Isolation and sequence of canine xenopsin and an extended fragment from its precursor.
Canine xenopsin and a 27 residue segment of its precursor immediately surrounding the xenopsin moiety were isolated from acidic extracts of stomach. The six C-terminal residues of canine xenopsin, H-Phe-His-Pro-Lys-Arg-Pro-Trp-Ile-Leu-OH, were identical to those in Xenopus xenopsin less than Glu-Gly-Lys-Arg-Pro-Trp-Ile-Leu-OH. The amino acid sequence determined for the segment of the precursor was similar to the corresponding region of Xenopus pro-xenopsin (approximately 33% homology) and to the related Xenopus precursors, pro-levitide, pro-PGLa, pro-magainin and pro-caerulein. These results, indicating evolutionary conservation of xenopsin and a portion of its precursor, suggest that this peptide has important biologic function(s).
Carraway
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Department of Physiology, University of Massachusetts Medical Center, Worcester 01655.
Mitra
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D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D004285:Dogs; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry* / Q000302:isolation & purification; D010446:Peptide Fragments / Q000737:chemistry* / Q000302:isolation & purification; D010455:Peptides; D011498:Protein Precursors / Q000737:chemistry* / Q000302:isolation & purification; D011863:Radioimmunoassay; D012689:Sequence Homology, Nucleic Acid; D029867:Xenopus Proteins
D000596:Amino Acids; D009842:Oligopeptides; D010446:Peptide Fragments; D010455:Peptides; D011498:Protein Precursors; D029867:Xenopus Proteins; C016832:xenopsin