Nielsen M, Klimek V, Hyttel J
Life Sci. 1984 Jul 16;35(3):325-32. doi: 10.1016/0024-3205(84)90116-4.
Frozen rat striatal tissue was exposed to 10 MeV electrons from a linear accelerator. Based on the theory of target size analysis, the molecular weights of dopamine D-1 receptors (labelled by 3H-piflutixol) and dopamine D-2 receptors (labelled by 3H-spiroperidol) were 79,500 daltons and 136,700 daltons, respectively. The size of the dopamine-stimulated adenylate cyclase was 202,000 daltons. The estimated molecular sizes were deduced by reference to proteins with known molecular weights which were irradiated in parallel. The results showed that the molecular entities for 3H-piflutixol binding and 3H-spiroperidol binding were not identical. The present results do not allow conclusions as to whether D-1 and D-2 receptors are two distinct proteins in the membrane, or whether the receptors are located on the same protein. In the latter case the binding of 3H-spiroperidol needs the presence of a second molecule.
将冷冻的大鼠纹状体组织暴露于来自直线加速器的10兆电子伏特电子束下。根据靶标大小分析理论，多巴胺D-1受体（用³H-匹莫齐特标记）和多巴胺D-2受体（用³H-螺哌啶醇标记）的分子量分别为79,500道尔顿和136,700道尔顿。多巴胺刺激的腺苷酸环化酶的大小为202,000道尔顿。通过参考平行照射的已知分子量蛋白质来推断估计的分子大小。结果表明，³H-匹莫齐特结合和³H-螺哌啶醇结合的分子实体并不相同。目前的结果无法得出关于D-1和D-2受体是膜中两种不同的蛋白质，还是受体位于同一蛋白质上的结论。在后一种情况下，³H-螺哌啶醇的结合需要第二种分子的存在。
