Toogood C I, McFarthing K G, Hulme E C, Smyth D G
Neuropeptides. 1984 Dec;5(1-3):121-4. doi: 10.1016/0143-4179(84)90042-8.
Evidence is presented that a new derivative of beta-endorphin, [125I] Tyr27 beta-endorphin, is a suitable ligand for the study of beta-endorphin binding sites in rat brain. The results obtained with this homogeneous mono-iodinated peptide demonstrated high affinity agonist binding sensitive to the presence of sodium and magnesium ion and to guanine nucleotide. Competition experiments using a series of opiates and opioid peptides including shorter forms of beta-endorphin revealed a range of potencies; beta-endorphin 1-31 exhibited the highest affinity. The findings suggest that binding sites that complement the structure of beta-endorphin are present in rat cortex.
有证据表明，β-内啡肽的一种新衍生物[125I]Tyr27β-内啡肽是研究大鼠脑中β-内啡肽结合位点的合适配体。用这种均一的单碘化肽获得的结果表明，高亲和力激动剂结合对钠、镁离子及鸟嘌呤核苷酸的存在敏感。使用一系列阿片类药物和阿片样肽（包括较短形式的β-内啡肽）进行的竞争实验揭示了一系列效价；β-内啡肽1-31表现出最高亲和力。这些发现表明，与β-内啡肽结构互补的结合位点存在于大鼠皮质中。
