Chemical characterization of vasoactive intestinal polypeptide-like immunoreactivity in ovine hypothalamus and intestine.
Two forms of pituitary adenylate cyclase activating polypeptides with 38 (PACAP38) and 27 residues (PACAP27) respectively were recently isolated from ovine hypothalamic tissues. The N-terminal 28 amino acids sequence of PACAP was found to have 68% homology with porcine vasoactive intestinal peptide (VIP). In order to determine whether the primary structure of VIP of ovine hypothalamus is identical with porcine VIP or similar to PACAP, VIP immunoreactivity as determined by radioimmunoassay for porcine VIP was isolated in a pure form from ovine hypothalamic extracts. VIP was also isolated from ovine intestine. Amino acid analysis as well as amino acid sequence analysis showed that ovine hypothalamic and intestinal VIP were identical to porcine VIP, but different from PACAP.
Miyata
A
A
US-Japan Biomedical Research Laboratories, Tulane University Herbert Research Center, Belle Chase, LA 70037.
Jiang
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L
Stibbs
H H
HH
Arimura
A
A
D000262:Adenylyl Cyclases / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D002846:Chromatography, Affinity; D002852:Chromatography, Ion Exchange; D007031:Hypothalamus / Q000737:chemistry*; D007421:Intestine, Small / Q000737:chemistry*; D008969:Molecular Sequence Data; D011863:Radioimmunoassay; D016415:Sequence Alignment; D012756:Sheep; D013552:Swine; D014660:Vasoactive Intestinal Peptide / Q000737:chemistry*
D014660:Vasoactive Intestinal Peptide; D000262:Adenylyl Cyclases