Matthieu J M, Everly J L, Brady R O, Quarles R H
Biochim Biophys Acta. 1975 May 5;392(1):167-74. doi: 10.1016/0304-4165(75)90177-4.
The in vivo incorporation of [35-S]sulfate, [3-H]fucose and [3-H]leucine into sciatic nerve myelin was investigatedmpolyacrylamide gel electrophoresis of thr proteins indicated that the 35-S-labeling of proteins occurred almost exclusively in the major myelin protein; A smaller myelin glycoprotein migrating just ahead of the major one was labeled with [3-H]fucose but did not incorporate 35-S to a detectable extent. There was little or no 35-S associated with basic proteins on polyacrylamide gels when the proteins were extracted with chloroform/methanol; Fucose-labeled myelin glycoproteins were converted to glycopeptides by pronase digestion; The glycopeptides gave a single peak on tsephadex G-50 in which the 3-H and 35-S coincided. The association of 35-S with glycopeptides was not caused by binding of sulfatide or free inorganic sulfate. This study shows that the major myelin protein in the sciatic nerve of the rat is glycosylated and sulfated.
研究了[35 - S]硫酸盐、[3 - H]岩藻糖和[3 - H]亮氨酸在大鼠坐骨神经髓鞘中的体内掺入情况。蛋白质的聚丙烯酰胺凝胶电泳表明，蛋白质的35 - S标记几乎只发生在主要髓鞘蛋白中；在主要髓鞘蛋白之前迁移的一种较小的髓鞘糖蛋白被[3 - H]岩藻糖标记，但未掺入可检测到的35 - S。当用氯仿/甲醇提取蛋白质时，聚丙烯酰胺凝胶上与碱性蛋白相关的35 - S很少或没有；岩藻糖标记的髓鞘糖蛋白经链霉蛋白酶消化后转化为糖肽；糖肽在葡聚糖G - 50上给出一个单峰，其中3 - H和35 - S重合。35 - S与糖肽的结合不是由硫脂或游离无机硫酸盐的结合引起的。这项研究表明，大鼠坐骨神经中的主要髓鞘蛋白是糖基化和硫酸化的。
