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- W2067317358 abstract "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." @default.
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- W2067317358 date "1990-06-01" @default.
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- W2067317358 title "In vivo progesterone regulation of protein phosphatase activity in Xenopus oocytes" @default.
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- W2067317358 doi "https://doi.org/10.1016/0012-1606(90)90311-6" @default.
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