Abstract
The specific protein fraction induced by estradiol in the rat uterus (IP) was purified by selective acid precipitation, DEAE cellulose chromatography, Sephadex G200 filtration and preparative cellogel electrophoresis. The determination of specific phosphoprotein phosphatase activities and of the level of IP purification after the different preparation steps, confirmed Kaye's results and allowed to state that IP was not a phosphoprotein phosphatase. The purified IP preparation did not display any detectable protein kinase activity, nor estradiol complexing ability. The injection of cordycepin (3' deoxyadenosine), an inhibitor of poly A synthesis, inhibits the synthesis of IP. This fact suggests that one of the earliest effects of estrogen is the production of Hn-RNA poly-A relative to IP. Cordycepin does not greatly affect the increase in ribosomal RNA observed under the effect of estradiol. The blocking of IP by cordycepin and the lack of inhibition at the nucleolus level under the same conditions show that the two early effects of the action of estrogen on the immature rat uterus are not directly correlated.
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