Abstract

The androgen receptor from rat submandibular gland was transformed by exposure to ATP at 0°C. The transformed 4 S receptor converted to a higher molecular weight form in a low-salt glycerol gradient centrifugation when ATP was removed from the sample. The sedimentation coefficient of the converted receptor was similar in the absence or presence of 20 mM molybdate; 7.8 ± 0.5 S without molybdate and 7.6 ± 0.3 S with molybdate. However, the receptor converting in the presence of molybdate could markedly bind to DNA-cellulose, while an entity without molybdate could not. These results suggest that molybdate directly interacts with the DNA-binding domain on the 4 S androgen receptor and prevents this domain from being concealed by conversion in low-salt conditions.

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