Aminopeptidases in human retroplacental sera: purification and characterization of two enzymes

Ten different maternal serum samples were analyzed for the hydrolysis of S-Bz-Cys-pNA (substrate for CAP) and Ala-pNA. The results showed clear differences in the activities in individual sera. Similar S-Bz-Cys-pNA hydrolysis activity was detected for all sera. However, Ala-pNA hydrolysis activity differed remarkably. Serum exhibiting low Ala-pNA hydrolysis activity contained only CAP, and that exhibiting high Ala-pNA hydrolyzing activity contained CAP and AAP. The two aminopeptidases were independently purified to a homogeneous state through the same purification procedures and some of their biochemical properties were compared. The enzymes were quite different with respect to molecular mass, the substrate specificities for some aminoacyl-pNA substrates, and the effects of inhibitors. Among various natural peptides tested for hydrolysis, the enzymes hydrolyzed Met-enkephalin most rapidly, but their modes of action were different. Furthermore, only CAP degraded oxytocin and AAP exhibited a high kinin-converting activity.