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XB-ART-25852
Dev Biol 1990 Jun 01;1392:427-31. doi: 10.1016/0012-1606(90)90311-6.
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In vivo progesterone regulation of protein phosphatase activity in Xenopus oocytes.

Cormier P , Mulner-Lorillon O , Belle R .


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Exogenous beta casein, previously phosphorylated in vitro by protein kinase A and casein kinase II, was microinjected into Xenopus oocytes to monitor in vivo protein phosphatase activities. Phosphatase activities were 1.6 and 3.4 fmol/min/oocyte, respectively, for beta casein phosphorylated by casein kinase II and beta casein phosphorylated by protein kinase A. Progesterone induced an early decrease (35% after 10 min) in phosphatase activity restricted to the protein kinase A sites of beta casein.

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