[Purification of the human prostate androgen receptor. I. Purification of the androgen receptor by affinity chromatography].

The androgen receptor (AR) was purified to establish a new method for measuring AR after producing the antibody for the purified AR. AR was purified from 1,700 g of benign prostatic hypertrophic tissue by combining affinity chromatography of heparin Sepharose CL-6B and of 17 alpha-carboxy-hexamethyl-17-hydroxy-4-androstane-3-one Sepharose 4B. The final purification fraction had the high affinity, low capacity binding to 3H-R 1881 in the presence of 1,000-fold molar excess of triamcinolone acetonide with a dissociation constant of 2.3 nM, showing the binding specificity of AR. Polyacrylamide gel electrophoresis did not reveal any albumin or TeBG mixed in the final purification fraction. These results showed that AR was partially purified, even though the degree of purification was low, around 38 fold calculated by the binding capacity per mg protein.