Walker M R, Lee J, Jefferis R
Department of Immunology, Medical School, University of Birmingham, U.K.
Biochim Biophys Acta. 1987 Sep 24;915(2):314-20. doi: 10.1016/0167-4838(87)90315-3.
Concanavalin A binding to glycoprotein bands on nitrocellulose blots was used to detect mannose, sorbose, N-acetylgalactosamine and/or glucose residues on 100% (31/31) of human Bence Jones protein light chains, following sodium dodecyl sulphate-polyacrylamide gel electrophoresis. All (20/20) light chains form IgG myeloma proteins and light chains from a preparation of normal polyclonal human IgG were also bound by concanavalin A. The specificity of concanavalin A for glycoproteins was demonstrated by its binding to human Fc fragments and a human monoclonal anti-Rhesus D antibody (REG-A), but not to human albumin pFc' fragments and aglycosylated REG-A derived from cells grown in the presence of the glycosylation inhibitor tunicamycin. These results suggest that all Bence Jones proteins and light chains from myeloma IgG proteins contain mono- or oligosaccharides linked O-glycosidically to serine or threonine residues.
在十二烷基硫酸钠-聚丙烯酰胺凝胶电泳后，使用伴刀豆球蛋白A与硝酸纤维素膜印迹上的糖蛋白条带结合，来检测100%（31/31）的人本周氏蛋白轻链上的甘露糖、山梨糖、N-乙酰半乳糖胺和/或葡萄糖残基。所有（20/20）来自IgG骨髓瘤蛋白的轻链以及来自正常多克隆人IgG制剂的轻链也都能与伴刀豆球蛋白A结合。伴刀豆球蛋白A对糖蛋白的特异性通过其与人Fc片段和人抗Rhesus D单克隆抗体（REG-A）的结合得以证明，但不与人白蛋白pFc'片段以及在糖基化抑制剂衣霉素存在下生长的细胞衍生的去糖基化REG-A结合。这些结果表明，所有本周氏蛋白以及骨髓瘤IgG蛋白的轻链都含有通过O-糖苷键与丝氨酸或苏氨酸残基相连的单糖或寡糖。
