메뉴 건너뛰기




Volumn 208, Issue 2, 1997, Pages 191-202

Synthesis of mono- and bifunctional peptide-dextran conjugates for the immobilization of peptide antigens on ELISA plates: Properties and application

Author keywords

Anti human gastrointestinal glutathione peroxidase; Anti peptide antibody; Biotin; Dextran; ELISA; Peptide conjugate

Indexed keywords

ANTIGEN; BIOTIN; DEXTRAN; GLUTATHIONE PEROXIDASE; INTESTINE ENZYME; MONOCLONAL ANTIBODY; PEPTIDE; POLYCLONAL ANTIBODY;

EID: 0344222212     PISSN: 00221759     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-1759(97)00149-X     Document Type: Article
Times cited : (41)

References (30)
  • 1
    • 0028294854 scopus 로고
    • A versatile synthetic peptide-based ELISA for identifying antibody epitopes
    • Ball J.M., Henry N.L., Montelaro R.C., Newman M.J. A versatile synthetic peptide-based ELISA for identifying antibody epitopes. J. Immunol. Methods. 171:1994;37-44.
    • (1994) J. Immunol. Methods , vol.171 , pp. 37-44
    • Ball, J.M.1    Henry, N.L.2    Montelaro, R.C.3    Newman, M.J.4
  • 2
    • 0026764424 scopus 로고
    • Dextran, a hapten carrier in immunoassays for s-triazines. A comparison with ELISAs based on hapten-protein conjugates
    • Böcher M., Giersch T., Schmid R.D. Dextran, a hapten carrier in immunoassays for s-triazines. A comparison with ELISAs based on hapten-protein conjugates. J. Immunol. Methods. 151:1992;1-8.
    • (1992) J. Immunol. Methods , vol.151 , pp. 1-8
    • Böcher, M.1    Giersch, T.2    Schmid, R.D.3
  • 3
    • 0008061650 scopus 로고
    • Direct coupling of an atrazine to microtiter plates for a competitive immunoassay for s-triazines
    • Böcher M., Sorensen K. Direct coupling of an atrazine to microtiter plates for a competitive immunoassay for s-triazines. Food Agric. Immunol. 6:1994;155-161.
    • (1994) Food Agric. Immunol. , vol.6 , pp. 155-161
    • Böcher, M.1    Sorensen, K.2
  • 5
    • 0028940880 scopus 로고
    • Antipeptide antibodies confirm the topology of the human norepinephrine transporter
    • Brüss M., Hammermann R., Brimijoin S., Bönisch H. Antipeptide antibodies confirm the topology of the human norepinephrine transporter. J. Biol. Chem. 270:1995;9197-9201.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9197-9201
    • Brüss, M.1    Hammermann, R.2    Brimijoin, S.3    Bönisch, H.4
  • 6
    • 0028909073 scopus 로고
    • Autoantibodies directed against ribosomal P proteins: Use of a multiple antigen peptide as the coating agent in ELISA
    • Caponi L., Pegoraro S., Di Bartolo V., Rovero P., Revoltella R., Bombardieri S. Autoantibodies directed against ribosomal P proteins: Use of a multiple antigen peptide as the coating agent in ELISA. J. Immunol. Methods. 179:1995;193-202.
    • (1995) J. Immunol. Methods , vol.179 , pp. 193-202
    • Caponi, L.1    Pegoraro, S.2    Di Bartolo, V.3    Rovero, P.4    Revoltella, R.5    Bombardieri, S.6
  • 7
    • 0023019719 scopus 로고
    • Diversity and structure of human T-cell receptor β-chain variable region genes
    • Concannon P., Pickering L.A., Kung P., Hood L. Diversity and structure of human T-cell receptor β-chain variable region genes. Proc. Natl. Acad. Sci. USA. 83:1986;6598-6602.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 6598-6602
    • Concannon, P.1    Pickering, L.A.2    Kung, P.3    Hood, L.4
  • 8
    • 0024561213 scopus 로고
    • Cross-reaction of antibodies to coupling groups used in the production of anti-peptide antibodies
    • Edwards R.J., Singleton A.M., Boobis A.R., Davies D.S. Cross-reaction of antibodies to coupling groups used in the production of anti-peptide antibodies. J. Immunol. Methods. 117:1989;215-220.
    • (1989) J. Immunol. Methods , vol.117 , pp. 215-220
    • Edwards, R.J.1    Singleton, A.M.2    Boobis, A.R.3    Davies, D.S.4
  • 9
    • 0023832630 scopus 로고
    • The influence of pH and ionic strength on the coating of peptides of herpes simplex virus type 1 in an enzyme-linked immunosorbent assay
