Fuchs K, Möhler H, Sieghart W
Department of Biochemical Psychiatry, Psychiatrische Universitätsklinik, Vienna, Austria.
Neurosci Lett. 1988 Aug 1;90(3):314-9. doi: 10.1016/0304-3940(88)90208-x.
gamma-Aminobutyric acid (GABA)-benzodiazepine receptors were purified from the brains of 5 to 10-day-old rats and photolabeled by [3H]flunitrazepam. After sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE), 3 different proteins with apparent molecular weight 51,000, 53,000 and 59,000 Da specifically and irreversibly labeled by [3H]flunitrazepam were revealed by autoradiography. The same 3 proteins were recognized by the alpha-subunit-specific monoclonal antibody bd-28. In contrast, a different protein with apparent molecular weight 56,000 Da was recognized by the beta-subunit-specific antibody bd-17. These results indicate that the various proteins specifically labeled by [3H]flunitrazepam are different alpha-subunits and distinct and different from the beta-subunit of the GABA-benzodiazepine receptor complex.
从5至10日龄大鼠的大脑中纯化γ-氨基丁酸（GABA）-苯二氮䓬受体，并用[³H]氟硝西泮进行光标记。经过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳（SDS-PAGE）后，通过放射自显影揭示了3种不同的蛋白质，其表观分子量分别为51,000、53,000和59,000 Da，它们被[³H]氟硝西泮特异性且不可逆地标记。这3种相同的蛋白质可被α亚基特异性单克隆抗体bd-28识别。相比之下，一种表观分子量为56,000 Da的不同蛋白质可被β亚基特异性抗体bd-17识别。这些结果表明，被[³H]氟硝西泮特异性标记的各种蛋白质是不同的α亚基，与GABA-苯二氮䓬受体复合物的β亚基不同且有区别。
