Mizuochi T, Taniguchi T, Shimizu A, Kobata A
J Immunol. 1982 Nov;129(5):2016-20.
Oligosaccharide patterns obtained from human IgG by hydrazinolysis were fairly constant from sample to sample. In contrast, a variety of oligosaccharide patterns were obtained from IgG myeloma proteins. Structural analysis of each oligosaccharide by sequential exoglycosidase digestion and methylation studied indicated that the different patterns of IgG myeloma proteins are produced by different degrees of incompleteness of the formation of a single sugar chain: Sia alpha 2 leads to Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 6(Sia alpha 2 leads to Gal beta 1 leads to 4GlcNAc beta 1 leads to Man alpha 1 leads to 3)(GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAcOT.
通过肼解从人IgG获得的寡糖模式在不同样本之间相当稳定。相比之下，从IgG骨髓瘤蛋白中获得了多种寡糖模式。通过顺序外切糖苷酶消化和甲基化研究对每种寡糖进行结构分析表明，IgG骨髓瘤蛋白的不同模式是由单糖链形成的不同程度的不完全性产生的：唾液酸α2连接到半乳糖β1连接到4-N-乙酰葡糖胺β1连接到2-甘露糖α1连接到6（唾液酸α2连接到半乳糖β1连接到4-N-乙酰葡糖胺β1连接到甘露糖α1连接到3）（N-乙酰葡糖胺β1连接到4）甘露糖β1连接到4-N-乙酰葡糖胺β1连接到4（岩藻糖α1连接到6）N-乙酰葡糖胺OT。
