Purification and partial characterization of the myelin-associated glycoprotein from adult rat brain.
The myelin-associated glycoprotein was purified from rat central nervous system myelin by selective extraction with lithium diiodosalicylate-phenol followed by gel filtration on a column of Sepharose CL-6B. Amino acid analysis of the purified glycoprotein revealed an excess of acidic over basic amino acids and a relatively high content of nonpolar residues. On the basis of weight, the molecule is about one-third carbohydrate consisting of 5% fucose, 23% mannose, 20% galactose, 34% N-acetylglucosamine, and 18% N-acetylneuraminic acid.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001923:Brain Chemistry; D002241:Carbohydrates / Q000032:analysis; D055598:Chemical Phenomena; D002621:Chemistry; D009185:Myelin Proteins / Q000302:isolation & purification*; D018992:Myelin-Associated Glycoprotein; D051381:Rats; D011919:Rats, Inbred Strains
D000596:Amino Acids; D002241:Carbohydrates; D009185:Myelin Proteins; D018992:Myelin-Associated Glycoprotein