Purification and Structural Characterization of Vasoactive Intestinal Polypeptide from the Trout and Bowfin

Yunxia W Lundberg, J. Michael Conlon

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

Vasoactive intestinal polypeptide (VIP) was purified from extracts of the stomachs of the rainbow trout, Oncorhynchus mykiss, and bowfin, Amia calva. The primary structure of VIP from both species was the same: His-Ser-Asp-Ala-IIe-Phe-Thr-Asp-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 structure 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.

Original languageEnglish (US)
Pages (from-to)94-101
Number of pages8
JournalGeneral and Comparative Endocrinology
Volume98
Issue number1
DOIs
StatePublished - Jan 1 1995

Fingerprint

Amia calva
vasoactive intestinal peptide
Trout
Vasoactive Intestinal Peptide
trout
Oncorhynchus mykiss
Amiiformes
Salmoniformes
Rana clamitans
Alligators and Crocodiles
alligators
amino acid substitution
Amino Acid Substitution
Vertebrates
frogs
Amino Acid Sequence
Chickens
Stomach
stomach
amino acid sequences

ASJC Scopus subject areas

  • Endocrinology

Cite this

Purification and Structural Characterization of Vasoactive Intestinal Polypeptide from the Trout and Bowfin. / Lundberg, Yunxia W; Conlon, J. Michael.

In: General and Comparative Endocrinology, Vol. 98, No. 1, 01.01.1995, p. 94-101.

Research output: Contribution to journalArticle

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