Lefranc G, Lefranc M P
Laboratoire d'Immunogénétique Moléculaire, URA CNRS 1191, Université Montpellier II Sciences, France.
Biochimie. 1990 Sep;72(9):639-51. doi: 10.1016/0300-9084(90)90046-j.
Techniques of genetic engineering, homologous recombination, and gene transfection make it feasible to produce antigen-binding molecules with widely varying structures. Novel proteins which possess the binding specificity of antibody associated with sequences such as an enzyme or toxin have potential use in immunoassays, in imaging, in immunotherapy. Antibody fusion proteins can also be used as a means to purify proteins or to study the function of surface protooncogenes. This paper reviews the recent data on the obtention and utilisation of the genetically engineered antibody molecules, as well as the approach which consists on the expression in vitro, in Escherichia coli, of a practically unlimited repertoire of Fab fragments and antibody sites.
基因工程、同源重组和基因转染技术使得生产具有广泛不同结构的抗原结合分子成为可能。具有与诸如酶或毒素等序列相关的抗体结合特异性的新型蛋白质在免疫测定、成像、免疫治疗中具有潜在用途。抗体融合蛋白也可用作纯化蛋白质或研究表面原癌基因功能的手段。本文综述了关于基因工程抗体分子的获得和利用的最新数据，以及在大肠杆菌中体外表达几乎无限的Fab片段和抗体位点库的方法。
