Bruyns A M, De Jaeger G, De Neve M, De Wilde C, Van Montagu M, Depicker A
Department of Genetics, Flanders Interuniversity Institute for Biotechnology, Universiteit Gent, Belguim.
FEBS Lett. 1996 May 13;386(1):5-10. doi: 10.1016/0014-5793(96)00372-9.
A gene encoding a single-chain variable (scFv) antibody fragment was expressed as a cytoplasmic and endoplasmic reticulum-targeted protein in transgenic tobacco plants. In both cases, the scFv accumulated up to 0.01% of total soluble protein (TSP). The same scFv fragment was also produced in the periplasm of Escherichia coli. Measurement of the affinity by ELISA indicates that the affinity of the bacterially made scFv is about 80-fold lower than that of the parental Fab fragment. The results suggest that the affinity of the plant-produced scFv fragments is reduced to a similar extent, implying that all the plant-produced scFv fragments are antigen binding.
一个编码单链可变区（scFv）抗体片段的基因在转基因烟草植株中表达为一种定位于细胞质和内质网的蛋白质。在这两种情况下，scFv的积累量均达到总可溶性蛋白（TSP）的0.01%。相同的scFv片段也在大肠杆菌的周质中产生。通过酶联免疫吸附测定（ELISA）对亲和力的测量表明，细菌产生的scFv的亲和力比亲本Fab片段低约80倍。结果表明，植物产生的scFv片段亲和力降低到了类似程度，这意味着所有植物产生的scFv片段都具有抗原结合能力。
