Characteristics of the corticosterone-receptor complex in rat liver cytosol.
Biochim Biophys Acta, 1976/6/15;434(2):483-9.
PMID: 182222
Abstract
Using a gel filtration on Sephadex G-150 in low ionic strength, it was possible to separate a corticosterone-binding protein in rat liver cytosol from corticosteroid-binding globulin after incubation of cytosol with [3H]corticosterone. The corticosterone-protein complex ("alpha-Complex") had a sedimentation coefficient of 8-9 S in low ionic strength. In high ionic strength, the alpha-Complex rapidly dissociated with a half-life of 15 h, compared to a half-life of 31 h for the hepatic dexamethasone-receptor complex under identical conditions (0 degrees C). The alpha-Compelx was saturable with an excess of unlabelled corticosterone of dexamethasone and was sensitive to heat and protease digestion. It is stressed that quantitation of the corticosterone-receptor complex must include separation of the receptor from corticosteroid-binding globulin as this protein binds corticosterone with high affinity and with a saturable amount of binding sites.
MeSH terms
Animals; Binding Sites; Binding, Competitive; Corticosterone; Cytosol; Dexamethasone; Kinetics; Liver; Male; Protein Binding; Proteins; Rats; Receptors, Cell Surface
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