Oxytocin is hydrolyzed by an enzyme in human placenta that is identical to the oxytocinase of pregnancy serum

Peptides. 1996;17(2):257-61. doi: 10.1016/0196-9781(95)02124-8.

Abstract

The hydrolysis of oxytocin (OT) by human placental subcellular fractions and pregnant sera was studied in the presence of bestatin, a potent inhibitor of aminopeptidases, and the antibody against pregnant serum oxyotocinase (P-LAP)(EC 3.4 11.3) by measuring liberated amino acids by high performance liquid chromatography (HPLC). Our immunotitration study and the effect of bastatin on the oxytocin-degrading protease showed that the initiating and responsible protease in oxyotocin degradation in human placenta and pregnant serum is P-LAP.

MeSH terms

  • Amino Acid Sequence
  • Chromatography, High Pressure Liquid
  • Cystinyl Aminopeptidase / blood*
  • Edetic Acid / pharmacology
  • Female
  • Humans
  • Hydrolysis
  • Leucine / analogs & derivatives
  • Leucine / pharmacology
  • Leucyl Aminopeptidase / metabolism
  • Lysosomes / enzymology
  • Microsomes / enzymology
  • Molecular Sequence Data
  • Oxytocin / metabolism*
  • Placenta / enzymology*
  • Pregnancy

Substances

  • Oxytocin
  • Edetic Acid
  • Leucyl Aminopeptidase
  • Cystinyl Aminopeptidase
  • Leucine
  • ubenimex