A system for the partial purification of the human androgen receptor following reversible denaturation

Androgen receptors from normal human foreskins were partially purified by sequential phosphocellulose chromatography and affinity chromatography resulting in a 28,000-fold purification and an 81% recovery. SDS-electrophoresis of the partially purified receptor preparation demonstrated that binding activity could be recovered and showed two peaks of specific binding mol. wt 35,000-55,000 and 85,000-105,000). This method demonstrates that androgen receptors can withstand harsh denaturation conditions and should prove to be a valuable tool for purifying the human androgen receptor.