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. 1975 Jul;72(7):2631–2634. doi: 10.1073/pnas.72.7.2631

Separation of "estrogen-induced" protein from phosphoprotein phosphatase activity of immature rat uterus.

A M Kaye, M D Walker, D Sömjen
PMCID: PMC432823  PMID: 170609

Abstract

Preparations of the "induced protein" which appears in the rat uterus within 40 min of estradiol administration have recently been reported to contain phosphoprotein phosphatase (phosphoprotein phosphohydrolase, EC 3.1.3.16) activity. We found that these two proteins distribute differently on ammonium sulfate fractionation of uterine cytosol. Preparative cellulose acetate electrophoresis afforded complete (greater than 99.9%) separation of phosphoprotein phosphatase activity from the induced protein. The specific activity of phosphoprotein phosphatase in uterine cytosol was unchanged 1, 4, 12, or 24 hr after estradiol administration. These results are incompatible with the view that the induced protein mediates estrogen action by virtue of an inherent phosphoprotein phosphatase activity.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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