The origin and distribution of oxytocinase

Page, Ernest W.; Titus, Mary Ann; Mohun, George; Glendening, Mary Beth

doi:10.1016/s0002-9378(16)36201-9

Cited by 92 publications

(19 citation statements)

References 17 publications

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“…The most convincing evidence was pre sented by Page et al [12], Using starch gel electrophoresis, they were able to demonstrate two bands with oxytocinase activity (CAPj and CAP2 bands) in pregnancy sera and placental extracts, whereas no such bands were detected in nonpregnancy and fetal sera. Sjohoi.m and Yman [17] showed that CAP, and CAP., represent two different conformational forms of a single enzyme, whose rate of migration is in a pH-dependent equi librium with each other.…”

mentioning

confidence: 88%

The Origin of Human Pregnancy Serum Oxytocmase

Oya¹,

Yoshino²,

Mizutani³

et al. 1974

Gynecol Obstet Invest

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Serial electrophoretic experiments concerning serum and placental oxytocinases were carried out with a direct staining method for cystine aminopeptidase activity. The pregnancy serum oxytocinase and the lysosomal oxytocinase in human placenta shared the same enzymatic characteristics, with regard to heat resistence, sensitivity to L-methionine inhibition and electrophoretic pattern. These similarities suggest that the possible site of production of pregnancy serum oxytocinase is the lysosomes of the placenta, from which the enzyme is released into maternal circulation during pregnancy. Absence of oxytocinase activity in fetal serum indicates that this enzyme does not leak into fetal circulation. The physiological significance of oxytocinase was discussed with special reference to the oxytocin-oxytocinase equilibrium during pregnancy and labor.

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mentioning

confidence: 88%

The Origin of Human Pregnancy Serum Oxytocmase

Oya¹,

Yoshino²,

Mizutani³

et al. 1974

Gynecol Obstet Invest

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“…According to Yman (17) its isoelectric point lies at pH 3.7, but can be raised to pH 4.5 by desialiation. In polyacrylamide electrophoresis one can detect -subject to the chosen test conditions -one or two bands which are named cystine aminopeptidase 1 and cystine aminopeptidase 2 (18,19).…”

Section: Discussionmentioning

confidence: 99%

Hydrolysis of Some Cystine Aminopeptidase and Aminopeptidase Substrates by Human Placental Enzymes after Isoelectric Focusing

Unger¹,

Struck²

1980

Clinical Chemistry and Laboratory Medicine

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“…The origin of the pregnancy enzymes (oxytocinase) is not known with certainty. Page et al (1961) claimed th at the placenta was the source, but Tuppy and II inlerberger (1964) and Beckman et al (1965) have produced evidence th at this is very unlikely.…”

Section: Discussionmentioning

confidence: 99%