Michaelson D M, Raftery M A
Proc Natl Acad Sci U S A. 1974 Dec;71(12):4768-72. doi: 10.1073/pnas.71.12.4768.
Association of purified acetylcholine receptor from Torpedo californica electroplax with lipids from the same organism results in a vesicular membrane system in which the receptor protein is oriented so that all neurotoxin binding sites appear to be on the outer surface. The reconstituted system is chemically excitable by acetylcholine and carbamylcholine, as measured by (22)Na(+) efflux. This excitability is specifically blocked by the antagonist alpha-bungarotoxin. These results demonstrate that the purified receptor macromolecule contains not only the specific neurotransmitter binding site but also the molecular elements necessary for ion translocation in order to effect postsynaptic depolarization.
将来自加州电鳐电板的纯化乙酰胆碱受体与同一生物体的脂质相结合，会形成一种囊泡膜系统，其中受体蛋白的取向使得所有神经毒素结合位点似乎都在外表面。通过（22）Na（+）外流测量，重构系统可被乙酰胆碱和氨甲酰胆碱化学激发。这种激发作用被拮抗剂α-银环蛇毒素特异性阻断。这些结果表明，纯化的受体大分子不仅包含特定的神经递质结合位点，还包含离子转运所需的分子元件，以实现突触后去极化。
