ABSTRACT
Calcitonin was originally identified as a factor having potent hypocalcemic actions. It is synthesized in the parafollicular cells of the thyroid gland of mammals and the ultimobranchial glands in lower vertebrates. The primary structure of calcitonin includes one residue of lysine and no residues of arginine. The structural gene for calcitonin was ligated so that the amino terminal residue of the mature peptide (cysteine) was separated from the fusion partner by a residue of arginine. The strategy utilized in this project was, therefore, to place an arginine residue as the bridge between the fusion partner and the amino terminal residue of the desired peptide product. Recombinant deoxyribonucleic acid technology promises to provide the most suitable and cost-effective approach for preparing peptides and proteins. The product, recombinant human calcitonin, was shown to elute from a reverse-phase high-pressure liquid chromatography column at the same position as authentic natural human-calcitonin.
