Bellini T, Rippa M, Matteuzzi M, Dallocchio F
J Neurochem. 1986 May;46(5):1644-6. doi: 10.1111/j.1471-4159.1986.tb01788.x.
A rapid procedure for purification of myelin basic protein has been developed. White matter is delipidated with 2-butanol, and the residue is extracted at pH 7.5 and 8.5. Myelin basic protein is solubilized by extraction in acetate buffer, pH 4.5. The entire procedure requires less than 4 h, and gives homogeneous protein essentially free of protease activity. This procedure can be scaled down to process milligram amounts of white matter; thus it can be very useful for purification of myelin basic protein from very limited amounts of human white matter obtained during surgery.
已开发出一种快速纯化髓鞘碱性蛋白的方法。用2-丁醇去除白质中的脂质，残留物在pH 7.5和8.5下进行提取。髓鞘碱性蛋白通过在pH 4.5的醋酸盐缓冲液中提取而溶解。整个过程耗时不到4小时，得到的蛋白质纯度高且基本无蛋白酶活性。该方法可按比例缩小以处理毫克量的白质；因此，对于从手术中获得的极少量人类白质中纯化髓鞘碱性蛋白非常有用。
