Purification of Chicken Intestinal Receptor for 1 Alpha, 25-dihydroxyvitamin D3 to Apparent Homogeneity

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1982 Jan 1

PMID 6275386

Citations 8

Authors

R U Simpson

H F DeLuca

Affiliations

Soon will be listed here.

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.

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Quantitation of endogenously occupied and unoccupied binding sites for 1,25-dihydroxyvitamin D3 in rat intestine.

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Development of hybridomas secreting monoclonal antibodies to the chicken intestinal 1 alpha,25-dihydroxyvitamin D3 receptor.

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Subcellular distribution of DNA-binding and non-DNA-binding 1,25-dihydroxyvitamin D receptors in chicken intestine.

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