Ishiura S, Nojima M, Yamamoto T, Fuchiwaki T, Okuyama T, Furuya H, Sugita H
Int J Biochem. 1986;18(9):765-9. doi: 10.1016/0020-711x(86)90051-0.
A linoleic acid-sensitive protease, ingensin, was purified to homogeneity from human placenta. The physical properties of the placental ingensin were found to be very similar to those of skeletal muscle ingensin [Ishiura et al. (1985) FEBS Lett. 189, 119-123]. The purified ingensin was activated by linoleic acid and SDS. The linoleic acid-activated form was inhibited preferentially by divalent cations, whereas the SDS-activated form was inhibited by monovalent cations instead.
一种对亚油酸敏感的蛋白酶——孕蛋白酶,从人胎盘中纯化至同质。发现胎盘孕蛋白酶的物理性质与骨骼肌孕蛋白酶非常相似[石浦等人(1985年),《欧洲生物化学学会联合会快报》189,119 - 123]。纯化的孕蛋白酶可被亚油酸和十二烷基硫酸钠激活。亚油酸激活的形式优先被二价阳离子抑制,而十二烷基硫酸钠激活的形式则被单价阳离子抑制。