Chapman A, Kornfeld R
J Biol Chem. 1979 Feb 10;254(3):816-23.
The structures of the predominant high mannose oligosaccharides present in a human IgM myeloma protein (Patient Wa) have been determined. The IgM glycopeptides, produced by pronase digestion, were fractionated on DEAE-cellulonalysis shows that glycopeptide I contains Asn, Pro, Ala, Thr, and His and glycopeptide II contains Asn, Val, and Ser, which are the same amino acids found in the sequences around Asn 402 and Asn 563 respectively, to which high mannose oligosaccharides are attached in IgM (Patient Ou) (Putnman, F.W., Florent, G., Paul, C., Shinoda, T., and Shimizu, A. (1973) Science 182, 287-290). The high mannose glycopeptides in IgM (Wa) exhibit heterogeneity in the oligosaccharide portion. Structural analysis of the major oligosaccharides indicates that the simplest structure is: (see article of journal). The larger oligosaccharides present have additional mannose residues linked alpha 1 yields 2 to terminal mannose residues in the above structure. Glycopeptide I contains primarily Man5 and Man6 species, while glycopeptide II contains Man6 and Man8 species. The two Man6 oligosaccharides have different branching patterns.
已确定人IgM骨髓瘤蛋白（患者Wa）中主要高甘露糖寡糖的结构。经链霉蛋白酶消化产生的IgM糖肽在DEAE - 纤维素上进行分级分离。分析表明，糖肽I含有天冬酰胺、脯氨酸、丙氨酸、苏氨酸和组氨酸，糖肽II含有天冬酰胺、缬氨酸和丝氨酸，这些分别是在IgM（患者Ou）中与高甘露糖寡糖相连的天冬酰胺402和天冬酰胺563周围序列中发现的相同氨基酸（Putnman, F.W., Florent, G., Paul, C., Shinoda, T., and Shimizu, A. (1973) Science 182, 287 - 290）。IgM（Wa）中的高甘露糖糖肽在寡糖部分表现出异质性。主要寡糖的结构分析表明，最简单的结构是：（见期刊文章）。存在的较大寡糖在上述结构中具有连接到末端甘露糖残基的额外以α1→2连接的甘露糖残基。糖肽I主要含有Man5和Man6种类，而糖肽II含有Man6和Man8种类。两种Man6寡糖具有不同的分支模式。
