Characteristics of the calf uterine androgen receptor.

The highest molecular weight form of the calf uterine androgen receptor separates as an 11S form in glycerol gradients. This "cytosolic" receptor, prepared in the presence of molybdate, polyethyleneimide and low ionic strength, dissociates into 9S and 7.2S forms with increasing KCl concentration. A 4.5S androgen binding component appears as the predominant form of the receptor in the absence of polyethyleneimide and this unit quantitatively converts to a stable 3.5S form in the absence of molybdate. Renaturation of partially purified protein, separated by SDS-PAGE electrophoresis, demonstrates the presence of an androgen binding component in the 110 kDa region of the gel. This renatured protein separates as a 4.5S component in glycerol gradients and has a Stokes radius of 6 nm. Photoaffinity labelling of partially purified receptor preparations, followed by SDS-PAGE electrophoresis, reveals the presence of an androgen binding component having a molecular weight of 115 kDa. The binding characteristics and specificity of the receptor binding to R1881 have been studied and a DHT-affinity chromatography resin used to purify the receptor.