Proceedings: Separation of the "estrogen-induced protein" from phosphoprotein phosphatase activity of immature rat uteri.

A. M. Kaye, M. D. Walker, D. Sömjen

Research output: Contribution to journalArticlepeer-review

Abstract

The distribution of phosphoprotein phosphatase (PPPase) and estrogen-induced protein (IP) from 19- to 20-day-old rat uteri before and after fractionation of uterine cytosol, by ammonium sulfate, and by preparative cellulose acetate gel electrophoresis was studied. There was a lack of significant difference between the specific activity of PPPase or its electrophoretic mobility in control extracts and those of extracts made 1 hour after injection of the rats with 5 mcg estradiol-17beta. Most of the recovered PPPase activity appeared in the fraction precipitating between 0-50% saturation with ammonium sulfate. Most of the IP is found at 50-80% saturation, and less than 10% of the PPPase activity. A single peak of PPPase activity was shown at a mobility of .5 relative to bovine serum albumin with electrophoresis of the 50-80% ammonium sulfate fraction. A peak of IP with mobility of 1.2 was also shown. ''The results are incompatible with the view that IP mediates estrogen action by virtue of its PPPase activity.''.

Original languageEnglish
Pages (from-to)1177
Number of pages1
JournalIsrael Journal of Medical Sciences
Volume11
Issue number11
StatePublished - Nov 1975

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