The binding of bispecific monoclonal antibodies to the solid phase-adsorbed antigensстатья

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Дата последнего поиска статьи во внешних источниках: 18 июля 2013 г.

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[1] The binding of bispecific monoclonal antibodies to the solid phase-adsorbed antigens / D. A. Dmitriev, Y. S. Massino, M. B. Smirnova et al. // Russian Journal of Bioorganic Chemistry. — 2001. — Vol. 27, no. 4. — P. 232–240. The ability of bispecific antibodies (Babs) formed by fusion of hybridomas and parent monoclonal antibodies (Mabs) to interact with the solid phase-adsorbed antigens was studied. Mabs specific to the three different antigens [horseradish peroxidase (HRP), human IgG (hIgG), and human myoglobin (Mb)] as well as Babs with the double specificity [antimyoglobin/antiperoxidase (anti-Mb/HRP) and anti-human IgG/antiperoxidase (anti-hIgG/HRP)] were used. It was shown by radioimmunological and immunoenzyme assays that parent Mabs bind to solid phase-adsorbed antigens considerably more effectively than Babs. The observed equilibrium binding constant (K-a) of antiperoxidase parental Mabs to immobilized HRP is 21 and 38 times higher than K-a for Babs binding sites (anti-Mb/HRP and anti-hIG/HRP, respectively) to peroxidase. It was calculated that about 90-95% of all bound parental antiperoxidase Mabs were associated with immobilized HRP bivalently, and only about 5-10% were bound monovalently. On the contrary, parental Mabs against hIgG bind to the sorbed antigen essentially only monovalently. It was also shown that the avidity of anti-Mb/HRP Babs significantly increased when two antigens, Mb and HRP were simultaneously adsorbed on the solid phase. These data imply that Babs bearing an enzyme-binding site (for example, binding to HRP) cannot be more effective than standard conjugates (e.g., enzyme-conjugated antibodies) in heterogeneous noncompetitive immunoassays. [ DOI ]

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