Monoclonal antibodies against human α-fetoprotein exploitation of an unusual calcium-dependent interaction with the antigen for analytical and preparative purposes

Seven murine hybridomas were established producing IgG1 monoclonal antibodies (mAbs) against three different epitopes of human α-fetoprotein (αFP). The interaction of two of these mAbs (AFP-01 and AFP-02) with the antigen was strongly inhibited by calcium-chelating agents. The mAb AFP-11 could be us...

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Veröffentlicht in:	Journal of immunological methods 1988-06, Vol.111 (1), p.67-73
Hauptverfasser:	Štefanová, Irena, Hořejší, Václav, Krištofová, Hana, Angelisová, Pavla, Žižkovský, Václav, Hilgert, Ivan
Format:	Artikel
Sprache:	eng
Schlagworte:	alpha-Fetoproteins - analysis alpha-Fetoproteins - immunology Animals Antibodies, immunoglobulins Antibodies, Monoclonal - biosynthesis Antibodies, Monoclonal - immunology Antigen-Antibody Reactions - drug effects Binding, Competitive Biological and medical sciences Calcium-dependent antibody Chelating Agents - pharmacology Collodion Electrophoresis, Polyacrylamide Gel Enzyme-Linked Immunosorbent Assay Epitopes - immunology Female Fundamental and applied biological sciences. Psychology Fundamental immunology Humans Hybridomas - metabolism Immunoaffinity chromatography Indicators and Reagents Mice Mice, Inbred BALB C Molecular immunology Monoclonal antibodies Monoclonal antibody Radioimmunoassay Structure-Activity Relationship α-Fetoprotein
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Beschreibung
Zusammenfassung:	Seven murine hybridomas were established producing IgG1 monoclonal antibodies (mAbs) against three different epitopes of human α-fetoprotein (αFP). The interaction of two of these mAbs (AFP-01 and AFP-02) with the antigen was strongly inhibited by calcium-chelating agents. The mAb AFP-11 could be used for estimation of αFP by RIA in the concentration range of 5–100 ng/ml. Several combinations of the mAbs could be used in a two-site sandwich-ELISA for similar purposes. Immunoaffinity chromatography on a column of immobilized mAb AFP-01 permitted the purification of αFP.
ISSN:	0022-1759 1872-7905
DOI:	10.1016/0022-1759(88)90060-9