Separation of "estrogen-induced" protein from phosphoprotein phosphatase activity of immature rat uterus.
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.
D000818:Animals; D003600:Cytosol / Q000187:drug effects / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D004958:Estradiol / Q000494:pharmacology*; D005260:Female; D008297:Male; D009132:Muscles / Q000201:enzymology; D010750:Phosphoproteins / Q000096:biosynthesis / Q000378:metabolism*; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D011479:Protamines; D011494:Protein Kinases; D051381:Rats; D014599:Uterus / Q000187:drug effects / Q000378:metabolism*
D010750:Phosphoproteins; D011479:Protamines; D004958:Estradiol; D011494:Protein Kinases; D010744:Phosphoric Monoester Hydrolases