Publication | Open Access
Primary structure of ovine hypothalamic somatostatin-28 and somatostatin-25.
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Citations
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References
1980
Year
Bioorganic ChemistryGastrointestinal Peptide HormoneMolecular PharmacologyProteomicsAnimal PhysiologyProtein ChemistryBiochemistryEndocrine MechanismNative PeptidesNervous SystemEndocrinologyPharmacologyTryptic PeptidesTrypsin DigestionPrimary StructureNatural SciencesPhysiologyMedicineEndocrine ResearchNeuropeptides
The primary structure of the NH2-terminally extended somatostatins isolated from ovine hypothalamic extracts, one containing 28 residues and the other 25, has been determined. The structure of somatostatin-28 is Ser-Ala-Asn-Ser-Asn-Pro-Ala-Met-Ala-Pro-Arg-Glu-Arg-Lys-Ala-Gly-Cys-Lys-Asn-Phe-Phe-Trp-Lys-Thr-Phe-Thr-Ser-Cys-OH; the shorter one, somatostatin-25, has the same sequence as somatostatin-28 except that the first three NH2-terminal residues are deleted. The two peptides as isolated were found to be oxidized at the methionine residue to the methionine sulfoxide. Their structures were established by subjecting the native peptides to direct sequence analysis in a Beckman 890C sequencer and identifying the released phenylthiohydantoin derivatives by high-performance liquid chromatography. Their structures were confirmed by trypsin digestion and isolation of all the tryptic peptides, followed by amino acid analysis of the tryptic fragments. Moreover, some of the tryptic peptides were matched with their respective synthetic replicates on high-performance liquid chromatography.
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