The Inhibition by Normal γG-Globulins of Antibodies Specific for Individual γG Myeloma Proteins

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Abstract
Summary: Thirty-three antisera to ten isolated γG myeloma globulins were first absorbed in order to show only individual antigenic specificity of the homologous myeloma protein. Further absorption with variable but usually large amounts of normal fraction II resulted in the complete neutralization of the individually specific antibodies in 13 antisera. Absorption with as much as 100 mg/ml of fraction II resulted in partial neutralization of individually specific antibodies for 19 sera, whereas one antiserum was practically not affected. The ability of fraction II to neutralize individually specific antibodies varied greatly for the different kinds of antibodies to a given myeloma globulin, even within the same antiserum. It was demonstrated that neutralization by normal γG-globulins of these antibodies to individual specific antigens was due to specific inhibition without precipitation. Inhibition curves showed that the molecular localization on normal γG-globulins of the antigenic structures involved in this inhibition phenomenon is similar to that of the individual specific antigens on the homologous myeloma globulin. These findings are discussed in view of the analogy of myeloma globulins to their normal counterparts and to purified antibodies.

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