Identification of human placental leucine aminopeptidase as oxytocinase.
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Tsujimoto M, Mizutani S, Adachi H, Kimura M, Nakazato H, Tomoda Y
Identification of human placental leucine aminopeptidase as oxytocinase.
Arch Biochem Biophys. 1992 Feb 1;292(2):388-92. doi: 10.1016/0003-9861(92)90007-j.
- PubMed ID
- 1731608 [ View in PubMed]
- Abstract
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.