Abstract
The amino acid sequences of both the alpha and beta subunits of porcine thyrotropin have been studied. Bovine thyrotropin primary structure was taken as a model for ordering the tryptic peptides of porcine thyrotropin. The amino acid sequence of the alpha subunit is identical to that of porcine luteinizing hormone, while oligosaccharide side-chains differ in composition. The primary structure of the beta subunit differs from that of bovine thyrotropin by six amino acid replacements, in positions 22, 24, 26, 36, 62 and 69, and by the absence of a methionyl residue at the carboxy terminus. Chemical evolutions of thyrotropin and luteinizing hormone are compared.
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