Vidal C J, Chai M S, Plummer D T
Department of Biochemistry, King's College London, Campden Hill, London, W8 7AH, U.K.
Neurochem Int. 1987;11(2):135-41. doi: 10.1016/0197-0186(87)90001-5.
Homogenization of rat brain with dilute buffer shows that about 15% of the acetylcholinesterase is soluble while the remaining 85% is present in a membrane-bound form which can be brought into solution by extraction with Triton X-100. The effect of temperature on the values of V(max) and K(m) of the buffer-soluble, the membrane-bound and the Triton-soluble forms of acetylcholinesterase have been compared and the results discussed in terms of possible changes in the conformation, dissociation or aggregation of the enzyme molecule. Gradient-gel electrophoresis of the soluble preparations carried out at 4 degrees C or 37 degrees C suggest that the normal tetrameric structure present at 4 degrees C dissociates into monomers and forms some higher molecular weight species at 37 degrees C. The effect of prior storage of the brains in toluene on these properties is also considered.
用稀释缓冲液对大鼠脑进行匀浆处理表明，约15%的乙酰胆碱酯酶是可溶的，而其余85%以膜结合形式存在，可通过用 Triton X - 100提取而溶解。比较了温度对缓冲液可溶、膜结合和 Triton 可溶形式的乙酰胆碱酯酶的V(max)和K(m)值的影响，并根据酶分子构象、解离或聚集的可能变化对结果进行了讨论。在4℃或37℃对可溶制剂进行的梯度凝胶电泳表明，4℃时存在的正常四聚体结构在37℃时解离成单体并形成一些更高分子量的物种。还考虑了预先将脑保存在甲苯中对这些性质的影响。
