Abstract
(1) The homoreactants directed to the tryptic 3 β5 S fragments, Fab″ and 5 S fragments, F(ab″) 2 from rabbit IgG could be demonstrated in normal rabbit IgG by agglutination of Fab″ or F(ab″) 2-conjugated erythrocytes. (2) These homoreactants could be distinguished from those directed to the papain fragments, Fab and the peptic fragment, Fab′ by inhibition test of hemagglutination with each fragment. The homoreactant directed to Fab″ seems to be different from that directed to F(ab″) 2. (3) Immunoadsorbents were prepared by conjugation of Fab, Fabt́ or Fab″ with insoluble polymer of rabbit serum albumin. The homoreactants directed to Fab and Fab″ could be purified by adsorption on, elution with 1 M propionic acid from the homologous immunoadsorbents and by absorption with the heterologous immunoadsorbents. (4) These purified homoreactants (radiolageled) showed preferential binding activities with the homologous immunoadsorbents. The binding activity was inhibited strongly by the homologous fragments but weakly by the heterologous fragments. These results indicate that the antigenic determinants exposed by tryptic digestion are different from those done by papain or peptic digestion.
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