Abstract
The chicken intestinal 1 alpha, 25-dihydroxyvitamin D3 receptor-like protein has been purified to apparent homogeneity as determined by sodium dodecyl sulfate gel electrophoresis. The techniques employed for the purification include selective precipitation of the receptor by Polymin P (polyethyleneimine) and (NH4)2SO4 and batch adsorption to and selective elution from hydroxylapatite, followed by gel exclusion and DEAE-cellulose chromatography. Finally, the labeled receptor was eluted at a pH of approximately 6.0 on a chromatofocusing column. The protein was purified 6100-fold and the receptor was obtained in 9% yield.