Monoclonal antibodies against plasma protease inhibitors: I. Production and characterization of 23 monoclonal antibodies against human α2

This is the authors' abstract. We don't add key points for this paper.

23 hybridomas secreting monoclonal antibodies against human alpha 2-antiplasmin, the fast-acting inhibitor of plasmin present in plasma, have been produced by the cell-fusion technique. Isotyping of the monoclonal antibodies has revealed that 14 monoclonal antibodies belong to the class IgG1, 6 to the class IgG2a, and 3 to the class IgG2b. All light chains belong to the kappa group. The specificity and relative avidity of these monoclonals have been determined using an indirect enzyme-linked immunosorbent assay. 13 monoclonals exhibit a relatively high avidity for alpha 2-antiplasmin, 5 are of intermediate avidity, and 5 of low avidity. The epitope specificity of these 23 monoclonal antibodies, originating from a single mouse, have been examined in inhibition experiments. A group of 10 monoclonal antibodies exhibit a very similar inhibition pattern. Partial inhibition effects displayed by 10 other antibodies define partially overlapping antigenic regions. The binding of these antibodies seems to produce a conformational change in the alpha 2-antiplasmin molecule, reducing the binding of two other antibodies. The last antibody defines an independent epitope.