173-179.
    • (1987) J. Immunol. Methods , vol.100 , pp. 173-179
    • Beatty, J.D.1    Beatty, B.G.2    Vlahos, W.G.3
  • 4
    • 0028939328 scopus 로고
    • Monoclonal antibodies against a minor and the major coat proteins of filamentous phage M13: Their application in phage display
    • Bhardwaj D., Singh S.S., Abrol S., Chaudhary V.K. Monoclonal antibodies against a minor and the major coat proteins of filamentous phage M13: their application in phage display. J. Immunol. Methods. 179:1995;165-175.
    • (1995) J. Immunol. Methods , vol.179 , pp. 165-175
    • Bhardwaj, D.1    Singh, S.S.2    Abrol, S.3    Chaudhary, V.K.4
  • 5
    • 0030935706 scopus 로고    scopus 로고
    • Simple monitoring of antiretroviral therapy with a signal-amplification-boosted HIV-1 p24 antigen assay with heat-denatured plasma
    • Boni J., Opravil M., Tomasik Z., Rothen M., Bisset L., Grob P.J., Luthy R., Schupbach J. Simple monitoring of antiretroviral therapy with a signal-amplification-boosted HIV-1 p24 antigen assay with heat-denatured plasma. AIDS. 11:1997;F47-F52.
    • (1997) AIDS , vol.11
    • Boni, J.1    Opravil, M.2    Tomasik, Z.3    Rothen, M.4    Bisset, L.5    Grob, P.J.6    Luthy, R.7    Schupbach, J.8
  • 6
    • 0026792839 scopus 로고
    • Simplified methods for construction, assessment and rapid screening of peptide libraries in bacteriophage
    • Christian R.B., Zuckermann R.N., Kerr J.M., Wang L., Malcolm B.A. Simplified methods for construction, assessment and rapid screening of peptide libraries in bacteriophage. J. Mol. Biol. 227:1992;711-718.
    • (1992) J. Mol. Biol. , vol.227 , pp. 711-718
    • Christian, R.B.1    Zuckermann, R.N.2    Kerr, J.M.3    Wang, L.4    Malcolm, B.A.5
  • 7
    • 0027175366 scopus 로고
    • Determination of one thousandth of an attomole (1 zeptomole) of alkaline phosphatase: Application in an immunoassay of proinsulin
    • Cook D.B., Self C.H. Determination of one thousandth of an attomole (1 zeptomole) of alkaline phosphatase: application in an immunoassay of proinsulin. Clin. Chem. 39:1993;965-971.
    • (1993) Clin. Chem. , vol.39 , pp. 965-971
    • Cook, D.B.1    Self, C.H.2
  • 8
    • 0030003076 scopus 로고    scopus 로고
    • Study on single alkaline phosphatase molecules: Reaction rate and activation energy of a reaction catalyzed by a single molecule and effect of thermal denaturation - The death of an enzyme
    • Craig D.B., Arriaga E., Wong J.C.Y., Lu H., Dovichi N.J. Study on single alkaline phosphatase molecules: reaction rate and activation energy of a reaction catalyzed by a single molecule and effect of thermal denaturation - the death of an enzyme. J. Am. Chem. Soc. 118:1996;5245-5253.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 5245-5253
    • Craig, D.B.1    Arriaga, E.2    Wong, J.C.Y.3    Lu, H.4    Dovichi, N.J.5
  • 10
    • 0028085530 scopus 로고
    • Kunitz domain inhibitors of tissue foctor factor VIIa: I. Potent inhibitors selected from libraries by phage display
    • Dennis M.S., Lazarus R.A. Kunitz domain inhibitors of tissue foctor factor VIIa: I. Potent inhibitors selected from libraries by phage display. J. Biol. Chem. 269:1994;22129-22144.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22129-22144
    • Dennis, M.S.1    Lazarus, R.A.2
  • 11
    • 0025004285 scopus 로고
    • Radom peptide libraries: A source of specific protein binding molecules
    • Devlin J.J., Panganiban L.C., Devlin P.E. Radom peptide libraries: a source of specific protein binding molecules. Science. 249:1990;404-406.
    • (1990) Science , vol.249 , pp. 404-406
    • Devlin, J.J.1    Panganiban, L.C.2    Devlin, P.E.3
  • 12
    • 0027946232 scopus 로고
    • Isolation of a peptide antagonist to the thrombin receptor using phage display
    • Doorbar J., Winter G. Isolation of a peptide antagonist to the thrombin receptor using phage display. J. Mol. Biol. 244:1994;361-369.
