Chen J, Lai L
Hua Xi Yi Ke Da Xue Xue Bao. 1990 Sep;21(4):354-6.
A simplified procedure for isolation and purification of myelin basic protein (MBP) from human brain is described. Purified myelin from white matter was isolated at first, then delipidated with heated organic solvents. The pellet was washed with triethanolamine buffer and extracted with 0.01 mol/L HCl. Finally the protein in the acidic supernatant was purified with Sephadex G-150 column. By using three different PAGE and immunoelectrophoresis, the purified MBP was identified as a homogeneous component with an apparent molecular weight of 18.5 kd and pI 10.6. This procedure has the advantage of simplicity, rapidity, high yield and purity.
本文描述了一种从人脑中分离和纯化髓鞘碱性蛋白（MBP）的简化方法。首先从白质中分离出纯化的髓磷脂，然后用加热的有机溶剂进行脱脂。沉淀用三乙醇胺缓冲液洗涤，并用0.01mol/L盐酸提取。最后，酸性上清液中的蛋白质用Sephadex G - 150柱进行纯化。通过三种不同的聚丙烯酰胺凝胶电泳（PAGE）和免疫电泳，鉴定纯化的MBP为一种均一成分，其表观分子量为18.5kd，等电点为10.6。该方法具有简单、快速、高产率和高纯度的优点。
