Isolation and purification of avian parathyroid hormone using high performance liquid chromatography, and some of its...

A peptide has been extracted in acetic acid from the parathyroid glands of chicks (Gallus domesticus) raised on a vitamin D-deficient diet. The peptide was purified by gel filtration and high-performance liquid chromatography (HPLC). Its degree of purity was ascertained also by SDS-polyacrylamide gel electrophoresis. The avian hormone had the same SDS electrophoretic mobility as bovine parathyroid hormone (bPTH) and therefore a similar molecular weight. The avian peptide was lower than bPTH in basic amino acids and considerably higher in glycine. Evidence for the identity of the peptide as avian parathyroid hormone relies on its source, the similarity of its molecular weight to that of bPTH, and its high potency in stimulating cyclic AMP production in kidney cells in vitro and in vivo.