Publication | Closed Access
Isolation from Porcine‐Intestinal Wall of a Vasoactive Octacosapeptide Related to Secretin and to Glucagon
525
Citations
15
References
1972
Year
Protein SecretionGastrointestinal PharmacologyGastroenterologySecretin‐like FashionPeptide ScienceDigestive TractGastrointestinal Peptide HormoneMolecular PharmacologySecretory GranulesMetabolic SignalingAnimal PhysiologyMolecular PhysiologyPorcine‐intestinal WallBiochemistrySystemic Smooth MuscleAmino Acid ResiduesEndocrinologyPharmacologyVasoactive Octacosapeptide RelatedPhysiologyGut BarrierMetabolismMedicine
A polypeptide composed of 28 amino acid residues has been isolated from porcine upper intestinal wall. In addition to exhibiting several biological activities which may be attributed to a relaxant effect on vascular and systemic smooth muscle it stimulates exocrine pancreatic secretion in a secretin‐like fashion, with an apparent efficiency, on a molar basis, of 5–10% of that of secretin and also gives rise to hyperglycaemia with about 30% of the efficiency of glucagon. Structurally it resembles secretin and glucagon in having a histidyl‐seryl sequence N‐terminally. Of the amino acid residues commonly occurring in mammalian proteins the residues of cysteine/cystine, glycine, proline and tryptophan are absent from it.
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