Rothman R B, Danks J A, Herkenham M, Cascieri M A, Chicchi G G, Liang T, Pert C B
Neuropeptides. 1984 Jun;4(4):343-9. doi: 10.1016/0143-4179(84)90009-x.
Using slide mounted sections of rat brain sausage, we have characterized the binding of [125I]Bolton Hunter conjugated eledoisin and [125I]Bolton Hunter conjugated substance P. Structure activity studies suggest that the two radiolabeled peptides bind to different binding sites. Autoradiographic studies support this notion. Whereas [125I]BH-SP sparsely labels the interpeduncular nucleus and does not label the substantia nigra at all, [125I]BH-ED densely labels the former and sparsely labels the latter structure. Further, the cortical labeling patterns obtained with the two peptides are strikingly different. These data support the hypothesis that there exist two classes of tachykinin binding sites in rat nervous tissue.
利用大鼠脑切片,我们已对[125I]博尔顿·亨特偶联的伊索辛和[125I]博尔顿·亨特偶联的P物质的结合特性进行了表征。结构活性研究表明,这两种放射性标记的肽与不同的结合位点结合。放射自显影研究支持了这一观点。[125I]BH-SP稀疏标记脚间核,根本不标记黑质,而[125I]BH-ED则密集标记前者,稀疏标记后者结构。此外,用这两种肽获得的皮质标记模式明显不同。这些数据支持了大鼠神经组织中存在两类速激肽结合位点的假说。