Isolation and characterization of a variant form of vasoactive intestinal polypeptide.
A variant form of the vasoactive intestinal polypeptide (VIP) has been isolated. It was found to consist of a molecule which instead of the C-terminal asparagine amide of VIP has a C-terminal extension of Gly-Lys-Arg. This VIP variant displaces VIP in a VIP receptor assay, reacts with N-terminally-directed antisera in a VIP radioimmunoassay and possesses VIP-like bioactivity in an assay measuring pancreatic juice secretion in the cat.
Gafvelin
G
G
Department of Biochemistry II and Chemistry I, Karolinska Institute, Stockholm, Sweden.
Andersson
M
M
Dimaline
R
R
Jörnvall
H
H
Mutt
V
V
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001667:Binding, Competitive; D002415:Cats; D002462:Cell Membrane; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D014644:Genetic Variation; D008099:Liver / Q000378:metabolism; D010189:Pancreatic Juice / Q000187:drug effects / Q000378:metabolism; D051381:Rats; D011964:Receptors, Gastrointestinal Hormone / Q000378:metabolism; D018005:Receptors, Vasoactive Intestinal Peptide; D014660:Vasoactive Intestinal Peptide / Q000302:isolation & purification* / Q000378:metabolism / Q000494:pharmacology
D000596:Amino Acids; D011964:Receptors, Gastrointestinal Hormone; D018005:Receptors, Vasoactive Intestinal Peptide; D014660:Vasoactive Intestinal Peptide