    • Geerligs H.J., Weijer W.J., Bloemhoff W., Welling G.W., Welling-Wester S. The influence of pH and ionic strength on the coating of peptides of herpes simplex virus type 1 in an enzyme-linked immunosorbent assay. J. Immunol. Methods. 106:1988;239-244.
    • (1988) J. Immunol. Methods , vol.106 , pp. 239-244
    • Geerligs, H.J.1    Weijer, W.J.2    Bloemhoff, W.3    Welling, G.W.4    Welling-Wester, S.5
  • 10
    • 0028907140 scopus 로고
    • Hydrocoating: A new method for coupling biomolecules to solid phases
    • Gregorius K., Mouritsen S., Elsner H.I. Hydrocoating: A new method for coupling biomolecules to solid phases. J. Immunol. Methods. 181:1995;65-73.
    • (1995) J. Immunol. Methods , vol.181 , pp. 65-73
    • Gregorius, K.1    Mouritsen, S.2    Elsner, H.I.3
  • 11
    • 0024555577 scopus 로고
    • Solid-phase immunoassay of serum antibodies to peptides. Covalent antigen binding to adsorbed phenylalanine-lysine copolymers
    • Hobbs R.N. Solid-phase immunoassay of serum antibodies to peptides. Covalent antigen binding to adsorbed phenylalanine-lysine copolymers. J. Immunol. Methods. 117:1989;257-266.
    • (1989) J. Immunol. Methods , vol.117 , pp. 257-266
    • Hobbs, R.N.1
  • 12
    • 0000448982 scopus 로고
    • Prediction of protein antigenic determinants from amino acid sequences
    • Hopp T.P., Woods K.R. Prediction of protein antigenic determinants from amino acid sequences. Proc. Natl. Acad. Sci. USA. 78:1981;3824-3828.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 3824-3828
    • Hopp, T.P.1    Woods, K.R.2
  • 13
    • 0028923790 scopus 로고
    • Conjugation to preactivated proteins using divinylsulfone and iodoacetic acid
    • Houen G., Jensen O.M. Conjugation to preactivated proteins using divinylsulfone and iodoacetic acid. J. Immunol. Methods. 181:1995;187-200.
    • (1995) J. Immunol. Methods , vol.181 , pp. 187-200
    • Houen, G.1    Jensen, O.M.2
  • 14
    • 0026702480 scopus 로고
    • Effective method for synthetic peptide immobilization that increases the sensitivity and specificity of ELISA procedures
    • Ivanov V.S., Suvorova Z.K., Tchikin L.D., Kozhich A.T., Ivanov V.T. Effective method for synthetic peptide immobilization that increases the sensitivity and specificity of ELISA procedures. J. Immunol. Methods. 153:1992;229-233.
    • (1992) J. Immunol. Methods , vol.153 , pp. 229-233
    • Ivanov, V.S.1    Suvorova, Z.K.2    Tchikin, L.D.3    Kozhich, A.T.4    Ivanov, V.T.5
  • 15
    • 0028942264 scopus 로고
    • Analysis of substrate recognition determinants in a synthetic peptide containing the Tyr 1173 autophosphorylation site of the epidermal growth factor receptor
    • Klingbeil C.K., Gill G.N., Cadena D.L. Analysis of substrate recognition determinants in a synthetic peptide containing the Tyr 1173 autophosphorylation site of the epidermal growth factor receptor. Arch. Biochem. Biophys. 316:1995;745-750.
    • (1995) Arch. Biochem. Biophys. , vol.316 , pp. 745-750
    • Klingbeil, C.K.1    Gill, G.N.2    Cadena, D.L.3
  • 16
    • 0029038913 scopus 로고
    • Localization of a sequential B-epitope in the VP2 protein of hepatitis A virus
    • Kulik L.N., Ivanov V.S., Tchikin L.D., Ostrovsky A.G., Ivanov V.T. Localization of a sequential B-epitope in the VP2 protein of hepatitis A virus. FEBS Lett. 367:1995;85-88.
    • (1995) FEBS Lett. , vol.367 , pp. 85-88
    • Kulik, L.N.1    Ivanov, V.S.2    Tchikin, L.D.3    Ostrovsky, A.G.4    Ivanov, V.T.5
  • 17
    • 0027968263 scopus 로고
    • Alcian blue-treated polystyrene microtitre plates for use in an ELISA to measure antibodies against synthetic peptides
    • Lagacé J., Arsenault S., Cohen E.A. Alcian blue-treated polystyrene microtitre plates for use in an ELISA to measure antibodies against synthetic peptides. J. Immunol. Methods. 175:1994;131-135.
    • (1994) J. Immunol. Methods , vol.175 , pp. 131-135
    • Lagacé, J.1    Arsenault, S.2    Cohen, E.A.3
  • 18
    • 0023225888 scopus 로고
    • Covalent binding of proteins to grafted plastic surfaces suitable for immunoassays. I. Binding capacity and characteristics of grafted polymers
