Okuyama T, Ishiura S, Villee C A
Placenta. 1986 Jan-Feb;7(1):43-9. doi: 10.1016/s0143-4004(86)80016-9.
The 30 000 g precipitate of homogenized rat placenta was incubated with 32P-adenosine triphosphate (ATP); several endogenous proteins were specifically phosphorylated in the presence of 0.5 mM calcium and phosphatidylserine (105K protein at mid pregnancy, and 78K protein at the latter part of pregnancy). The calcium- and phospholipid-dependent protein kinase activity in the 30 000 g precipitate was six times greater than the activity in the supernatant fraction. The total protein kinase C activity in the precipitate was considerably greater at the end of pregnancy than it was at mid pregnancy. Diethylaminoethyl cellulose-purified membrane-bound protein kinase C was slightly inhibited by inhibitors of lipoxygenase, NDGA or ETYA, but not by SHAM or BW755C. Haemin and polylysine strongly inhibited this activity.
将匀浆后的大鼠胎盘30000g沉淀与32P - 三磷酸腺苷（ATP）一起孵育；在存在0.5mM钙和磷脂酰丝氨酸的情况下，几种内源性蛋白质发生了特异性磷酸化（妊娠中期为105K蛋白，妊娠后期为78K蛋白）。30000g沉淀中的钙和磷脂依赖性蛋白激酶活性比上清液部分的活性高六倍。沉淀中的总蛋白激酶C活性在妊娠末期比妊娠中期显著更高。用二乙氨基乙基纤维素纯化的膜结合蛋白激酶C受到脂氧合酶抑制剂NDGA或ETYA的轻微抑制，但不受SHAM或BW755C的抑制。血红素和聚赖氨酸强烈抑制这种活性。
