Chaudhuri D, Kushari J, Mukherjea M
Eur J Obstet Gynecol Reprod Biol. 1982 Aug;13(5):309-16. doi: 10.1016/0028-2243(82)90054-5.
The presence of phosphodiesterase IV has been demonstrated in the human fetal brain, liver and placenta as early as in the 6th week of intrauterine development. The enzyme activity in each tissue increases with gestation, being maximum at 18-21 wk and then decreases. The Km values of this enzyme for bis-(p-nitrophenyl)-phosphate hydrolysis in the brain, liver and placenta are 2.94 mM, 1.47 mM and 1.66 mM, respectively. Presence of sulfhydryl group in the active center of the placental enzyme has been demonstrated with the help of cationic study. EDTA inhibits the enzyme in all three tissues. Effect of concanavalin A reveals the absence or unexposition of glucose, mannose and N-acetylglucosamine moieties in the active site of the enzyme in each of the three tissues. Maximum enzyme activity has been found to be localized in the soluble supernatant fraction obtained on centrifuging the brain and liver homogenate at 105,000 x g and in 20,000 x g pellet of the placenta.
早在子宫内发育的第6周,就已证实在人类胎儿大脑、肝脏和胎盘中存在磷酸二酯酶IV。每个组织中的酶活性随孕期增加,在18 - 21周时达到最高,然后下降。该酶在大脑、肝脏和胎盘中水解双(对硝基苯基)磷酸酯的Km值分别为2.94 mM、1.47 mM和1.66 mM。通过阳离子研究已证实在胎盘酶的活性中心存在巯基。EDTA在所有三种组织中均抑制该酶。伴刀豆球蛋白A的作用表明,在这三种组织的每一种中,该酶的活性位点均不存在或未暴露葡萄糖、甘露糖和N - 乙酰葡糖胺部分。已发现最大酶活性定位于在105,000 x g离心大脑和肝脏匀浆获得的可溶性上清液部分以及胎盘中20,000 x g的沉淀中。