Martínez de Melían E R, Morero R D, Farías R N
Biochim Biophys Acta. 1976 Jan 23;422(1):127-37. doi: 10.1016/0005-2744(76)90014-0.
Electrophoretic patterns of acetylcholinesterase (acetylcholine hydrolase, EC 3.1.1.7) from rat erythrocyte were studied. The enzyme was solubilized by the following treatments: a) Triton X-100, b) sodium deoxycholate, or c) ultrasonic irradiation. When the erythrocyte membrane was solubilized by Triton X-100 at concentrations higher than 0.3%, by 10 mM sodium deoxycholate, or by ultrasonic irradiation for more than 5 min, a single band of acetylcholinesterase activity appeared in the gel. Two bands of activity were stained in the gel when the membrane was solubilized by Triton X-100 at concentrations between 0.1--0.2%, or by ultrasound for 5 min. Electrophoretic patterns of acetylcholinesterase from rats fed a fat-sufficient diet were similar to those for the enzyme from animals fed a fat-free diet. The recombination of lipids with the enzyme eluted from the gels confirmed the "phenotypic allosteric desensitization phenomenon".
研究了大鼠红细胞乙酰胆碱酯酶（乙酰胆碱水解酶，EC 3.1.1.7）的电泳图谱。该酶通过以下处理进行增溶：a）Triton X-100，b）脱氧胆酸钠，或c）超声辐照。当红细胞膜在浓度高于0.3%的Triton X-100、10 mM脱氧胆酸钠作用下或超声辐照超过5分钟时增溶，凝胶中会出现一条乙酰胆碱酯酶活性条带。当膜在浓度为0.1 - 0.2%的Triton X-100作用下或超声处理5分钟增溶时，凝胶中会出现两条活性条带。喂食脂肪充足饮食的大鼠的乙酰胆碱酯酶电泳图谱与喂食无脂肪饮食的动物的该酶电泳图谱相似。从凝胶上洗脱下来的酶与脂质的重组证实了“表型变构脱敏现象”。
