Aminopeptidase A in human placenta and pregnant serum

Abstract The activities of serum aminopeptidases (APs) derived from the placenta rise during pregnancy. To confirm the localization of AP-A, which liberates N-terminal acidic amino acids, in placental tissue and to identify it in the serum of pregnant women, Chromatographic separation was performed. When a placental extract was subjected to DEAE cellulose column chromatography, the Glu-MCA degradative activity, or AP-A, was separated into two entities. Inhibition testing revealed that the enzyme eluted in Fraction No. 20 from the DEAE-cellulose column consisted of typical AP-A with a molecular weight of approximately 500 000. When the Glu-MCA degradative activity was observed by filtering pregnant serum through HPLC TSK G3000 gel, the activity was found to be due to serum CAP rather than AP-A. What had been thought to be a biochemicophysiological action inherent in blood AP-A raised additional questions.