Smith P F, Al-Samarrai T H, Lynn R J
Yale J Biol Med. 1983 Sep-Dec;56(5-6):425-9.
The partial characterization of the structure of the lipoglycan (LG) from Acholeplasma axanthum is added to the previous complete structural analysis of the lipoglycan from A. granularum. The terminal sequence of A. axanthum LG is Glcp(beta 1----2)-Glcp(beta 1----2)-Glcp(beta 1----6)-; of A. granularum Glcp(beta 1----2)-Glcp(alpha 1----4)-Glcp(beta 1----4)-. These specific residues define the major antigenic determinants of the LG as determined by blockage of hemagglutination of LG coated erythrocytes by specific oligosaccharides and binding of radiolabeled LG to specific immunoglobulins. The binding of LG to mammalian cells occurs by an interaction between specific eucaryotic cell receptors and the internal sequence of the oligosaccharide chain of LG. Size and sugar chains of LG rather than fatty acid residues appears to define the binding site on the LG.
来自黄色无胆甾原体的脂多糖（LG）结构的部分特征已补充到先前对颗粒无胆甾原体脂多糖的完整结构分析中。黄色无胆甾原体LG的末端序列为Glcp(β1→2)-Glcp(β1→2)-Glcp(β1→6)-；颗粒无胆甾原体的为Glcp(β1→2)-Glcp(α1→4)-Glcp(β1→4)-。这些特定残基确定了LG的主要抗原决定簇，这是通过特定寡糖对LG包被红细胞血凝的阻断以及放射性标记的LG与特异性免疫球蛋白的结合来确定的。LG与哺乳动物细胞的结合是通过特定真核细胞受体与LG寡糖链内部序列之间的相互作用发生的。LG的大小和糖链而非脂肪酸残基似乎决定了LG上的结合位点。
