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Purification and characterization of 1,25(OH)2D3 receptor from human placenta
A Tanamura1, S Nomura, O Kurauchi
1Department of Obstetrics and Gynecology, Nagoya University School of Medicine, Japan.
Objective:
To characterize the receptor for 1,25-dihydroxycholecalciferol [1,25-(OH)2D3], we purified it from nuclear fractions of human placentae.
Methods:
Human placental fractions were concentrated with ammonium sulfate, extracted from hydroxylapatite, and then chromatographed on Sepharcryl S-200 and DEAE-cellulose.
Results:
The receptor for [1,25(OH)2D3] was purified approximately 1,500-fold. The molecular weight of the receptor was estimated to be 55 K dalton by gel filtration. The receptor fractions showed a dissociation constant (Kd) of 3.0 x 10(-10) mol/l, and adsorbed to the DNA cellulose column. D3 analogs, estradiol, and progesterone had almost no effect on 1,25(OH)2D3 binding.
Conclusion:
These properties of the 1,25(OH)2D3 receptor in human placenta are similar to those of the chicken intestinal 1,25(OH)2D3 receptor.