    • (1994) J. Mol. Biol. , vol.244 , pp. 361-369
    • Doorbar, J.1    Winter, G.2
  • 15
    • 0016812341 scopus 로고
    • Isolation of hepatitis B surface antigen (HBsAg) by affinity chromatography on antibody-coated immunoadsorbents
    • Houwen B., Goudeau A., Dankert J. Isolation of hepatitis B surface antigen (HBsAg) by affinity chromatography on antibody-coated immunoadsorbents. J. Immunol. Methods. 8:1975;185-194.
    • (1975) J. Immunol. Methods , vol.8 , pp. 185-194
    • Houwen, B.1    Goudeau, A.2    Dankert, J.3
  • 16
    • 0023144221 scopus 로고
    • Bispecific antibody-producing hybrid hybridomas selected by a fluorescence activated cell sortor
    • Karawajew L., Micheel K.B., Behrsing O., Gaestel M. Bispecific antibody-producing hybrid hybridomas selected by a fluorescence activated cell sortor. J. Immunol. Method. 96:1987;256-270.
    • (1987) J. Immunol. Method , vol.96 , pp. 256-270
    • Karawajew, L.1    Micheel, K.B.2    Behrsing, O.3    Gaestel, M.4
  • 17
    • 0002765887 scopus 로고
    • Bispecifc monoclonal anti-CA125 X anti-peroxidase antibodies in the measurement of the ovarian carcinoma antigen
    • Kreutz F.T., Suresh M.R. Bispecifc monoclonal anti-CA125 X anti-peroxidase antibodies in the measurement of the ovarian carcinoma antigen. J. Tumor Marker Oncol. 10:1995;43-45.
    • (1995) J. Tumor Marker Oncol. , vol.10 , pp. 43-45
    • Kreutz, F.T.1    Suresh, M.R.2
  • 18
    • 0031003601 scopus 로고    scopus 로고
    • Novel bispecific immunoprobe for rapid and sensitive detection of prostate-specific antigen
    • Kreutz F.T., Suresh M.R. Novel bispecific immunoprobe for rapid and sensitive detection of prostate-specific antigen. Clin. Chem. 43:1997;649-656.
    • (1997) Clin. Chem. , vol.43 , pp. 649-656
    • Kreutz, F.T.1    Suresh, M.R.2
  • 20
    • 0024334886 scopus 로고
    • Design and applications of biomimetic anthraquinone dyes, purification of calf intestinal alkaline phosphatase with immobilized terminal ring analogues of C.I. reactive blue 2
    • Lindner N.M., Jeffcoat R., Lowe C.R. Design and applications of biomimetic anthraquinone dyes, purification of calf intestinal alkaline phosphatase with immobilized terminal ring analogues of C.I. reactive blue 2. J. Chromatogr. 473:1989;227-240.
    • (1989) J. Chromatogr. , vol.473 , pp. 227-240
    • Lindner, N.M.1    Jeffcoat, R.2    Lowe, C.R.3
  • 22
    • 0030976150 scopus 로고    scopus 로고
    • Bacteriaophage display and discovery of peptide leads for drug development
    • Lowman H.B. Bacteriaophage display and discovery of peptide leads for drug development. Annu. Rev. Biophys. Biomol. Struct. 26:1997;401-424.
    • (1997) Annu. Rev. Biophys. Biomol. Struct. , vol.26 , pp. 401-424
    • Lowman, H.B.1
  • 26
    • 0029610344 scopus 로고
    • Mammalian cell fusion in an electroporation device
    • Radomska H.S., Eckhardt L.A. Mammalian cell fusion in an electroporation device. J. Immunol. Methods. 188:1995;209-217.
    • (1995) J. Immunol. Methods , vol.188 , pp. 209-217
    • Radomska, H.S.1    Eckhardt, L.A.2
  • 29
    • 0025112794 scopus 로고
    • Searching for peptide ligands with an epitope library
    • Scott J.K., Smith G.P. Searching for peptide ligands with an epitope library. Science. 249:1990;386-390.
    • (1990) Science , vol.249 , pp. 386-390
    • Scott, J.K.1    Smith, G.P.2
  • 30
    • 0022556009 scopus 로고
    • "Single-shot" intrasplenic immunization for the production of monoclonal antibodies
    • Spitz M. "Single-shot" intrasplenic immunization for the production of monoclonal antibodies. Methods Enzymol. 121:1986;33-41.
