Open AccessPartial purification of a glucocorticoid receptor.
Author(s) -
Douglas Failla,
Gordon M. Tomkins,
Daniel V. Santi
Publication year - 1975
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.72.10.3849
Subject(s) - glucocorticoid receptor , chromatography , size exclusion chromatography , glucocorticoid , chemistry , agarose , receptor , elution , steroid , sepharose , yield (engineering) , biochemistry , biology , hormone , endocrinology , enzyme , materials science , metallurgy
A simple method for purification of the glucocorticoid receptor from hepatoma tissue culture cells has been developed. The procedure, which requires only about 24 hr, involves biospecific adsorption of the receptor to deoxycorticosterone derivatized agarose, elution with a glucocorticoid, and gel filtration. The receptor-steroid complex is obtained in 35-40% yield and is about 2000-fold purified. It possesses properties similar to those reported in crude extracts, including sedimentation coefficient in glycerol gradients and activation-dependent binding to nuclei.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom