Abstract
We have prepared a new affinity chromatography reagent, 17α-epoxypropyl-dihydro-testosterone linked to Thiopropyl-Sepharose, with potential for use in purification of androgen receptor and other specific androgen binding proteins. The linkage is stable, and the ligand has reasonably high affinity for the receptor. Starting with 5α-androstane-3β-ol-17-one, we synthesized in two steps 17α-allyl-dihydrotestosterone, which was then oxidized to 17α-epoxypropyl-DHT yielding 2 diastereomers in about a 4:1 ratio. The 17α-allyl-DHT had about 50% of DHT's affinity for rat uterine androgen receptor, while the affinity of the major epoxide isomer was 9% and that of the minor isomer was 4%. Reaction of the epoxides with Thiopropyl-Sepharose-6B gave about 7 μ mol of covalently bound DHT per ml of beads. These beads took up 83% of the androgen receptor from a rat uterine cytosol in a preliminary study, which more than equalled the performance of identically prepared estradiol beads successfully used for estrogen receptor purification. The use of the new DHT beads in purifications of the androgen receptor and other binding proteins is now being explored by other laboratories.
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