AMINO ACID SEQUENCE OF SALMON ULTIMOBRANCHIAL CALCITONIN

Abstract

Salmon ultimobranchial calcitonin has been isolated and rendered pure, as demonstrated by several chemical criteria. Its amino acid sequence was determined by means of manual Edman degradation of the intact molecule and of several peptide subfragments. Results of automated degradation provided confirmation of the structure. The salmon molecule possesses, in common with other calcitonins, a 32-amino acid peptide chain terminating in prolinamide and containing half-cystine residues at positions 1 and 7. Although the sequence of the salmon hormone differs considerably from that of the porcine, bovine and human calcitonins, the four hormones are homologous in 9 of 32 positions. The much higher biological potency possessed by the salmon calcitonin makes it of particular interest for future structure function studies.