Abstract
The purification of the IgM monoclonal antibody 436 against a breast tumor antigen from mouse ascitic fluid is reported. The purified immunoglobulin was radioiodinated and the resulting product assessed for its binding capacity and binding specificity. Purified IgM-436 served for F(ab') 2μpreparation which was tested for its antigen binding capacity. Radioiodinated IgM-436 and its F(ab')2μ retained their immunological activity which was never lower than those of the corresponding cold products.
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