Amino acid sequence of catfish pancreatic somatostatin I

Two peptides, pancreatic somatostatins I and II, larger and more acidic than synthetic tetradecapeptide somatostatin, have been purified from pancreatic islets of channel catfish (Ictalurus punctata). These peptides have reduced immunoreactivity in a radioimmunoassay for synthetic somatostatin, but...

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Bibliographic Details
Published in:The Journal of biological chemistry 1980-03, Vol.255 (6), p.2251-2254
Main Authors: Oyama, H, Bradshaw, R A, Bates, O J, Permutt, A
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Fishes
Hypothalamus - analysis
Organ Specificity
Pancreas - analysis
Peptide Fragments - analysis
Radioimmunoassay
Sheep
Somatostatin
Trypsin
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Summary:Two peptides, pancreatic somatostatins I and II, larger and more acidic than synthetic tetradecapeptide somatostatin, have been purified from pancreatic islets of channel catfish (Ictalurus punctata). These peptides have reduced immunoreactivity in a radioimmunoassay for synthetic somatostatin, but full biological activity was measured as inhibition of growth hormone released from isolated rat anterior pituitary cells. Pancreatic somatostatin I is composed of 22 amino acids. Eight additional amino acids are found as an NH2-terminal extension of the segment which is homologous to synthetic tetradecapeptide somatostatin. Seven of fourteen residues of tetradecapeptide somatostatin are present in the COOH-terminal portion of catfish pancreatic somatostatin I. The sequence is NH2-Asp-Asn-Thr-Val-Arg-Ser-Lys-Pro-Leu-Asn-Cys-Met-Asn-Tyr-Phe-Trp-Lys-Ser-Ser-Thr-Ala-Cys-COOH. There is considerable homology with the carboxyl end of synthetic tetradecapeptide somatostatin.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(19)85880-5