Abstract
Procedures for the purification of antiprotein antibodies from serum, secretions, or culture fluids based upon differences in their physicochemical properties because of their antigenic specificities are limited because of their structural heterogeneity. Affinity chromatography that utilizes the specific and reversible interaction of antibodies with their antigen has permitted the isolation and characterization of antibodies from a wide variety of sources. Isolation of myeloma proteins with antibody activity secreted from human and murine lymphoid malignancies, antibodies from immunized and diseased individuals, and minute quantities of antibodies synthesized in vitro may be accomplished with immunoadsorbents. Immunoadsorbents may also be used as antibodies. If not extensively derivatized, antibodies retain their reactivity with their specific antigen. Preparation of antibody immunoadsorbents has facilitated the isolation of proteins, polypeptide chain components of proteins, or their degradation products.
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