Pereyra P M, Horvath E, Braun P E
McGill University, Dept. Biochemistry, Montreal, Quebec, Canada.
Neurochem Res. 1988 Jun;13(6):583-95. doi: 10.1007/BF00973301.
Isolated CNS myelin membranes were extracted with Triton X-100 under conditions previously established for the isolation of cytoskeletal proteins. Treated myelin retained much of its characteristic lamellar structure despite the removal of most of the major myelin basic protein (18.5 kDa) and the proteolipid protein, which together normally constitute 60% of the total myelin protein. The SDS-PAGE profile of this extract residue demonstrated an enrichment in proteins of Mr 30 to 60 kilodaltons (the Wolfgram group). The major myelin proteins were identified by antibodies on Western immunoblots, as were the 2'3'-cyclic nucleotide 3'-phosphodiesterase (CNP), actin, tubulin, myelin-associated glycoprotein (MGP) and the 21.5 kDA MBP. The overall behavior of CNP, the 21.5 kDa MBP, MGP and tubulin towards Triton extraction is reminiscent of the behavior of other membrane-skeletal complexes, supporting the idea that these and other minor myelin proteins might be part of heteromolecular complexes with interactions spanning several lamellae of the myelin sheath.
在先前为分离细胞骨架蛋白而确定的条件下，用Triton X-100提取分离的中枢神经系统髓鞘膜。尽管去除了大部分主要的髓鞘碱性蛋白（18.5 kDa）和蛋白脂质蛋白，而这两种蛋白通常共占髓鞘总蛋白的60%，但处理后的髓鞘仍保留了其大部分特征性的层状结构。该提取物残渣的SDS-PAGE图谱显示，分子量为30至60千道尔顿的蛋白质（沃尔夫格拉姆组）有所富集。通过蛋白质免疫印迹法上的抗体鉴定了主要的髓鞘蛋白，以及2',3'-环核苷酸3'-磷酸二酯酶（CNP）、肌动蛋白、微管蛋白、髓鞘相关糖蛋白（MGP）和21.5 kDa的髓鞘碱性蛋白（MBP）。CNP、21.5 kDa的MBP、MGP和微管蛋白对Triton提取的总体行为让人联想到其他膜骨架复合物的行为，这支持了这样一种观点，即这些以及其他次要的髓鞘蛋白可能是异分子复合物的一部分，其相互作用跨越髓鞘的几个板层。
