Kanety H, Fuchs S
Department of Chemical Immunology, Weizmann Institute of Science, Rehovot, Israel.
Biochem Biophys Res Commun. 1988 Sep 15;155(2):930-6. doi: 10.1016/s0006-291x(88)80585-0.
Azido-haloperidol was synthesized and applied as a photoaffinity ligand for the D2-dopamine receptor. In bovine striatal membranes, azido-haloperidol bound reversibly to the receptor (KD = 15 nM), and when exposed to light, it bound to the receptor irreversibly. This irreversible inactivation was prevented by the dopaminergic agonist N-propylnorapomorphine or the dopaminergic antagonists haloperidol and (+)-butaclamol. The photoaffinity labeled D2-receptor was probed with anti-haloperidol antibodies following gel electrophoresis and transfer to nitrocellulose. A major polypeptide of 94 kDa reacted with the anti-haloperidol antibodies. This polypeptide band was not observed when the photoaffinity labeling was performed in the presence of (+)-butaclamol or spiperone.
叠氮氟哌啶醇被合成并用作多巴胺D2受体的光亲和配体。在牛纹状体膜中，叠氮氟哌啶醇与受体可逆性结合（解离常数KD = 15 nM），且在光照下，它与受体不可逆性结合。多巴胺能激动剂N-丙基去甲阿扑吗啡或多巴胺能拮抗剂氟哌啶醇和（+）-布他拉莫可阻止这种不可逆失活。凝胶电泳并转移至硝酸纤维素膜后，用抗氟哌啶醇抗体探测光亲和标记的D2受体。一条94 kDa的主要多肽与抗氟哌啶醇抗体发生反应。当在（+）-布他拉莫或螺哌隆存在的情况下进行光亲和标记时，未观察到该多肽条带。
