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Preparation and characterization of β1‐bungarotoxin bispecific monoclonal antibody
Author(s) -
Yang C. C.,
Chan H. L.
Publication year - 1999
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549900202163
Subject(s) - monoclonal antibody , bungarotoxin , characterization (materials science) , chemistry , antibody , microbiology and biotechnology , materials science , immunology , biology , nanotechnology , biochemistry , receptor , acetylcholine receptor
10.1080/15216549900202163.abs A hybrid hybridoma (tetradoma) that produces bispecific monoclonal antibodies (mAbs)2, which recognize two different epitopes on the A chain of β1‐bungarotoxin (β1‐bgt) at peptide sequences 46‐51 and 100‐106, has been obtained by fusing two hybridoma cell lines. The bispecific mAb were observed to inhibit 98% of the enzymatic activity of β1‐bgt and neutralize its lethal toxicity completely. The avidity between the bispecific mAb and β1‐bgt was noted to be 4.5×1010 (liter/nmol), which is about 45‐150 folds higher than the avidity of its two parental mAbs. All the soluble complexes, obtained from bispecific mAb and β1‐bgt with different molar ratios, emerged in the void volume of size exclusion chromatography column, indicating multiple complexes of β1‐bgt and bispecific mAb were formed. Based on these results, it indicated that the binding of bispecific mAb with its two epitopes on β1‐bgt, which facilitates the immuno‐complex formation and enhances the avidity, also highly neutralizes the biological activity of β1‐bgt.