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• W2038334945 abstract "Binding of [3H]dihydroergocryptine to platelet lysates appears to have all the characteristics of binding to α-adrenergic receptors. At 25°C binding reaches equilibrium within 20 min and is reversible upon addition of excess phentolamine. Binding is saturable with 183±22 fmol of [3H]dihydroergocryptine bound per mg of protein at saturation, corresponding to 220±26 sites per platelet. Kinetic and equilibrium studies indicate the dissociation constant of [3H]dihydroergocryptine for the receptors is 1-3 nM. The specificity of the binding sites is typical of an α-adrenergic receptor. Catecholamine agonists compete for occupancy of the [3H]dihydroergocryptine binding sites with an order of potency (−)epinephrine> (−)norepinephrine≫ (−)isoproterenol. Stereospecificity was demonstrated inasmuch as the (+)isomers of epinephrine and norepinephrine were 10-20-fold less potent than the (−)isomers. The potent α-adrenergic antagonists phentolamine, phenoxybenzamine, and yohimbine competed potently for the sites, whereas β-antagonists such as propranolol and dichlorisoproterenol were quite weak. Dopamine and serotonin competed only at high concentrations (0.1 mM)." @default.
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• W2038334945 date "1978-02-01" @default.
• W2038334945 modified "2023-09-27" @default.
• W2038334945 title "Identification of α-Adrenergic Receptors in Human Platelets by [3H]Dihydroergocryptine Binding" @default.
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• W2038334945 doi "https://doi.org/10.1172/jci108950" @default.
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