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    Arch Biochem Biophys. 1992 Feb 1;292(2):388-92.

    Identification of human placental leucine aminopeptidase as oxytocinase.

    Tsujimoto M, Mizutani S, Adachi H, Kimura M, Nakazato H, Tomoda Y.

    Source

    Suntory Institute for Biomedical Research, Osaka, Japan.

    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.

    PMID:
    1731608
    [PubMed - indexed for MEDLINE]

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