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Human myometrium contains alpha 3-adrenergic receptors which can be identified by binding of the alpha 2-adrenergic antagonist [3H]rauwolscine. Scatchard analysis of saturation binding data on myometrial membranes revealed that [3H]rauwolscine bound to a single class of noncooperative sites (262 +/- 89 fmol/mg of membrane protein) with high affinity (i.e., with an equilibrium dissociation constant of 5.3 +/- 2.2 nM). The alpha 2-adrenergic nature of these sites was derived from the order of potencies and stereospecificity of alpha-adrenergic agonists and antagonists to compete with [3H]rauwolscine binding.
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