Purification and structural characterization of vasoactive intestinal polypeptide from the trout and bowfin.
Vasoactive intestinal polypeptide (VIP) was purified from extracts of the stomachs of the rainbow trout, Oncorhynchus mykiss, and the bowfin, Amia calva. The primary structure of VIP from both species was the same: His-Ser-Asp-Ala-Ile-Phe-Thr-Asp-Asn-Tyr10- Ser-Arg-Phe-Arg-Lys-Gln-Met-Ala-Val-Lys20-Lys-Tyr-Leu-Asn-Ser-Val- Leu-Thr. This amino acid sequence shows only one amino acid substitution (Val5-->Ile) compared with the common sequence of VIP from the chicken, alligator, and European green frog. The structural identity of VIP from the trout and bowfin is consistent with the close phylogenetic relationship between the Salmoniformes and the Amiiformes and the data indicate that pressure to conserve the complete primary structure of VIP during vertebrate evolution has been very strong.
Wang
Y
Y
Department of Biomedical Sciences, Creighton University School of Medicine, Omaha, Nebraska 68178, USA.
Conlon
J M
JM
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D005399:Fishes; D008969:Molecular Sequence Data; D017686:Oncorhynchus mykiss; D017421:Sequence Analysis; D017385:Sequence Homology; D013270:Stomach / Q000737:chemistry; D014660:Vasoactive Intestinal Peptide / Q000737:chemistry* / Q000302:isolation & purification*
D000596:Amino Acids; D014660:Vasoactive Intestinal Peptide