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XB-ART-25775
Peptides 1990 Jan 01;114:747-52.
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Isolation and sequence of canine xenopsin and an extended fragment from its precursor.

Carraway RE , Mitra SP .


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).

PubMed ID: 2235681
Article link: Peptides
Grant support: [+]

Species referenced: Xenopus
Genes referenced: levi magainins pgla xt6l