Characterization of Opioid Receptor Subtypes in Solution
Characterization of Opioid Receptor Subtypes in Solution
复制标题
溶液中阿片受体亚型的表征
作者：
C. Demoliou;E. Barnard
摘要：稳定的阿片受体结合活性，保留不同的亚型特异性（μ，6，和K）已获得高产率在毛地黄皂苷提取物的大鼠脑细胞膜，已与Mg 2+预孵育溶解前。受体活性对Mg 2+离子的依赖性也表现在可溶状态，其中Mg 2+的存在导致阿片肽与δ、μ和K位点的高亲和力和高容量结合（后一种亚型通过[3 H]强啡肽1 -8的结合来测量）。阿片类生物碱与可溶性受体位点的结合比阿片肽结合对Mg 2+的依赖性小。可溶性阿片样物质结合活性显示出与膜结合受体相同的对Na+离子和鸟嘌呤核苷酸的敏感性。配体-受体相互作用提供了强正协同性的证据，这是根据溶液中配体结合时受体亚基的缔合-解离来解释的。脑啡肽的结合与存在的大分子（表观斯托克斯半径> 60 μ m）有关，而这些大分子和存在的几种小分子（< 60 μ m）结合阿片类生物碱和强啡肽1 -8。
Abstract: Stable opioid receptor binding activity that retains distinct subtype specificities (μ, 6, and K) has been obtained in high yields in digitonin extracts of rat brain membranes that had been preincubated with Mg2+ prior to solubilization. The dependence on Mg2+ ions for receptor activity is also expressed in the soluble state, where the presence of Mg2+ leads to high‐affinity and high‐capacity opioid peptide binding to the δ, μ, and K sites (the latter subtype measured by the binding of [3H]dynorphin1–8). Binding of opiate alkaloids to soluble receptor sites is less dependent on Mg2+ than is opioid peptide binding. Soluble opioid binding activity shows the same sensitivity to Na+ ions and guanine nucleotides as the membrane‐bound receptor. The ligand‐receptor interactions give evidence of strong positive cooperativity, which is interpreted in terms of association‐dissociation of receptor subunits on ligand binding in solution. Binding of enkephalin peptides is associated with the large macromolecules present (apparent Stokes radii > 60 Å), whereas both those and several small species present (< 60 Å) bind opiate alkaloids and dynorphin1–8.
大鼠脑中 mu 和 kappa 阿片受体亚型的溶解和初步表征。
影响因子：
3.6
作者：
Chow,T;Zukin,RS
通讯作者：
Zukin,RS