Untersuchungen zur histochemischen Lokalisation der Leucin- und Cystinaminopeptidase (Oxytocinase) in der Placenta

Fractionation and characterization of cystine aminopeptidase (oxytocinase) and arylamidase of the human placenta

“…It has been confirmed that the inactivation is enzymic in nature. Various lines of evidence indicate that the syncytiotrophoblast is the site of placental oxytocinase (Page, 1946;Semm & Waidl, 1962;James, 1966;Seelig & Roemheld, 1969;Small & Watkins, 1975). Oxytocinase hydrolyses the peptide bond between N-terminal cystine and adjacent tyrosine, resulting in the loss of the biological effect of oxytocin.…”

Synthetic Oligopeptide Substrates Their Diagnostic Application in Blood Coagulation, Fibrinolysis, and Other Pathologic States

“…There is general agreement today that certain proteinases of placental origin in the serum or urine of pregnant women accurately reflect the devel opment and functional capability of the fetoplacental unit [180]. Two such proteinases, leucine aminopeptidase (LAP) and cysteine aminopeptidase (CAP), have been histochemically demonstrated [404] and isolated from human placenta [147]. As pregnancy progresses, the syncytiotrophoblast layer of the placenta releases increasing amounts of these two neutral proteinases.…”