Mulner-Lorillon O, Poulhe R, Cormier P, Labbe J C, Doree M, Belle R
Laboratoire de Physiologie de la Reproduction, INRA, UA CNRS 555, Université Pierre et Marie Curie, Paris, France.
FEBS Lett. 1989 Jul 17;251(1-2):219-24. doi: 10.1016/0014-5793(89)81458-9.
This paper describes the purification of a 47 kDa protein from Xenopus laevis oocytes that becomes phosphorylated when the oocytes undergo meiotic maturation. This protein (p47) is part of a high molecular mass complex containing at least two other proteins of molecular mass 30 and 36 kDa. This complex can be isolated from stage VI oocytes before maturation. We obtained a pattern for phosphopeptides in p47 phosphorylated in vivo very similar to that of the purified protein phosphorylated in vitro by p34cdc2 (a H1 kinase which is a component of the M-phase promoting factor) and [gamma-32P]ATP. Therefore, the purified p47, already described as a marker of MPF activity, is the first reported in vivo substrate for the cell division control kinase.
本文描述了从非洲爪蟾卵母细胞中纯化出一种47 kDa的蛋白质，当卵母细胞进行减数分裂成熟时，该蛋白质会发生磷酸化。这种蛋白质（p47）是一种高分子量复合物的一部分，该复合物至少还包含另外两种分子量分别为30 kDa和36 kDa的蛋白质。这种复合物可以在成熟前从VI期卵母细胞中分离出来。我们获得了体内磷酸化的p47中磷酸肽的模式，该模式与由p34cdc2（一种H1激酶，是M期促进因子的组成部分）和[γ-32P]ATP在体外磷酸化的纯化蛋白质的模式非常相似。因此，已被描述为MPF活性标志物的纯化p47，是首个被报道的细胞分裂控制激酶的体内底物。
