O'Brien R D, Gilmour L P, Eldefrawi M E
Proc Natl Acad Sci U S A. 1970 Feb;65(2):438-45. doi: 10.1073/pnas.65.2.438.
An equilibrium dialysis technique, applied to lyophilized particulate fractions of Torpedo electroplax, gave data consistent with a single kind of macromolecular binding of muscarone, with binding constant, 7 x 10(-7)M and an amount of 1 nmole per gram original electroplax. The effects on muscarone binding of 38 drugs suggested that muscarone binding reflected acetylcholine receptor activity. Of 18 enzyme preparations, only trypsin, chymotrypsin, and phospholipase C reduced binding activity, suggesting that a phospholipoprotein was binding. Partial "solubilization" of the binding protein was achieved, but the "solubilized" activity did not migrate on electrophoresis. Additional evidence was provided that acetylcholinesterase was not responsible for this muscarone binding.
一种平衡透析技术应用于电鳐电板的冻干颗粒级分,得到的数据与毒蝇蕈碱的单一类型大分子结合一致,结合常数为7×10⁻⁷M,每克原始电板的结合量为1纳摩尔。38种药物对毒蝇蕈碱结合的影响表明,毒蝇蕈碱结合反映了乙酰胆碱受体活性。在18种酶制剂中,只有胰蛋白酶、糜蛋白酶和磷脂酶C降低了结合活性,这表明是一种脂蛋白在结合。结合蛋白实现了部分“溶解”,但“溶解”后的活性在电泳中不迁移。此外还提供了证据表明乙酰胆碱酯酶与这种毒蝇蕈碱结合无关。