Elliott J, Dunn S M, Blanchard S G, Raftery M A
Proc Natl Acad Sci U S A. 1979 Jun;76(6):2576-9. doi: 10.1073/pnas.76.6.2576.
Torpedo californica postsynaptic membrane fragments were treated with base, which resulted in membranes that were depleted of many nonacetylcholine receptor polypeptides and contained acetylcholine receptor subunits of Mr 40,000, 50,000, 60,000, and 65,000 (Raftery, M.A., Vandlen, R.L., Reed, K.L. & Lee T. (1975) Cold Spring Harbor Symp. Quant. Biol. 40, 193-202). A 43,000-Mr polypeptide and some other components were quantitatively extracted. Base-treated membranes retained the capacity to bind [3H]perhydrohistrionicotoxin and the local anesthetics dibucaine and tetracaine. The regulation of this binding by carbamylcholine, as well as the kinetic mechanism of perhydrohistrionicotoxin binding, was unchanged. [3H]Perhydrohistrionicotoxin binding activity was largely reconstituted from 2% sodium cholate extracts of base-treated membranes. Therefore, the perhydrostrionicotoxin binding site appears to be located on one or more of the acetylcholine receptor polypeptides, and the reconstitution of that binding site from detergent extracts does not require the presence of a 43,000-Mr polypeptide.
用碱处理加州电鳐突触后膜片段，结果得到的膜中许多非乙酰胆碱受体多肽被去除，并且含有分子量为40,000、50,000、60,000和65,000的乙酰胆碱受体亚基（拉夫特里，M.A.，范德伦，R.L.，里德，K.L. & 李，T.（1975年）《冷泉港定量生物学研讨会论文集》40，193 - 202）。一种分子量为43,000的多肽和一些其他成分被定量提取。经碱处理的膜保留了结合[³H]全氢组氨毒素以及局部麻醉剂丁卡因和丁哌卡因的能力。氨甲酰胆碱对这种结合的调节以及全氢组氨毒素结合的动力学机制没有改变。[³H]全氢组氨毒素结合活性在很大程度上可从经碱处理的膜的2%胆酸钠提取物中重新构建。因此，全氢组氨毒素结合位点似乎位于一种或多种乙酰胆碱受体多肽上，并且从去污剂提取物中重建该结合位点不需要存在分子量为43,000的多肽。
