Abstract
The turtle, Pseudemus seripta, synthesizes an agglutinin antibody against Salmonella typhosa ‘H’ antigen that is confined to the macroglobulin component of whole serum. This immune macroglobulin was purified and found to have a molecular weight of 850,000. It had a total carbohydrate content of 6·7 per cent and amannose to galactose ratio different from that of human immunoglobulins. Following extensive reduction and alkylation, the molecule was dissociated into heavy and light chains which upon purification were found to have molecular weights of ≈67,000 and ≈22,500 respectively. The amino acid composition as well as certain properties of the molecule were similar to mammalian IgM. A free N-terminal residue could not be demonstrated for either the heavy or light chain. Examination by electron microscopy revealed a pentameric molecular structure. These data indicate a phylogenetic relationship among immune macroglobulins of several species and these implications are discussed.
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