Abstract
The binding of 3H-clonidine to bovine brain coated vesicles was studied. The binding was reversible and saturable. Saturation studies revealed a one-site interaction: Kd was 8.7 nM and Bmax was 24.5 fmol/mg protein. Noradrenaline, yohimbine and phenoxybenzamine displaced 3H-clonidine binding from the binding sites at concentrations of 10(-7)-10(-4) M. The results indicate that the coated vesicles from the bovine cerebral cortex contain 3H-clonidine binding sites comparable to the low affinity sites of alpha 2-adrenergic receptors in bovine brain membranes.
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