Gredal O, Parkinson D, Nielsen M
Eur J Pharmacol. 1987 Jun 4;137(2-3):241-5. doi: 10.1016/0014-2999(87)90228-7.
[3H]SCH 23390 binding was examined in membranes of rat retina. The binding was saturable with a dissociation constant of 0.2 nM and the maximum number of binding sites was 236 +/- 74 fmol/mg protein. The pharmacology of [3H]SCH 23390 binding indicated that the binding was specific for a dopamine D-1 receptor because the binding was preferentially inhibited by D-1-selective agonists and antagonists but not by dopamine D-2-selective agonists and antagonists. The same membrane preparations were used to characterize the dopamine D-2 receptor binding as measured with [3H]spiperone and the amount of binding sites was found to be similar to the amount of D-1 sites. It is concluded that [3H]SCH 23390 is a useful tool to examine dopamine D-1 receptors in the retina.
在大鼠视网膜膜中检测了[3H]SCH 23390的结合情况。该结合具有饱和性,解离常数为0.2 nM,结合位点的最大数量为236±74 fmol/mg蛋白质。[3H]SCH 23390结合的药理学表明,该结合对多巴胺D-1受体具有特异性,因为该结合优先被D-1选择性激动剂和拮抗剂抑制,而不被多巴胺D-2选择性激动剂和拮抗剂抑制。使用相同的膜制剂来表征用[3H]螺哌隆测量的多巴胺D-2受体结合情况,发现结合位点的数量与D-1位点的数量相似。得出结论,[3H]SCH 23390是检测视网膜中多巴胺D-1受体的有用工具。