Inhibition of 3H-nitrendipine binding on rat aortic and cerebral cortex membranes by benidipine hydrochloride
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منابع مشابه
Binding of a calcium antagonist, [3H]nitrendipine, to high affinity sites in bovine aortic smooth muscle and canine cardiac membranes.
[(3)H]Nitrendipine, a potent calcium channel antagonist [3-ethyl-5-methyl-1-1,4-dihydro-2,6 - dimethyl - 4 - (3 - nitrophenyl) - 3,5 - pyridine carboxylate], was used to label high affinity binding sites on membranes prepared from bovine aortic smooth muscle. The binding of [(3)H]nitrendipine is rapid (t(1/2) < 5 min) and reversible at 37 degrees C. The binding sites have a high affinity for [(...
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Binding of the dihydropyridine calcium antagonist [3H]nitrendipine was studied in cardiac myocytes incubated in normal and high potassium buffer so that we might examine the voltage dependence of dihydropyridine binding. Hearts were obtained from adult male Wistar rats, and isolated calcium tolerant myocytes were dissociated by enzymatic dispersion. Cells in 5.6 mM extracellular potassium showe...
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Background: It has been suggested that organophosphates may inhibit gamma-aminobutyric acid (GABA) metabolism in synaptosomal preparations. In the present investigation, we have assessed the interaction between paraoxon and the GABA system at synaptic level. Methods: Synaptosomes were prepared from male Wistar rats (200-250 g). Cerebral cortex was dissected and homogenized, then centrifuged at ...
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[12-3H]Forskolin (27 Ci/mmol) has been used to study binding sites in rat brain tissue by using both centrifugation and filtration assays. The binding isotherm measured in the presence of 5 mM MgCl2 by using the centrifugation assay is described best by a two-site model: Kd1 = 15 nM, Bmax1 (maximal binding) = 270 fmol/mg of protein; Kd2 = 1.1 microM; Bmax2 = 4.2 pmol/mg of protein. Only the hig...
متن کاملCharacterization of [3H]phenobarbital binding to rat brain membranes.
The binding of [3H]phenobarbital to rat brain membranes was studied in order to determine its characteristics and specificity. The binding reaction was rapid and occurred at sites of low affinity. (Kd = 700 microM) and very high density (Bmax = 2.7 nmol/mg protein). It was unaffected by temperature changes from 0 degrees C to 95 degrees C and was maximal at pH 5. Detergents in low concentration...
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ژورنال
عنوان ژورنال: Japanese Journal of Pharmacology
سال: 1989
ISSN: 0021-5198
DOI: 10.1016/s0021-5198(19)56570-2