Storch M J, Licht T, Petersen K G, Obermeier R, Kerp L
Diabetes. 1987 Sep;36(9):1005-9. doi: 10.2337/diab.36.9.1005.
To define the specificity and epitope of five monoclonal antibodies (MoAbs) to human insulin, binding studies with artificially modified insulins and a number of native insulins were done. Epitopes on the A-chain (A4, A8-A10) and on the end of the B-chain (B30) could be identified. For two MoAbs, substructures of the amino acid B30 were found, which were essential for binding (hydroxyl and methyl groups of B30). In contrast to most antisera, MoAbs to human insulin show high specificity. However, as the study shows, the specificity is not absolute. With suitable artificial epitope modifications, cross-reaction can be seen. Two of the MoAbs used here show sufficient specificity to discriminate between insulin and proinsulin.
为确定5种抗人胰岛素单克隆抗体(MoAb)的特异性和表位,开展了人工修饰胰岛素和多种天然胰岛素的结合研究。可识别A链(A4、A8 - A10)以及B链末端(B30)上的表位。对于两种单克隆抗体,发现了B30氨基酸的亚结构,这些亚结构对结合至关重要(B30的羟基和甲基)。与大多数抗血清不同,抗人胰岛素单克隆抗体具有高度特异性。然而,如该研究所显示,这种特异性并非绝对。通过合适的人工表位修饰,可观察到交叉反应。此处使用的两种单克隆抗体具有足够的特异性,可区分胰岛素和胰岛素原。