Solid-phase synthesis of sauvagine-(17-40).
The solid-phase synthesis of the tetracosapeptide corresponding to the C-terminal amino acid sequence of sauvagine is described. After purification by gel filtration, the polypeptide appeared to possess an acceptable degree of homogeneity, as judged by different kinds of electrophoresis and chromatography, and by automated Edman degradation analysis. Preliminary pharmacological results indicate that the fragment-(17-40) is practically devoid of any sauvagine activity on the circulatory system and endocrine glands; a weak effect on gastric emptying delay has been demonstrated (1% of the natural product).
D000595:Amino Acid Sequence; D029845:Amphibian Proteins; D000818:Animals; D003062:Codon; D003346:Corticotropin-Releasing Hormone / Q000235:genetics; D007202:Indicators and Reagents; D010446:Peptide Fragments / Q000138:chemical synthesis*; D036361:Peptide Hormones; D010455:Peptides / Q000138:chemical synthesis*; D012756:Sheep; D013329:Structure-Activity Relationship
D029845:Amphibian Proteins; D003062:Codon; D007202:Indicators and Reagents; D010446:Peptide Fragments; D036361:Peptide Hormones; D010455:Peptides; C025727:sauvagine; D003346:Corticotropin-Releasing Hormone