AMINO ACID SEQUENCE OF SALMON ULTIMOBRANCHIAL CALCITONIN
AUTOR(ES)
Niall, H. D.
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=223410Documentos Relacionados
- Phosphatydylglycerol promotes bilayer insertion of salmon calcitonin.
- Ultimobranchial gland of freshwater catfish, Heteropneustes fossilis, in response to calcitonin administration
- cDNA and deduced amino acid sequence of the Salmo salar (Atlantic salmon) adult hemoglobin alpha chain.
- Preparation and Characterization of Salmon Calcitonin–biotin Conjugates
- Down-regulation of rat kidney calcitonin receptors by salmon calcitonin infusion evidenced by autoradiography
