[Aminoacid-p-nitroanilides splitting activities in the mouse human placenta (author's transl)].
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.
D000596:Amino Acids / Q000378:metabolism; D000626:Aminopeptidases / Q000032:analysis; D002403:Cathepsins / Q000032:analysis; D010122:Cystinyl Aminopeptidase / Q000032:analysis; D010450:Endopeptidases / Q000032:analysis; D005260:Female; D006801:Humans; D006863:Hydrogen-Ion Concentration; D009574:Nitro Compounds / Q000378:metabolism; D010920:Placenta / Q000201:enzymology*; D011247:Pregnancy
D000596:Amino Acids; D009574:Nitro Compounds; D002403:Cathepsins; D010450:Endopeptidases; D000626:Aminopeptidases; D010122:Cystinyl Aminopeptidase
Aminosäure-p-Nitroanilide spaltende Enzymaktivitäten der reifen menschlichen Plazenta. I.