Contamination of serotonin-2 binding sites by an alpha-1 adrenergic component in assays with (3H)spiperone.
Contamination of serotonin-2 binding sites by an alpha-1 adrenergic component in assays with (3H)spiperone.
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(3H)螺哌酮测定中 α-1 肾上腺素能成分对 5-羟色胺-2 结合位点的污染。
DOI：
10.1016/0024-3205(84)90288-1
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发表时间：
1984
期刊：
影响因子：
6.1
通讯作者：
Finch,CE
中科院分区：
文献类型：
--
作者：
Morgan,DG;Marcusson,JO;Finch,CE
(3H)螺哌隆与小鼠皮质膜中的两个位点结合。这些结合位点被麦角新碱和哌唑嗪区分，但不被布他拉莫、麦角酸二乙胺或酮色林区分。其中一个位点是多巴胺能的，是真正的S-2结合位点。另一种成分是肾上腺素能的，对应于α-1肾上腺素受体。在使用（3 H）螺哌隆或（3 H）酮色林的其他S-2结合试验中可能存在该α-1组分。在小鼠皮质中未发现（3 H）螺哌隆与多巴胺能D-2位点结合。建议避免S-2结合试验的α-1污染的方法。
(3H) Spiperone binds to two sites in mouse cortical membranes. These binding sites are discriminated by methysergide and prazosin, but not by butaclamol, lysergic acid diethylamide, or ketanserin. One of these sites is serotonergic in nature and is the authentic S-2 binding site. The other component is adrenergic and corresponds to the alpha-1 adrenoreceptor. This alpha-1 component may be present in other S-2 binding assays using (3H)spiperone, or (3H)ketanserin. No (3H)spiperone binding to dopaminergic D-2 sites was found in mouse cortex. Methods of avoiding alpha-1 contamination of S-2 binding assays are suggested.