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Query: UNIPROT:P01178 (oxytocin)
 15,767 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Oxytocinase (cystyl-aminopeptidase) [EC 3.4.11.3] was isolated from monkey placenta in a purified form by a six-step prodedure comprising extraction from monkey placenta homogenate, ammonium sulfate fractionation, repeated chromatography on hydroxylapatite, chromatography on a column of DEAE-cellulose and gel filtration on a column of Sephadex G-200. The purified enzyme showed a single band on polyacrylamide disc electrophoresis. Oxytocin was inactivated by this enzyme preparation. The enzyme hydrolyzed several aminoacyl-beta-naphthylamides. A terminal amino group was required for enzyme activity. The molecular weight of the purified enzyme was estimated to be 87,000 by gel filtration and 83,000 by sodium dodecyl sulfate gel electrophoresis. Other properties of the enzyme, the effects of metal ions and various chemical reagents on the enzyme activity, the pH optimum, and Km values for a number of aminoacyl-beta-naphthylamides were also examined.
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PMID:Purification and properties of oxytocinase (cystine amino-peptidase) from monkey placenta. 1 46

The authors studied the dynamics of natural substrates of neurohumoral origin (oxytocin and lysine-vasopressin) by the serum of pregnant and nonpregnant women in relation to the pH in the medium, within pH limits of 2.5 to 8. The values obtained in a polarographic study of depression of the complex oxytocin and lysine-vasopressin polarographic wave by pregnancy and non-pregnancy sera and the results of a parallel analysis of free amino acids of the inactivated substrates under the same conditions showed that, apart from deep degradation of the studied substrates at the optimum pH (5.5 minus 8), less pronounced degradation of the molecule at low pH values (3 minus 4,5), i.e. in a non-physiological blood medium, also occurred. On the basis of their results, the authors submit the hypothesis of the existence of oxytocinase isoenzymes and of the probable presence of several peptidases with overlapping specificity.
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PMID:The influence of pH in the medium on degradation of neurohormones by pregnancy serum. 23 51

1 Synthetic analogues of oxytocin and of lysine-vasopressin with an hydroxyl group in either the L ro D configuration replacing the primary amino group have been tested for biological activity.2 [1-(L-2-Hydroxy-3-mercaptopropanoic acid)] oxytocin ([L-Hmp(1)]oxytocin) was 1.5 to 2 times more potent than oxytocin on the rat uterus in situ, the rat mammary strip and the rat mammary gland in situ and 3 times more potent on the rat isolated uterus.3 The pressor activity of [1-(L-2-hydroxy-3-mercaptopropanoic acid)-8-lysine]vasopressin ([L-Hmp(1), Lys(8)] vasopressin) was 2.2 and the antidiuretic activity 2.1 times that of lysine-vasopressin.4 The [D-Hmp(1)] analogues of oxytocin and vasopressin were much less potent than the [L-Hmp(1)] analogues.5 The responses to oxytocin and its hydroxy analogues in vivo were qualitatively indistinguishable but the pressor and antidiuretic responses to the hydroxy analogues of lysine-vasopressin were prolonged compared with those to the parent hormone.6 The hydroxy analogues of oxytocin and lysine-vasopressin were not inactivated by pregnancy plasma oxytocinase.7 The results are discussed in relation to the importance of the primary amino group for the biological activity and metabolism of the neurohypophysial hormones.
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PMID:Hydroxy analogues of oxytocin and of lysine-vasopressin. 51 8

The oxytocinase levels have been tested prior to, during and after oxytocin challenge tests in 42 pregnant women. There was no relation between labour and the activity of the enzyme. There was no change in the activity during and after oxytocin infusion. Repeated challenge tests did not change these results. The use of the oxytocinase as a parameter of placental function is not influenced by oxytocin infusions.
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PMID:[The activity of L-cystine-aminopeptidase (oxytocinase) in the serum of pregnant women during intravenous application of oxytocin (author's transl)]. 73 20

In women during the third trimester of normal pregnancy and at labour the level of oxytocin and progesterone in plasma were determined by means of radioimmunoassay and the activity of oxytocinase was measured spectrophotometrically. The plasma oxytocin levels measured from the 25th week of pregnancy showed a gradual increase with the peak values at the 39th and 40th week. At labour, the oxytocin values remain at the same level as these found at the end of pregnancy. The increase in oxytocin levels at contractions compared to its values found between contractions was not statistically significant. Oxytocinase levels showed also an ascending character until the 38th week of pregnancy. Later, a decrease was found which continued until the termination of pregnancy. At labour, there was a decrease in progesterone level in plasma which was about at the limit of significance.
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PMID:Plasma oxytocin and oxytocinase levels in third trimester of pregnancy and at labour. 108 29

The hydrolysis of oxytocin by human placental subcellular fractions was studied in the presence of selective inhibitors by measuring liberated amino acids by high performance liquid chromatography (HPLC). Oxytocin degradation by microsomal and lysosomal fractions was inhibited by bestatin, amastatin and puromycin. The IC50 values of these inhibitors on oxytocin degradation by both fractions were similar to those of these inhibitors on the human placental aminopeptidase M measured by L-Leu-p-nitroanilide as a substrate (LAP activity), which we reported previously. However, purified aminopeptidase M from human placental microsomal fractions could not liberate any amino acid from oxytocin. Since phosphoramidon (1 mumol/l), a putative metalloendopeptidase inhibitor, and N-benzylcarbonyl-valyl-prolinal (Z-Val-prolinal) (14 mumol/l), a selective inhibitor of post-proline endopeptidase, could not significantly influence the degradation of oxytocin by either subcellular fractions, neither enzyme seems to be actively involved in oxytocin degradation. These results strongly suggested the existence of oxytocinase(s) other than the above three enzymes in microsomal and/or lysosomal fractions of human placenta.
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PMID:Degradation of oxytocin by the human placenta: effect of selective inhibitors. 135 23

1. Bothrops jararaca plasma or serum hydrolysed L-cystine-di-beta-naphthylamide (CNAse activity) at a degree comparable to that of plasma or serum in pregnant women. 2. In adult snakes, activity was less in males. It was not altered in pregnancy but increased after delivery, being higher at pH 6.4 (unspecific enzymes) than at pH 7.9 (true pregnant woman plasma oxytocinase). 3. Its optimum pH was 5.9, different from that of other known enzymes that hydrolyse the same substrate. 4. Bothrops jararaca plasma also hydrolysed vasopressin, oxytocin and vasotocin. 5. These hydrolysing activities were unexpected for an ovoviviparous reptile.
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PMID:Hydrolysis of L-cystine-di-beta-naphthylamide and neurohypophyseal peptides by the plasma of the snake Bothrops jararaca. 152 15

A technique for complete oxytocinase inhibition has been combined with a rapid serial sampling strategy to determine plasma oxytocin concentrations in twelve women during the early and late first stage and in eight women throughout the second stage of labour. The progress of labour is not related to an increase in oxytocin concentration, uterine contractions are not associated with changes in plasma oxytocin concentration and hypocontractile labour does not appear to be the result of a deficit of oxytocin. The majority of patients do not demonstrate an increase in plasma oxytocin concentration during the second stage of labour; however, a minority produce a large surge immediately before delivery. The results do not support a role for oxytocin during spontaneous labour unless uterine activity is controlled by extremely low plasma hormone concentrations or the uterus becomes sensitive to a constant oxytocin concentration.
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PMID:Plasma oxytocin during the first and second stages of spontaneous human labour. 162 87

Human placental leucine aminopeptidase (P-LAP) was purified from retroplacental serum for the first time by serial chromatography on columns of Matrex Blue A, DEAE-Sepharose CL-6B, phenyl-Sepharose 4B, chelating-Sepharose, and Sepharose CL-6B. The purified P-LAP was apparently homogeneous on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and the apparent molecular weight (Mr) was estimated to be 210,000. By comparing P-LAP activity with cystine aminopeptidase activity, we concluded that both activities were shared by the same molecule. We also examined the hydrolytic activity of P-LAP using naturally occurring peptide hormones and found that the enzyme hydrolyzed oxytocin, vasopressin, and angiotensin III. These results suggest that P-LAP shows oxytocinase activity and plays an important role in the regulation of the plasma level of these hormones during pregnancy.
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PMID:Identification of human placental leucine aminopeptidase as oxytocinase. 173 8

Serum oxytocic and oxytocinase activities were examined in 50 females with normal pregnancy and 50 with threatened abortion by using biological (oxytocin) and biochemical (oxytocinase) methods. The findings suggest that there is no regular changes in serum oxytocic activity in the course of pregnancy, whereas its oxytocinase activity significantly increases with pregnancy development. The females with threatened abortion showed the same values of serum oxytocic activity as those with normal pregnancy, but much lower oxytocinase activity. The assay of serum oxytocinase activity may be of diagnostic value when threatened abortion is suspected.
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PMID:[Serum oxytocin and oxytocinase activities in women during pregnancy]. 186 62


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