Avalle B, Thomas D, Friboulet A
Laboratoire de Technologie Enzymatique-UPRES-A CNRS 6022, Université de Technologie de Compiègne, France.
FASEB J. 1998 Aug;12(11):1055-60. doi: 10.1096/fasebj.12.11.1055.
Antigen mimicry by anti-idiotypic antibodies is investigated as a reliable strategy to achieve molecular imprinting of an enzymatic activity. A monoclonal anti-idiotypic antibody (Ab2-9G4H9) was elicited by using a monoclonal antibody (Ab1-7AF9) specific for the beta-lactamase active site. Catalytic features of Ab2 were characterized with beta-lactamase substrates. The antibody combining site appeared to have retained a part of the catalytic specificity. The relevance of the idiotypic mimicry concept for the generation of catalytic antibodies was further demonstrated by eliciting a third generation antibody (Ab3), which was shown to recognize beta-lactamase: the complete internal image properties of Ab2 9G4H9, including binding and catalytic properties, were thus checked.
抗独特型抗体的抗原模拟作为一种实现酶活性分子印迹的可靠策略受到了研究。通过使用针对β-内酰胺酶活性位点的单克隆抗体（Ab1-7AF9）诱导产生了一种单克隆抗独特型抗体（Ab2-9G4H9）。用β-内酰胺酶底物表征了Ab2的催化特性。抗体结合位点似乎保留了部分催化特异性。通过诱导产生第三代抗体（Ab3）进一步证明了独特型模拟概念与催化抗体产生的相关性，结果表明Ab3能识别β-内酰胺酶：由此检验了Ab2 9G4H9完整的内影像特性，包括结合和催化特性。
