Purification and characterization of 1,25(OH)2D3 receptor from human placenta.
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.


CONCLUSIONS
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.
Tanamura
A
A
Department of Obstetrics and Gynecology, Nagoya University School of Medicine, Japan.
Nomura
S
S
Kurauchi
O
O
Furui
T
T
Mizutani
S
S
Tomoda
Y
Y
D005260:Female; D006801:Humans; D008970:Molecular Weight; D010920:Placenta / Q000737:chemistry*; D012333:RNA, Messenger / Q000302:isolation & purification; D018167:Receptors, Calcitriol / Q000302:isolation & purification* / Q000378:metabolism
D012333:RNA, Messenger; D018167:Receptors, Calcitriol