3he antigen binding capacity and idiotypic specifity of isolated and reassociated chains of an IgG1 myeloma protein with anti-horse-alpha-2-macroglobulin activity (Fero) and of an IgM cryoglobulin with anti-IgG activity (Far), were investigated by precipitation and inhibition of precipitation methods. The binding capacity of heavy chains obtained from both proteins was about 10-fold higher than that of the light chains. The inhibitory capacity of recombinants composed of the autologous heavy chains of protein Fero was not significantly higher than that of the isolated heavy chains. Autologous light chians reassociated with heterolgous heavy chains were mnore effective in the inhibition test, than the isolated chains. Heterologous recombinants could not precipitae the antigen. The heavy chains of protein Far recombined with heterologous light chian showed a higher binding capacity than did the separated heavy chains. These recombinants had cyoprecipitation ability. Expression of idiotypic determinants of both proteins was more or less parallel with the antibody activity. The activity of H chains to form antibodies of similar specificity with series of L chains differing in V sequences is discusse.d.
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