Marton L S, Stefansson K
J Cell Biol. 1984 Nov;99(5):1642-6. doi: 10.1083/jcb.99.5.1642.
By the use of a rat IgG monoclonal antibody (mab), a mouse mab and human serum containing an IgM mab, all of which react with isolated human myelin-associated glycoprotein (MAG) on immunoblots and bind only to proteins with relative mobilities identical to MAG and dMAG on immunoblots of homogenates of adult human spinal cord, we demonstrated the following: in homogenates of central nervous system tissue from human fetuses of gestational ages that antedate myelination, the anti-MAG antibodies react only with proteins with molecular weights of 250,000 or larger. During myelination the molecular weights of proteins with which the anti-MAG antibodies react shift towards the lower molecular weights found in adult myelin. Amongst those central nervous system regions examined, the shift towards the low molecular weights occurred earliest in the region that is first to become myelinated and latest in the one that is the last to myelinate. Once myelination is completed, the antibodies react only with proteins with relative mobilities identical to those of MAG and dMAG. These developmental changes in molecular weights of "MAG-related proteins" may prove useful as an index of chemical processes on the basis of which myelination occurs.
通过使用大鼠IgG单克隆抗体（mab）、小鼠mab和含有IgM mab的人血清，所有这些抗体在免疫印迹上均与分离的人髓鞘相关糖蛋白（MAG）发生反应，并且在成人脊髓匀浆的免疫印迹上仅与相对迁移率与MAG和dMAG相同的蛋白质结合，我们证明了以下几点：在髓鞘形成之前的胎龄的人胎儿的中枢神经系统组织匀浆中，抗MAG抗体仅与分子量为250,000或更大的蛋白质发生反应。在髓鞘形成过程中，抗MAG抗体所反应的蛋白质的分子量向成人髓鞘中发现的较低分子量转移。在所检查的那些中枢神经系统区域中，向低分子量的转移最早发生在最先开始髓鞘形成的区域，最晚发生在最后开始髓鞘形成的区域。一旦髓鞘形成完成，抗体仅与相对迁移率与MAG和dMAG相同的蛋白质发生反应。“MAG相关蛋白”分子量的这些发育变化可能被证明是髓鞘形成所基于的化学过程的有用指标。
