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[Selective interaction of immunoglobulin polypeptide chains. Quantitative evaluation of the idiotypic and antigen
We have analysed reassociated Ig molecules, containing heavy (H) or light (L) chains of Ig-B2 monoclonal antibody with human fibronectin binding activity and L of H chains of normal mouse serum immunoglobulin (Ig-NM). Examination of Ig-B2 idiotype expression in reassociated Ig indicated that 0.4% L-NM and 0.8% H-NM were able to restore Ig-B2 idiotype. The analysis of antigen binding capacity of reassociated Ig demonstrated, that only 4% H-NM created antigen binding site in complex with L-B2. We have determined the leading role of L-chain in creation of idiotype and binding site of Ig-B2. Selectivity of interaction between H and L chains is discussed. The results indicate, that not more than 4-6% of random H--L combinations produce functional Ig.
We have analysed reassociated Ig molecules, containing heavy (H) or light (L) chains of Ig-B2 monoclonal antibody with human fibronectin binding activity and L of H chains of normal mouse serum immunoglobulin (Ig-NM). Examination of Ig-B2 idiotype expression in reassociated Ig indicated that 0.4% L-NM and 0.8% H-NM were able to restore Ig-B2 idiotype. The analysis of antigen binding capacity of reassociated Ig demonstrated, that only 4% H-NM created antigen binding site in complex with L-B2. We have determined the leading role of L-chain in creation of idiotype and binding site of Ig-B2. Selectivity of interaction between H and L chains is discussed. The results indicate, that not more than 4-6% of random H--L combinations produce functional Ig.