Quarles R H, Barbarash G R, Figlewicz D A, McIntyre L J
Biochim Biophys Acta. 1983 May 4;757(1):140-3. doi: 10.1016/0304-4165(83)90162-9.
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.
通过用二碘水杨酸锂-苯酚进行选择性提取,然后在琼脂糖CL-6B柱上进行凝胶过滤,从大鼠中枢神经系统髓磷脂中纯化出髓磷脂相关糖蛋白。对纯化的糖蛋白进行氨基酸分析,结果显示酸性氨基酸多于碱性氨基酸,且非极性残基含量相对较高。按重量计算,该分子约三分之一为碳水化合物,由5%的岩藻糖、23%的甘露糖、20%的半乳糖、34%的N-乙酰葡糖胺和18%的N-乙酰神经氨酸组成。