    • (1986) Methods Enzymol. , vol.121 , pp. 33-41
    • Spitz, M.1
  • 31
    • 0024660580 scopus 로고
    • Redirecting the cellular immune response
    • Staerz U.D., Bevan M.J. Redirecting the cellular immune response. Int. Rev. Immunol. 4:1989;159-173.
    • (1989) Int. Rev. Immunol. , vol.4 , pp. 159-173
    • Staerz, U.D.1    Bevan, M.J.2
  • 32
    • 0025273561 scopus 로고
    • Dissection of functional domains in phage fd adsorption protein, discrimination between attachment and penetration sites
    • Stengele I., Bross P., Garces X., Giray J., Rasched I. Dissection of functional domains in phage fd adsorption protein, discrimination between attachment and penetration sites. J. Mol. 212:1990;143-149.
    • (1990) J. Mol. , vol.212 , pp. 143-149
    • Stengele, I.1    Bross, P.2    Garces, X.3    Giray, J.4    Rasched, I.5
  • 33
    • 0022555989 scopus 로고
    • Bispecific monoclonal antibodies from hybrid hybridomas
    • Suresh M.R., Cuello A.C., Milstein C. Bispecific monoclonal antibodies from hybrid hybridomas. Methods Enzymol. 121:1986;210-228.
    • (1986) Methods Enzymol. , vol.121 , pp. 210-228
    • Suresh, M.R.1    Cuello, A.C.2    Milstein, C.3
  • 34
    • 0022998719 scopus 로고
    • Advantages of bispecific hybridomas in one-step immunochemistry and immunoassays
    • Suresh M.R., Cuello A.C., Milstein C. Advantages of bispecific hybridomas in one-step immunochemistry and immunoassays. Proc. Natl. Acad. Sci. U. S. A. 83:1986;7989-7993.
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 7989-7993
    • Suresh, M.R.1    Cuello, A.C.2    Milstein, C.3
  • 36
    • 0030590643 scopus 로고    scopus 로고
    • Enhancement of ELISAs for screening peptides in epitope phage display libraries
    • Valadon P., Scharff M.D. Enhancement of ELISAs for screening peptides in epitope phage display libraries. J. Immunol. Methods. 197:1996;171-197.
    • (1996) J. Immunol. Methods , vol.197 , pp. 171-197
    • Valadon, P.1    Scharff, M.D.2
  • 37
    • 0023224968 scopus 로고
    • Bi-specific monoclonal antibodies: Selective binding and complement fixation to cells that express two different surface antigens
    • Wong J.T., Covin R.B. Bi-specific monoclonal antibodies: selective binding and complement fixation to cells that express two different surface antigens. J. Immunol. 139:1987;1369-1374.
    • (1987) J. Immunol. , vol.139 , pp. 1369-1374
    • Wong, J.T.1    Covin, R.B.2
  • 38
    • 0032549611 scopus 로고    scopus 로고
    • Mimetic ligand-based affinity purification of immune complexes and immunoconjugates
    • Xu D., Leveugle B., Kreutz F.T., Suresh M.R. Mimetic ligand-based affinity purification of immune complexes and immunoconjugates. J. Chromatogr. B. 706:1998;217-229.
    • (1998) J. Chromatogr. B , vol.706 , pp. 217-229
    • Xu, D.1    Leveugle, B.2    Kreutz, F.T.3    Suresh, M.R.4
  • 39
    • 0014748362 scopus 로고
    • Rapid bacteriophage sedimentation in the presence of polyethylene glycol and its application to large-scale virus purification
    • Yamamoto K.R. Rapid bacteriophage sedimentation in the presence of polyethylene glycol and its application to large-scale virus purification. Virology. 40:1970;734-753.
    • (1970) Virology , vol.40 , pp. 734-753
    • Yamamoto, K.R.1
  • 40
    • 0032212020 scopus 로고    scopus 로고
    • Bispecific antibodies as novel bioconjugates
    • Ying C., Suresh M.R. Bispecific antibodies as novel bioconjugates. Bioconjug. Chem. 9(6):1998;635-644.
    • (1998) Bioconjug. Chem. , vol.9 , Issue.6 , pp. 635-644
    • Ying, C.1    Suresh, M.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.