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  • Title: [Aminoacid-p-nitroanilides splitting activities in the mouse human placenta (author's transl)].
    Author: Unger T, Struck H.
    Journal: Arch Gynakol; 1977 Jul 08; 222(4):311-8. PubMed ID: 19006.
    Abstract:
    Proteolytic activities of human placental extract are determined with the aid of a sensitive micromethod, based upon the Bratton-Marshall-reaction, and aminoacid-p-nitroanilides as substrates. The activities are differentiated by using 19 substrates, by adding 10 effectors, and by incubating the assays within the pH-range from 6.0--8.4. Besides Oxitocinase- and Aminopeptidase-like activities, a very active neutral peptidase, so far unknown in human placenta, an acid peptidase, e.g. Cathepsin C or Dipeptide-aminopeptidase II, and some other enzymes, not yet indentified by us, are demonstrated.
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