Journal article
Purification of chick oviduct progesterone receptor apoprotein
Abstract
The 8S progesterone receptor from chick oviduct has been partially purified (500-fold) as the apoprotein lacking hormone. The procedure employs polyethylene glycol precipitation, phosphocellulose, DNA cellulose, DEAE cellulose, hydroxylapatite and ethyl agarose column chromatography. As shown for the native cytosolic receptor, the purified apoprotein can be dissociated into A and B subunits. Qualitative and quantitative analysis of subunit …
Authors
Maggi A; Compton JG; Fahnestock M; Schrader WT; O'malley BW
Journal
The Journal of Steroid Biochemistry and Molecular Biology, Vol. 15, , pp. 63–68
Publisher
Elsevier
Publication Date
December 1981
DOI
10.1016/0022-4731(81)90259-4
ISSN
0960-0760