Briley M S, Changeux J P
Eur J Biochem. 1978 Mar 15;84(2):429-39. doi: 10.1111/j.1432-1033.1978.tb12184.x.
The change of affinity of the acetylcholine receptor for agonists and the influence of local anaesthetics has been studied in detail in receptor-rich membranes. These properties are changed after solubilisation by ionic detergents. A method for reproducibly reintegrating the receptor protein into a lipid environment is described. Reintegration of the receptor results in partial recovery of the binding and fluorescence properties of the membrane-bound receptor protein. In particular, the slow affinity change caused by agonists can be recovered but not the effect of local anaesthetics on this change. The fluorescence response to cholinergic ligands of the reintegrated receptor protein labelled with quinacrine does not appear identical to that found with the native receptor-rich membranes. It is suggested that the failure to recover the sensitivity to local anaesthetics is at the origin of the difficulties to regain functional reconstitution.
在富含受体的膜中，已对乙酰胆碱受体与激动剂的亲和力变化以及局部麻醉药的影响进行了详细研究。这些特性在通过离子去污剂溶解后会发生改变。本文描述了一种将受体蛋白可重复地重新整合到脂质环境中的方法。受体的重新整合导致膜结合受体蛋白的结合和荧光特性部分恢复。特别是，激动剂引起的缓慢亲和力变化可以恢复，但局部麻醉药对这种变化的影响却无法恢复。用喹吖因标记的重新整合受体蛋白对胆碱能配体的荧光反应似乎与天然富含受体的膜中的反应不同。有人认为，无法恢复对局部麻醉药的敏感性是难以实现功能重建的根源。
