Characterization of specific binding sites for corticosterone in mouse liver plasma membrane
| Autor: | Miguel Trueba, M. J. Sancho, Iñaki Ibarrola, Jose M. Macarulla, Ana Isabel Vallejo, Aida Marino |
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| Rok vydání: | 1989 |
| Předmět: |
Male
Receptors Steroid medicine.medical_treatment Biology Biochemistry Binding Competitive Steroid chemistry.chemical_compound Mice Receptors Glucocorticoid Cell surface receptor Corticosterone medicine Animals Corticosterone binding Binding site Receptor Phentolamine Binding Sites Cell Membrane Propranolol Steroid hormone Kinetics Membrane chemistry Liver |
| Zdroj: | Membrane biochemistry. 8(4) |
| ISSN: | 0149-046X |
| Popis: | The specific binding of [3H]corticosterone to mouse liver purified plasma membrane fractions is a saturable, reversible, and temperature-dependent process. Only one type of independent and equivalent binding sites has been determined in plasma membrane (Kd = 4.1 nM and Bmax = 3368 fmol/mg). As can be deduced from displacement data obtained in plasma membrane, the high-affinity binding site is different from nuclear glucocorticoid, nuclear progesterone, and Na+, K(+)-ATPase digitalis receptors. Probably this corticosterone binding site or receptor is the same one determined previously for [3H]cortisol in mouse liver plasma membrane. Such beta- and alpha-adrenergic antagonists as propranolol and phentolamine did not affect [3H]corticosterone binding to plasma membranes; therefore, this binding site is independent of these receptors. The binding sites in plasma membranes are not exclusive for corticosterone, but other steroids are also bound with very different affinities. |
| Databáze: | OpenAIRE |
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