Partial purification of a glucocorticoid receptor.
AUTOR(ES)
Failla, D
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=433093Documentos Relacionados
- Somatomedin receptor of human placenta: solubilization, photolabeling, partial purification, and comparison with insulin receptor.
- Purification of a prolactin receptor.
- Purification of a putative brain somatostatin receptor.
- Monoclonal antibodies against the rat liver glucocorticoid receptor.
- An antiserum to the rat liver glucocorticoid receptor.