| Research Abstract |
Our research aimed to purify placental aminopeptidase, to show their involvement in the metabolization and degradation of bioactive peptides possibly devited from the fetus, and to show their clinical application for placental function test.
The following are the 7 aminopeptidases that we purified: P-LAP(oxytocinase),aminopeptidase M,Angiotensin-converting enzyme(kininase II),Aminopeptidase A,Kininase I (carborypeptidase N),Dipeptidyl peptidase IV,Post-proline endopeptidase, aminopeptidase B.
Degradation of bioactive peptides by high purified placental aminopeptidases was studied using HPLC. Our study showed the aminopeptidases in pregnancy serum and placenta, which degrade oxytocin,vasopressin,angiotensin II and III,bradykinin,endogenous opioids,tuftsin,thymopentin and splenopentin. Pregnancy serum aminopeptidase activities are known to increase during pregnancy. However, their physiological significance is not completely known. Our study showed the aminopeptidases in pregrancy serum responsible for degradation of oxytocin,angiotensin and buradykinin etc.
We showed possible clinical use of these aminopeptidases as a placental function test.
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