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PubMed1966

Conformational changes in sperm-whale metmyoglobin due to combination with antibodies to apomyoglobin.

1. 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.

Antibodies↗
PubMed1967

Immunochemistry of sperm-whale myoglobins prepared with various modified porphyrins and metalloporphyrins.

1. The preparation and characterization of manganese, iron, cobalt, nickel, copper and zinc metalloporphyrins is described. Ferrihaem was also esterified with pyrid-4-ylpropanol and the derivative characterized as the diester. 2. Complexes of these various porphyrins, as well as protoporphyrin IX, with apomyoglobin were formed and the resulting artificial myoglobins characterized. 3. Very little complex-formation was obtained with nickel, cobalt and manganese metalloporphyrins and apomyoglobin. 4. Myoglobin prepared with copper metalloporphyrin was immunochemically identical with native ferrimyoglobin. All the other artificial myoglobins were less reactive to varying degrees. 5. The changes in antigenic reactivities were attributed to conformational reorganization caused by the different co-ordination tendencies of the various metals or by the modification of the side chains of the haem.

Animals↗
PubMed1970

Comparison of immunoadsorbents prepared by coupling sperm-whale myoglobin to a variety of insoluble polymers.

Immunoadsorbents that were potentially suitable for the fractionation of antibodies to myoglobin were prepared by coupling myoglobin to aminoethylcellulose, bromoacetylcellulose, CM-cellulose, an ethylene-maleic anhydride co-polymer and Sepharose 4B. A comparison of the properties of the preparations indicated that Sepharose-myoglobin was superior, as an immunoadsorbent, to the other conjugates. Elution of adsorbed antibodies with m-propionic acid, pH2.5, gave yields of precipitable antibody higher than those achieved with other dissociating solvents. Propionic acid eluted 60-100% of the antibody adsorbed by Sepharose-myoglobin, and 60-90% of the eluted protein was precipitable antibody.

Adsorption↗