Open AccessStructure of the Porcine Vasoactive Intestinal Octacosapeptide
Author(s) -
Mutt Viktor,
Said Sami I.
Publication year - 1974
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1974.tb03373.x
Subject(s) - secretin , cyanogen bromide , vasoactive intestinal peptide , chemistry , glucagon , motilin , amino acid , biochemistry , leucine , secretin family , trypsin , peptide sequence , alanine , isoleucine , peptide , stereochemistry , biology , pancreas , endocrinology , enzyme , neuropeptide , receptor , hormone , gene
The amino acid sequence of the porcine vasoactive intestinal octacosapeptide is His‐Ser‐Asp‐Ala‐Val‐Phe‐Thr‐Asp‐Asn‐Tyr‐Thr‐Arg‐Leu‐Arg‐Lys‐Gln‐Met‐Ala‐Val‐L ys‐Lys‐Tyr‐Leu‐Asn‐Ser‐Ile‐Leu‐Asn‐NH 2 . Its amino acid residues 1, 2, 6 and 7, counted from the N‐terminus, are identical to those in the corresponding positions in both porcine glucagon and secretin. The residues in positions 3, 12, 13, 14 and 23 are identical to those in secretin, but not in glucagon, and position 10 is occupied by a tyrosyl and position 28 by an asparaginyl residue, like in glucagon but not in secretin. If in addition to identical amino acid residues also chemically similar residues, such as isoleucine in position 26 of the octacosapeptide, as compared to leucine in secretin and glucagon, are taken into consideration then the similarity between these three polypeptides is still more evident. At a more remote level there is some structural resemblance also between these peptides and the other four peptides from the intestinal wall, cholecystokinin‐pancreozymin, motilin, the gastric inhibitory peptide and substance P, the structures of which are known. The elucidation of the structure of the octacosapeptide was facilitated by the finding that pancreatic kallikrein preferentially cleaved only one of the three bonds in its N‐terminal cyanogen bromide heptadecapeptide that are susceptible to cleavage with trypsin.