Partial purification of the nuclear estrogen receptor from chicken liver by affinity chromatography.

The crude nuclear extract from the liver of estrogenized chickens contains 0.3-1 pmol/g tissue of the estrogen receptor. The receptor has been partially purified by ammonium sulphate precipitation and affinity chromatography on 17 beta-estradiol-17-hemisuccinyl-ovalbumin-Sepharose 4B. A 12% pure receptor preparation (2700-fold purification) with a yield of 17% could be obtained. The partially purified receptor has retained most properties which it displayed in cruder preparations, e.g. the dissociation constant of 10(-9)-10(-10) M, the hormone specificity and the sedimentation coefficient of 3.9 S. The size (Stokes radius, 2.9 nm; molecular weight, 49 000) and the asymetry (f/f0 = 1.10) of the receptor molecule, however, appear slightly reduced after the purification.