The binding properties of p-[125I]iodoclonidine [( 125I]PIC) to human platelet membranes and the functional characteristics of PIC are reported. [125I]PIC bound rapidly and reversibly to platelet membranes, with a first-order association rate constant (kon) at room temperature of 8.0 +/-
Imidazoline binding sites are labeled by [3H]clonidine (I1) or by [3H]idazoxan (I2). I2-sites are mitochondrial. The subcellular localization of I1-sites in brain is unknown. Crude membranes from bovine rostral ventrolateral medulla (RVLM) were further purified by discontinuous sucrose density gradient.
This study sought to identify and characterize subtypes of alpha 2-adrenoceptors in rabbit ciliary body. Radioligand binding assays were performed with the alpha 2-agonist ligand [125I]-p-iodoclonidine ([125I]PIC) and the antagonist ligand [3H]rauwolscine. Both [125I]PIC and [3H]rauwolscine bound to a single
The Journal of pharmacology and experimental therapeutics, 264(1), 172-182 (1993-01-01)
Both the hypotension and the sedation elicited by centrally acting antihypertensive agents are traditionally attributed to activation of alpha 2 adrenergic receptors. Second-generation centrally acting agents such as moxonidine are less sedating but retain antihypertensive efficacy. A novel receptor which
The Journal of pharmacology and experimental therapeutics, 267(3), 1493-1502 (1993-12-01)
Human platelets are shown to possess at least two high-affinity, imidazol(in)e-preferring binding sites that are pharmacologically distinct from alpha-2 adrenoceptors. These nonadrenergic sites were radiolabeled even in the presence of a 10 microM norepinephrine mask of alpha-2 adrenoceptors. Heterogeneity at
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