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 +/-
The Journal of pharmacology and experimental therapeutics, 279(2), 694-702 (1996-11-01)
To identify selective compounds for nonadrenergic I1-imidazoline receptors (I1), the affinities of 22 ligands for [125I]p-iodoclonidine binding have been compared at human platelet I1-imidazoline binding sites (analyzed under norepinephrine mask of alpha-2 AR) and at human alpha-2A, alpha-2B and alpha-2C
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.
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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