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XB-ART-26635
FEBS Lett 1989 Jul 17;2511-2:219-24. doi: 10.1016/0014-5793(89)81458-9.
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Purification of a p47 phosphoprotein from Xenopus laevis oocytes and identification as an in vivo and in vitro p34cdc2 substrate.

Mulner-Lorillon O , Poulhe R , Cormier P , Labbe JC , Doree M , Belle R .


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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.

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Species referenced: Xenopus laevis
Genes referenced: cdk1 nsfl1c