RECONSTITUTION OF IMMUNOLOGIC ACTIVITY BY INTERACTION OF POLYPEPTIDE CHAINS OF ANTIBODIES

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Abstract
Dissociation of purified guinea pig antibodies against f1 shage, f2 phage, and the dinitrophenyl group into L and H polypeptide chains led to a marked drop in the activity of the separated fractions. Mixture of the L and H chain fractions of the same antibody preparation resulted in partial reconstitution of activity as measured by phage neutralization or equilibrium dialysis. Reconstitution of activity against a given antigen was also found using mixtures of H chains from antibodies originally directed against that antigen and L chains from unrelated antibodies or gamma-globulin. In every case, however, the reconstitution of activity was greatest when both L and H chains from the homologous antibodies were mixed. Mixtures of L chain fractions from homologous antibodies and H chain fractions from unrelated antibodies usually showed no activity. In some cases, however, activity was observed when L and H chains from antibodies originally unrelated to the test antigen were mixed. The results support the chain interaction hypothesis of antibody activity and suggest that both H and L chains contribute to immunologic specificity.

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