CHARACTERIZATION OF RECEPTORS FOR FMRFAMIDE-RELATED NEUROPEPTIDES

该项目涉及识别和表征 FMRFamide的受体（Phe-Met-Arg-Phe-NH 2），是一种广泛的 分布的神经肽FMRFamine受体溶解自 用两性离子洗涤剂CHAPS清洗鱿鱼脑溶解的 受体结合FMRFamide，Kd约为0.15 Nm，并显示出 结构-活性关系类似于受体， 不溶解的鱿鱼膜配体亲和力对鸟嘌呤敏感 核苷酸，表明受体与G蛋白的偶联- 调节途径，并与早期的工作表明， FMRFamide对鱿鱼腺苷酸环化酶刺激作用目前的努力 目的在于获得所述化合物的分子大小的估计， 受体的早期的方法使用光反应类似物的 FMRFaminde鉴定了一个52 kDa的蛋白质，但随后的工作表明， 这种蛋白质不是受体的基础上， 配体特异性和亲和力以及GTP敏感性。这种蛋白质可以 是一种参与肽加工的酶，因为它的特异性 与非酰胺化FMRF相比，FMRFamide。

This project is concerned with the identification and characterization of the receptor for FMRFamide (Phe-Met-Arg-Phe-NH2), a widely distributed neuropeptide. FMRFamine receptors were solubilized from squid brain using the zwitterionic detergent CHAPS. The solubilized receptor bound FMRFamide with Kd about 0.15 Nm and displayed a structure-activity relationship similar to that of the receptor in unsolubilized squid membranes. Ligand affinity was sensitive to guanine nucleotides, indicating the coupling of the receptor to a G protein- regulated pathway and consistent with earlier work demonstrating the stimulation of squid adenylate cyclase by FMRFamide. Current efforts are directed towards obtaining an estimate of the molecular size of the receptor. An earlier approach using photoreactive analogues of FMRFaminde identified a protein of 52 kDa, but subsequent work suggested that this protein is not the receptor on the basis of differences in ligand specificity and affinity, and GTP sensitivity. This protein may be an enzyme involved in peptide processing because of its specificity for FMRFamide in comparison to the non-amidated FMRF.