Abstract
Murine myeloma anti-idiotypic and anti-Ig class antibodies were insolubilized with ethyl chloroformate and used as immunoadsorbents for the isolation of the corresponding immunoglobulins. The isolation was achieved from whole serum in a one-step purification procedure. The following globulins were isolated: two myeloma γl globulins, one myeloma γ 2a globulin, a myeloma μ globulin and normal IgGl and IgM. Judged by electrophoretic, immunoelectrophoretic and immunogenic criteria the isolated globulins could not be distinguished from those present in whole serum. For the various immunoadsorbents, the ratio of antibody insolubilized to globulin antigen isolated ranged from 1.45 : 1 to 3 : 1.
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