Immunoelectrophoretic Analysis of Serum Proteins in Agar and in Agarose

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Abstract
Summary Several antigen-antibody precipitin systems were compared by immuno-electrophoretic analysis using agar and agarose as the supporting medium. Electroendosmosis was reduced in agarose, mobility of components was more rapid, lateral separation of alpha and beta globulin components was increased and better definition of individual precipitin arcs in this medium was observed. Some precipitin reactions which failed to develop in agar gave clear reactions in agarose. The reverse was never observed. There were some individual antigen-antibody reactions in which there appeared to be little change in either the shape or position of the precipitin arcs on either medium, but increased clarity was always observed on the agarose medium. The advantages of agarose for I.E.A. when increased sensitivity is required, as in quantitating antigens or in testing for homogeneity of purified proteins, should be considered.

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