An improved method for the isolation of normal immunoglobulin E is described. The method is based on the use of an immunoadsorbent formed by the mechanical entrapment of antibodies against a myeloma immunoglobulin E into a lattice of a highly cross-linked macroporous polyacrylamide gel. Normal immunoglobulin E was isolated from an immunoglobulin E-rich serum pool as well as from an individual healthy donor. The isolated immunoglobulin E was contaminated with about 20% of immunoglobulin G. An antiserum against normal immunoglobulin E was prepared by immunizing rabbits with the isolated immunoglobulin E.

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