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

Alvin M. Kaye | Zendy; Michael Walker | Zendy; Dalia Sömjen | Zendy

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

Author(s) -

Alvin M. Kaye,

Michael Walker,

Dalia Sömjen

Publication year - 1975

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.72.7.2631

Subject(s) - phosphoprotein , cytosol , phosphatase , uterus , biochemistry , protein phosphatase 2 , acid phosphatase , estrogen , chemistry , phosphorylation , biology , microbiology and biotechnology , endocrinology , enzyme

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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