Rabbits were immunized with purified rat liver catalase as an antigen, and antisera were collected. Anti-catalase immunoglobulin was purified from the antisera and was dissociated into subunits by reduction with mercaptoethanol. H- and L-chains were isolated after alkylation, and their antibody activities were investigated. No strong evidence has been so far obtained in support of localization of the antibody activity on any of those isolated subunits.
When anti-catalase immunoglobulin was reduced and the dissociated subunits were permitted to recombine, the anti-catalase activity was completely recovered. Dialysis against 1M propionic acid prior to recombination resulted in as much as 40% loss in antibody activity upon subsequent recombination. Alkylated H- and L-chains were also recombined, but the antibody activity of the reconstituted material, having the size of 7S immunoglobulin, was found to be one-tenth that of the native anti-catalase immunoglobulin.

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