| pubmed-article:6316168 | pubmed:abstractText | When attempting to characterize the nature of adrenoceptors in bovine pial arteries, we found specific 3H-yohimbine binding was saturable, reversible and of high affinity (KD = 18.3 +/- 1.2 nM) with a Bmax of 687 +/- 27 fmol/mg protein (N = 4). On the other hand, there was no specific 3H-prazosin binding in these tissues. Scatchard and Hill plot analyses of specific 3H-yohimbine binding indicated one class of binding sites. From kinetic analyses of the data, association and dissociation rate constants of 1.6 +/- 0.3 X 10(7) M-1min-1 and 0.51 +/- 0.04 min-1, respectively, were calculated (N = 3). The dissociation constant from the equation KD = K-1/K+1 was 35.7 +/- 7.6 nM, such being in good agreement with the KD value estimated from Scatchard plots. Specific binding of 3H-yohimbine was displaced effectively by alpha 2 adrenergic agents and less effectively by alpha 1 adrenergic agents or beta adrenergic agents. Ki values for adrenergic drugs of 3H-yohimbine binding were as follows: yohimbine, 25 nM; clonidine, 260 nM; methoxamine, 6.8 microM; propranolol, 8.7 microM; prazosin, 21 microM; phenylephrine, 22 microM; noradrenaline, 27 microM; adrenaline, 66 microM; isoproterenol, 3,300 microM. These results indicate that alpha adrenoceptors in the bovine cerebral arteries can be classified as the alpha 2 subtype. | lld:pubmed |
