Direct evidence is presented that uterus 17β-estradiol receptor is phosphorylated in, vitro by an endogenous kinase. Nuclear phosphatase, cytosol Ca2+-stimulated kinase (the former inactivating and the latter reactivating the hormone binding of the 17β-estradiol receptor) and receptor were purified from calf uterus. 17β-estradiol binding was inactivated by phosphatase, then reactivated by kinase in the presence of [γ-32P] ATP, Ca2+ and calmodulin, and the receptor was examined by various methods. The results of gel electrophoresis in non denaturating and denaturating conditions, and of centrifugation through sucrose gradients of receptor preincubated with monoclonal antibodies showed that the receptor is phosphorylated.
|Number of pages||9|
|Journal||Biochemical and Biophysical Research Communications|
|Publication status||Published - Dec 15 1982|
ASJC Scopus subject areas
- Molecular Biology