    • Larsson P.H., Johansson S.G.O., Hult A., Göthe S. Covalent binding of proteins to grafted plastic surfaces suitable for immunoassays. I. Binding capacity and characteristics of grafted polymers. J. Immunol. Methods. 98:1987;129-135.
    • (1987) J. Immunol. Methods , vol.98 , pp. 129-135
    • Larsson, P.H.1    Johansson, S.G.O.2    Hult, A.3    Göthe, S.4
  • 19
    • 0025362071 scopus 로고
    • Covalent binding of detergent-solubilized membrane glycoproteins to 'Chemobond' plates for ELISA
    • Lutz H.U., Stammler P., Fischer E.A. Covalent binding of detergent-solubilized membrane glycoproteins to 'Chemobond' plates for ELISA. J. Immunol. Methods. 129:1990;211-220.
    • (1990) J. Immunol. Methods , vol.129 , pp. 211-220
    • Lutz, H.U.1    Stammler, P.2    Fischer, E.A.3
  • 22
    • 0028281399 scopus 로고
    • A method for the high efficiency of water-soluble carbodiimide-mediated amidation
    • Sehgal D., Vijay I.K. A method for the high efficiency of water-soluble carbodiimide-mediated amidation. Anal. Biochem. 218:1994;87-91.
    • (1994) Anal. Biochem. , vol.218 , pp. 87-91
    • Sehgal, D.1    Vijay, I.K.2
  • 23
    • 0030589816 scopus 로고    scopus 로고
    • Preferential labeling of α-amino N-terminal groups in peptides by biotin: Application to the detection of specific anti-peptide antibodies by enzyme immunoassays
    • Sélo I., Négroni L., Créminon C., Grassi J., Wal J.M. Preferential labeling of α-amino N-terminal groups in peptides by biotin: Application to the detection of specific anti-peptide antibodies by enzyme immunoassays. J. Immunol. Methods. 199:1996;127-138.
    • (1996) J. Immunol. Methods , vol.199 , pp. 127-138
    • Sélo, I.1    Négroni, L.2    Créminon, C.3    Grassi, J.4    Wal, J.M.5
  • 24
    • 0029034341 scopus 로고
    • Peptide-specific antibodies as probes of the topography of the voltage-gated channel in the mitochondrial outer membrane of Neurospora crassa
    • Stanley S., Dias J.A., DÁrcangelis D., Mannella C.A. Peptide-specific antibodies as probes of the topography of the voltage-gated channel in the mitochondrial outer membrane of Neurospora crassa. J. Biol. Chem. 270:1995;16694-16700.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16694-16700
    • Stanley, S.1    Dias, J.A.2    Dárcangelis, D.3    Mannella, C.A.4
  • 25
    • 0025370436 scopus 로고
    • Highly specific characterization of tyrosine phosphoproteins in tumor cells based on monoclonal antibodies defined by conjugated phosphotyramine
    • Steinhilber G., Sproll M.W., Wolff J.M., Anderer F.A. Highly specific characterization of tyrosine phosphoproteins in tumor cells based on monoclonal antibodies defined by conjugated phosphotyramine. Cancer Res. 10:1990;907-912.
    • (1990) Cancer Res. , vol.10 , pp. 907-912
    • Steinhilber, G.1    Sproll, M.W.2    Wolff, J.M.3    Anderer, F.A.4
  • 26
    • 0029833251 scopus 로고    scopus 로고
    • Recent advances in multiple antigen peptides
    • Tam J.P. Recent advances in multiple antigen peptides. J. Immunol. Methods. 196:1996;17-32.
    • (1996) J. Immunol. Methods , vol.196 , pp. 17-32
    • Tam, J.P.1
  • 27
    • 0025358532 scopus 로고
    • Biotinyl-estradiol derivatives in enzyme immunoassay: Structural requirements for optimal antibody binding
    • Tiefenauer L.X., Andres R.Y. Biotinyl-estradiol derivatives in enzyme immunoassay: Structural requirements for optimal antibody binding. J. Steroid Biochem. 35:1990;633-639.
    • (1990) J. Steroid Biochem. , vol.35 , pp. 633-639
    • Tiefenauer, L.X.1    Andres, R.Y.2
  • 30
    • 0029961377 scopus 로고    scopus 로고
    • Multi-well ELISA based on independent peptide antigens for antibody capture. Application to Lyme disease serodiagnosis
    • Yu Z., Carter J.M., Sigal L.H., Stein S. Multi-well ELISA based on independent peptide antigens for antibody capture. Application to Lyme disease serodiagnosis. J. Immunol. Methods. 198:1996;25-33.
    • (1996) J. Immunol. Methods , vol.198 , pp. 25-33
    • Yu, Z.1    Carter, J.M.2    Sigal, L.H.3    Stein, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.