Multiple binding sites of [3H]clonidine on hepatic plasma membranes.
The binding of [3H]clonidine on mouse liver plasma membrane was a rapid, saturable and reversible process. It was characterized by two types of population: high affinity receptors with KD of 6.76 +/- 1.02 nM and Bmax of 106.15 +/- 24.05 fmol/mg protein, and low affinity receptors with KD of 63.66 +/- 12.85 nM and Bmax of 818.06 +/- 128.49 fmol/mg protein. Displacement of [3H]clonidine from its binding sites by various ligands indicated that alpha 1--as well as alpha 2--adrenoceptors were involved in the high affinity system. The respective participation of these two types of receptors was discussed.
D000316:Adrenergic alpha-Agonists / Q000494:pharmacology; D000317:Adrenergic alpha-Antagonists / Q000494:pharmacology; D000818:Animals; D001667:Binding, Competitive; D002462:Cell Membrane / Q000378:metabolism; D054755:Imidazoline Receptors; D066298:In Vitro Techniques; D007700:Kinetics; D008099:Liver / Q000378:metabolism*; D008297:Male; D051379:Mice; D011942:Receptors, Adrenergic, alpha / Q000378:metabolism; D018341:Receptors, Adrenergic, alpha-2
D000316:Adrenergic alpha-Agonists; D000317:Adrenergic alpha-Antagonists; D054755:Imidazoline Receptors; D011942:Receptors, Adrenergic, alpha; D018341:Receptors, Adrenergic, alpha-2