Matthieu J M, Quarles R H, Poduslo J F, Brady R O
Biochim Biophys Acta. 1975 May 5;392(1):159-66. doi: 10.1016/0304-4165(75)90176-2.
The in vivo incorporation of [35-S]sulfate and [3H]fucose into rat brain myelin was investigatedmmost of the 35S in the myelin was in sulfatide, but about 4% was associated with the residual proteins after chloroform/methanol extraction. Polyacrylamide gel electrophoresis of these proteins indicated that the major 35-S-labeled component corresponded to the major fucose-labeled glycoproteinmthe labeling of this predominant glycoprotein with sulfate was more selective than with fucose, since there was relatively little incorporation of sulfate into some of the minor fucose-labeled glycoproteins. There was little or no 35-S associated with proteolipid or basic protein on polyacrylamide gels. The fucose-labeled glycoproteins were converted to glycopeptides by pronase digestion and separated into two major classes by gel filtration on Sephadex-G-50. Only the higher molecular weight class contained significant amounts of 35-S. The association of 35-S with the glycopeptides was not due to binding of sulfatide or free inorganic sulfate. The results indicate that the predominant myelin-associated glycoprotein in rat brain is sulfated.
研究了[35-S]硫酸盐和[3H]岩藻糖在大鼠脑髓鞘中的体内掺入情况。髓鞘中大部分的35S存在于硫脂中，但约4%与氯仿/甲醇提取后的残留蛋白质相关。这些蛋白质的聚丙烯酰胺凝胶电泳表明，主要的35-S标记成分与主要的岩藻糖标记糖蛋白相对应。该主要糖蛋白的硫酸盐标记比岩藻糖标记更具选择性，因为在一些次要的岩藻糖标记糖蛋白中，硫酸盐的掺入相对较少。在聚丙烯酰胺凝胶上，几乎没有或没有35-S与蛋白脂质或碱性蛋白相关。岩藻糖标记的糖蛋白经链霉蛋白酶消化后转化为糖肽，并通过Sephadex-G-50凝胶过滤分为两大类。只有较高分子量的类别含有大量的35-S。35-S与糖肽的结合不是由于硫脂或游离无机硫酸盐的结合。结果表明，大鼠脑中主要的髓鞘相关糖蛋白是硫酸化的。
