Oxytocin biotransformation in the rat limbic brain

Abstract

Two peptide fragments of oxytocin were isolated by high-pressure liquid chromatography from digests of oxytocin obtained after exposure to a SPM preparation of the rat limbic brain. The structures of these peptides, being Gln-Asn-Cys(O)x-Pro-Leu-GlyNH2 and Gln-Asn-Cys(-S-S-Cys)-Pro-Leu-GlyNH2, were assessed by quantitative amino acid analysis, combined with the determination of N-terminal end groups and cysteic acid residues after performic acid treatment. The fragments comprised the 4–9 and 1,4–9 sequences of oxytocin, respectively. The types of proteolytic enzymes involved in their formation are discussed and a pathway for the conversion of oxytocin by SPM is proposed.

SPM, synaptosomal plasma membrane(s); HPLC, high-pressure liquid chromatography; DNS-, dansyl-,1-dimethylaminonaphthalene-5-sulfonyl-