Stephenson F A, Mamalaki C, Casalotti S O, Barnard E A
Biochem Soc Symp. 1986;52:33-40.
The GABAA/benzodiazepine receptor has been purified to homogeneity from bovine and rat cerebral cortex. Under optimum conditions, the purified receptor has been shown to possess four distinct drug-binding sites, for GABA, benzodiazepine, barbiturate and Cl- channel gating classes of ligands. The receptor is a multi-subunit membrane glycoprotein with an oligomeric size of 230,000 Da. It contains at least two subunits, alpha and beta, the first of which can be photoaffinity-labelled with the benzodiazepine, flunitrazepam. Polyclonal and monoclonal antibodies have been raised to the native receptor and both have been used in an immunological characterization of the receptor protein in detergent extracts and likewise in purified preparations from bovine cerebral cortex.
γ-氨基丁酸A型/苯二氮䓬受体已从牛和大鼠大脑皮层中纯化至同质状态。在最佳条件下，纯化后的受体已被证明具有四个不同的药物结合位点，分别针对γ-氨基丁酸、苯二氮䓬、巴比妥酸盐和氯离子通道门控类配体。该受体是一种多亚基膜糖蛋白，寡聚体大小为230,000道尔顿。它至少包含两个亚基，α和β，其中第一个亚基可被苯二氮䓬氟硝西泮进行光亲和标记。已针对天然受体产生了多克隆和单克隆抗体，二者均用于去污剂提取物中受体蛋白的免疫特性分析，同样也用于牛大脑皮层的纯化制剂中。
