The above data indicate the presence of mercaptoethanol sensitive, slowly sedimenting anti-BSA antibody in the duck which by gel filtration and radio-immunoelectrophoresis did not behave like a mammalian 7S γ globulin. The gel filtration experiment suggested that the antibody was somewhat larger in size than the 7S proteins and the radioimmunoelectrophoretic patterns localized the antibody activity to a protein which migrated separately from the 7S γ globulin line. This antibody bears a striking resemblance in some of its characteristics to the β2A (γ1A) immunoglobulin described in the mammal. Although the evidence is still not complete, data obtained with ragweed skin-sensitizing antibody indicate that β2A (γ1A) antibodies are a) larger than 7S(8), and b) mercaptoethanol sensitive(9).
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H M Grey (1963) studied this question.
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