Rao A S, Liao J, Kabat E A, Osserman E F, Harboe M, Nimmich W
J Biol Chem. 1984 Jan 25;259(2):1018-26.
Four of six human monoclonal IgM proteins were found to react best with Klebsiella polysaccharides containing 3,4py beta DGal (pyruvic acetalated D-galactopyranose), one with Klebsiella polysaccharides with 4,6pyDGlc; the sixth is uncharacterized. The combining sites of two of these (IgMWEA and IgMNAE) were essentially indistinguishable by quantitative precipitin studies at varying pH and by quantitative precipitin inhibition assays, but the other two differed in specificity of their combining sites from these and from each other. These differences were detected by precipitin inhibition assays with 3,4py beta DGal-containing oligosaccharide alditols, the R and S isomers of methyl 4,6py alpha DGal, the R isomer of methyl 4,6py beta DGal, or the R and S isomers of methyl 4,6py alpha DGlc, and -beta DGlc. In all of these except the S isomer of methyl 4,6pyDGal and R isomer of methyl 4,6pyDGlc, the carboxyl group is axial to the plane of the acetal ring. Their specificity appears to be determined by the nonreducing ends of chains and is considered to be cavity-type.
六种人源单克隆IgM蛋白中有四种与含有3,4-吡喃型β-D-半乳糖（丙酮酸缩醛化的D-吡喃半乳糖）的克雷伯氏菌多糖反应最佳，一种与含有4,6-吡喃型-D-葡萄糖的克雷伯氏菌多糖反应最佳；第六种未作表征。通过在不同pH下进行的定量沉淀素研究以及定量沉淀素抑制试验发现，其中两种（IgMWEA和IgMNAE）的结合位点基本无法区分，但另外两种的结合位点特异性与这两种不同，且彼此也不同。这些差异通过使用含有3,4-吡喃型β-D-半乳糖的低聚糖糖醇、4,6-吡喃型α-D-半乳糖的甲基R和S异构体、4,6-吡喃型β-D-半乳糖的甲基R异构体或4,6-吡喃型α-D-葡萄糖的甲基R和S异构体以及β-D-葡萄糖进行沉淀素抑制试验检测出来。在所有这些物质中，除了4,6-吡喃型-D-半乳糖的S异构体和4,6-吡喃型-D-葡萄糖的R异构体之外，羧基都位于缩醛环平面的轴向。它们的特异性似乎由链的非还原端决定，被认为是腔型的。
