Abstract
A antigen-antibody crossed electrophoresis technique, described by Laurell, was modified, the first step-electrophoresis being performed in polyacrylamide gel. This allowed separation of molecules not only by their charge but also by their difference in molecular size. Various murine IgA myeloma proteins, when analyzed in this way with a monospecific rabbit antiserum against mouse IgA, showed different precipitin profiles, each one typical for a particular myeloma protein. A proportional distribution of the various molecular size units of IgA can be obtained directly from a serum sample without any prior purification by this procedure.
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