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  • Title: Isolation and sequence of canine xenopsin and an extended fragment from its precursor.
    Author: Carraway RE, Mitra SP.
    Journal: Peptides; 1990; 11(4):747-52. PubMed ID: 2235681.
    Abstract:
    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).
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