The isolation and chemical characterization of a novel vasoactive intestinal peptide-related peptide from a teleost fish, the cod, Gadus morhua.

An octacosapeptide that shows sequence homology to porcine vasoactive intestinal peptide (VIP) has been isolated from a teleost fish, the cod, Gadus morhua. The full primary sequence is His-Ser-Asp-Ala-Val-Phe-Thr-Asp-Asn-Tyr-Ser-Arg-Phe-Arg-Lys-Gln-Met-Ala-Ala- Lys-Lys-Tyr-Leu-Asn-Ser-Val-Leu-Ala. This peptide contains four, or five substitutions, compared with dogfish and porcine VIP, respectively. The residues in positions 13, 26 and 28 are different in all three species. These substitutions seem to have little effect on bioactivity, since cod VIP was virtually equipotent with porcine VIP in stimulating amylase release from guinea-pig pancreatic acini. During the isolation procedure an N-terminally modified form of VIP (Des-His, or 2-28 cod VIP) was also isolated. The available data suggest the sequence of VIP is well conserved in vertebrates which is consistent with an important biological role.