Benke D, Cicin-Sain A, Mertens S, Mohler H
Institute of Pharmacology, University of Zurich, Switzerland.
J Recept Res. 1991;11(1-4):407-24. doi: 10.3109/10799899109066418.
To identify subunit variants of the GABAA-receptor antisera were developed against specific cDNA-derived peptide sequences of the alpha 1- and alpha 3-subunits of rat brain. The alpha 1-subunit antiserum selectively recognized a protein of 50 +/- 1 kDa in rat and bovine GABAA-receptor preparations, while the alpha 3-subunit antiserum interacted with a protein doublet of 59 +/- 2 kDa and 61 +/- 3 kDa. The alpha 1-subunit immunoreactivity resides in a large population of GABAA-receptors as shown by immunoprecipitation of 63 +/- 6% of [3H]flumazenil binding sites with the alpha 1-subunit antiserum. In contrast, only 24 +/- 3% of receptor binding sites were precipitated with the alpha 3-subunit antiserum. Co-precipitation studies suggest that the alpha 1- and alpha 3-subunit immunoreactivities do not share the same receptor population while the gamma 2-subunit immunoreactivity is associated with the alpha 1-subunit immunoreactivity.
为了鉴定GABAA受体的亚基变体,制备了针对大鼠脑α1和α3亚基特定cDNA衍生肽序列的抗血清。α1亚基抗血清在大鼠和牛的GABAA受体制剂中选择性识别一种50±1 kDa的蛋白质,而α3亚基抗血清与59±2 kDa和61±3 kDa的蛋白质双峰相互作用。如用α1亚基抗血清免疫沉淀63±6%的[3H]氟马西尼结合位点所示,α1亚基免疫反应性存在于大量的GABAA受体中。相比之下,用α3亚基抗血清仅沉淀了24±3%的受体结合位点。共沉淀研究表明,α1和α3亚基免疫反应性不共享相同的受体群体,而γ2亚基免疫反应性与α1亚基免疫反应性相关。