Isolation and structures of xenopsin-related peptides from rat stomach, liver and brain.
Using radioimmunoassay for detection, a mammalian counterpart to amphibian xenopsin (XP) was isolated and sequenced from pepsin-treated extracts of three different rat tissues and shown to be H-Phe-His-Pro-Lys-Arg-Pro-Trp-Ile-Leu-OH. This peptide, which shares six of the eight residues in XP, existed primarily in large molecular form(s) in the rat from which it could be liberated by the enzyme, pepsin. The XP-related sequence was differentially distributed through tissues, with concentrations ranging from ca. 80 pmol/g in diaphragm and skeletal muscle to ca. 800 pmol/g in stomach, liver and intestine. Like XP, the mammalian peptide potently crossreacted in a radioreceptor assay for neurotensin. These results prove the existence of radioreceptor-active XP-related sequences in multiple tissues of the rat.
Carraway
R E
RE
Department of Physiology, University of Massachusetts Medical Center, Worcester 01655.
Mitra
S P
SP
Muraki
K
K
D000595:Amino Acid Sequence; D000818:Animals; D001923:Brain Chemistry; D008099:Liver / Q000737:chemistry*; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000032:analysis / Q000302:isolation & purification*; D010455:Peptides; D011863:Radioimmunoassay; D051381:Rats; D013270:Stomach / Q000737:chemistry*; D029867:Xenopus Proteins
D009842:Oligopeptides; D010455:Peptides; D029867:Xenopus Proteins; C016832:xenopsin