Muramatsu T, Ogata M, Koide N
Biochim Biophys Acta. 1976 Aug 24;444(1):53-68. doi: 10.1016/0304-4165(76)90223-3.
Approximately 70% of fucose-labeled glycopeptides from the cell surface and cellular material of rat fibroblasts (3Y1B cells) were hydrolyzed by endo-beta-N-acetylglucosaminidase D in the presence of neuraminidase, beta-galactosidase and beta-N-acetylglucosaminidase. Structure of the susceptible glycopeptides were found to be very similar to non-membrane glycopeptides of the complex heteropolysaccharide unit, such as the sialylated glycopeptides of thyroglobulin. On the other hand, the resistant glycopeptides were also refractory toward endo-beta-N-acetylglucosaminidase H and alpha-mannosidase, and appeared to be a mixture of glycopeptides with unique structures.
在神经氨酸酶、β-半乳糖苷酶和β-N-乙酰氨基葡萄糖苷酶存在的情况下,来自大鼠成纤维细胞(3Y1B细胞)细胞表面和细胞物质的约70%的岩藻糖标记糖肽被内切β-N-乙酰氨基葡萄糖苷酶D水解。发现易感性糖肽的结构与复合杂多糖单元的非膜糖肽非常相似,如甲状腺球蛋白的唾液酸化糖肽。另一方面,抗性糖肽对内切β-N-乙酰氨基葡萄糖苷酶H和α-甘露糖苷酶也具有抗性,并且似乎是具有独特结构的糖肽混合物。