Abstract
The nature of the 1,25-dihydroxyvitamin D 3 receptor from chick intestine was examined in regard to its response to sodium molybdate. Sodium molybdate (10 m m) stabilized the receptor from crude nuclear extract but not that from the supernatant or cytoplasmic fraction, suggesting the molybdate may act by binding to the DNA binding region of the receptor. At a concentration of 50 m m, sodium molybdate prevented aggregation of the nuclear receptor. This concentration of sodium molybdate also inhibited the receptor from binding to DNA cellulose while the same ionic strength KCl (90 m m) did not. These properties also suggest that molybdate interacts with the DNA binding region. Purification of the receptor using DNA cellulose chromatography has also been improved by using a sodium molybdate gradient (0–0.2 m) instead of the KCl gradient used previously.
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