ADPase activity in human maternal and cord blood: possible evidence for a placenta-specific vascular protective mechanism.
ADPase enzyme activity was assessed in maternal and cord plasma by adding radiolabelled ADP and quantitating the degradation products. Cord plasma had sufficiently greater ADPase activity than the corresponding maternal plasma obtained ante- and post-partum. Thus, residual radiolabelled ADP was 30, 32 and 17% of total radioactivity after 30 min incubation (37 degrees C) in maternal ante-partum, maternal post-partum and cord plasmas, respectively. ADPase may act as a platelet aggregation inhibitor in the placental and fetal circulation.
Barradas
M A
MA
Department of Chemical Pathology and Human Metabolism, Royal Free Hospital, London, UK.
Mikhailidis
D P
DP
Dandona
P
P
D001081:Apyrase / Q000097:blood* / Q000502:physiology; D005230:Fatty Acids, Nonesterified / Q000097:blood; D005260:Female; D005312:Fetal Blood / Q000032:analysis*; D006801:Humans; D010744:Phosphoric Monoester Hydrolases / Q000097:blood*; D010974:Platelet Aggregation; D011247:Pregnancy / Q000097:blood*; D011249:Pregnancy Complications, Cardiovascular / Q000209:etiology; D013927:Thrombosis / Q000209:etiology
D005230:Fatty Acids, Nonesterified; D010744:Phosphoric Monoester Hydrolases; D001081:Apyrase