背景 为了解糖肽特异性抗体细微特性,本文着重研究人类MN血型系统。F(ab)噬菌体展示技术曾被应用于F(ab)家族构建,其间H-链Fd片段保持不变,L-链则被拖曳。这样形成了2种F(ab):N92和NNA7,分别对N具有低和高的亲和力。尽管它们的L-链序列较短,并具有92％的氨基酸同源性,它们在N-末端及补体决定区3(CDR3)89、91、92位置具有差异并 Background In order to understand the subtle characteristics of glycopeptide-specific antibodies, this article focuses on the human MN blood group system. F (ab) phage display technology has been applied to the F (ab) family of constructs, during which the H-chain Fd fragment remains unchanged and the L-chain is dragged. This resulted in two F (ab): N92 and NNA7, with low and high affinity for N, respectively. Despite their short L-chain sequences and 92% amino acid homology, they differ in the N-terminal and complementarity determining region 3 (CDR3) 89,91,92 positions