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D H Copp

Publications and source records attributed to D H Copp.

At least 55 records · Page 3Linked to original sources

Amino acid sequence of salmon ultimobranchial calcitonin.

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.

Amino Acid Sequence↗

Calcitonin.

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Amino Acids↗

Calcitonin from ultimobranchial glands of dogfish and chickens.

Acid extracts of thyroid glands from a small shark Squalus suckleyi and domestic fowl Gallus domestica contained no detectable calcitonin activity, while very potent hypocalcemic responses were obtained in rats with similar extracts from the ultimobranchial glands of these two species. The calcitonin concentration was 4 to 40 times that present in hog thyroid, which, as in most other mammals, contains ultimobranchial tissue. The evidence suggests that calcitonin is a fundamental calcium-regulating hormone present in all higher vertebrates and that it is an ultimobranchial rather than a thyroid hormone. It also indicates an important and hitherto unrecognized function for the ultimobranchial glands.

Animals↗