[35-S]sulfate incorporation into myelin glycoproteinsmi=entral nervous system.
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.
D000818:Animals; D001921:Brain / Q000378:metabolism*; D002850:Chromatography, Gel; D002855:Chromatography, Thin Layer; D004591:Electrophoresis, Polyacrylamide Gel; D005643:Fucose / Q000378:metabolism; D006023:Glycoproteins / Q000096:biosynthesis*; D008297:Male; D009186:Myelin Sheath / Q000378:metabolism*; D009419:Nerve Tissue Proteins / Q000096:biosynthesis*; D011402:Pronase; D051381:Rats; D013431:Sulfates / Q000378:metabolism*; D013462:Sulfur Radioisotopes; D014316:Tritium
D006023:Glycoproteins; D009419:Nerve Tissue Proteins; D013431:Sulfates; D013462:Sulfur Radioisotopes; D014316:Tritium; D005643:Fucose; D011402:Pronase