Oestradiol stimulates tyrosine phosphorylation and hormone binding activity of its own receptor in a cell‐free system.

摘要: Recent experiments have shown that calf uterus oestrogen receptor exists in a tyrosine-phosphorylated hormone binding form and non-phosphorylated, non-hormone form. We report here physiological concentrations of oestradiol complex with the stimulate kinase converts into through phosphorylation on tyrosine. The activity this enzyme has been followed by reactivation sites tyrosine phosphatase-inactivated receptor. Phosphorylation demonstrated interaction 32P-phosphorylated proteins anti-receptor antibody either sucrose gradient centrifugation or SDS-PAGE immunoprecipitated proteins. Hormone stimulation is inhibited occupancy anti-oestrogen tamoxifen. Oestradiol-receptor increases affinity for dephosphorylated Findings are consistent observation several protein kinases associated peptide receptors stimulated to This first activation steroid hormone. finding hormones can regulate their own also new.