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No ferrihaem was detected in the precipitate formed by metmyoglobin with an antiserum to apomyoglobin and the extinction at 410mmu of metmyoglobin, due to ferrihaem, was decreased by the univalent fragments of apomyoglobin antibodies. It was concluded that the combination of apomyoglobin antibodies with metmyoglobin caused the release of ferrihaem. As the removal of ferrihaem from metmyoglobin is accompanied by a conformational change, it was concluded that the conformation of metmyoglobin was altered by the apomyoglobin antibodies. 2. Antisera to metmyoglobin were divided into two groups; antisera of the first group revealed differences between the immunological reactivities of metmyoglobin and apomyoglobin, whereas no differences were detected with antisera of the second group. 3. Metmyoglobin was only partially re-formed by adding haematin to the precipitate produced by apomyoglobin with an antiserum of the first group, whereas complete re-formation of metmyoglobin was achieved in the presence of antisera of the second group. No metmyoglobin was formed on the addition of haematin to the precipitates produced by either metmyoglobin or apomyoglobin with the anti-apomyoglobin serum. 4. Immune precipitates formed by antisera to metmyoglobin dissociated at pH1.8, whereas those formed by the anti-apomyoglobin serum did not dissociate. 5. These results suggest that apomyoglobin possessed different conformations when combined with metmyoglobin antibodies and apomyoglobin antibodies.
MJ Crumpton (Fri,) studied this question.